Fuzzy Complex Formation between the Intrinsically Disordered Prothymosin α and the Kelch Domain of Keap1 Involved in the Oxidative Stress Response
Kelch-like ECH-associated protein 1 (Keap1) is an inhibitor of nuclear factor erythroid 2-related factor 2 (Nrf2), a key transcription factor for cytoprotective gene activation in the oxidative stress response. Under unstressed conditions, Keap1 interacts with Nrf2 in the cytoplasm via its Kelch dom...
Saved in:
Published in | Journal of molecular biology Vol. 425; no. 6; pp. 1011 - 1027 |
---|---|
Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
England
Elsevier Ltd
25.03.2013
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Kelch-like ECH-associated protein 1 (Keap1) is an inhibitor of nuclear factor erythroid 2-related factor 2 (Nrf2), a key transcription factor for cytoprotective gene activation in the oxidative stress response. Under unstressed conditions, Keap1 interacts with Nrf2 in the cytoplasm via its Kelch domain and suppresses the transcriptional activity of Nrf2. During oxidative stress, Nrf2 is released from Keap1 and is translocated into the nucleus, where it interacts with the small Maf protein to initiate gene transcription. Prothymosin α (ProTα), an intrinsically disordered protein, also interacts with the Kelch domain of Keap1 and mediates the import of Keap1 into the nucleus to inhibit Nrf2 activity. To gain a molecular basis understanding of the oxidative stress response mechanism, we have characterized the interaction between ProTα and the Kelch domain of Keap1 by using nuclear magnetic resonance spectroscopy, isothermal titration calorimetry, peptide array analysis, site-directed mutagenesis, and molecular dynamic simulations. The results of nuclear magnetic resonance chemical shift mapping, amide hydrogen exchange, and spin relaxation measurements revealed that ProTα retains a high level of flexibility, even in the bound state with Kelch. This finding is in agreement with the observations from the molecular dynamic simulations of the ProTα–Kelch complex. Mutational analysis of ProTα, guided by peptide array data and isothermal titration calorimetry, further pinpointed that the region 38NANEENGE45 of ProTα is crucial for the interaction with the Kelch domain, while the flanking residues play relatively minor roles in the affinity of binding.
[Display omitted]
► The mechanism of binding of ProTα with the Kelch domain of Keap1 was studied. ► Results revealed fuzzy complex formation between ProTα and Kelch. ► The 38NANEENGE45 region in ProTα is crucial for interaction with the Kelch domain. ► New insight into how ProTα interacts with the Kelch domain is gained. |
---|---|
AbstractList | Kelch-like ECH-associated protein 1 (Keap1) is an inhibitor of nuclear factor erythroid 2-related factor 2 (Nrf2), a key transcription factor for cytoprotective gene activation in the oxidative stress response. Under unstressed conditions, Keap1 interacts with Nrf2 in the cytoplasm via its Kelch domain and suppresses the transcriptional activity of Nrf2. During oxidative stress, Nrf2 is released from Keap1 and is translocated into the nucleus, where it interacts with the small Maf protein to initiate gene transcription. Prothymosin α (ProTα), an intrinsically disordered protein, also interacts with the Kelch domain of Keap1 and mediates the import of Keap1 into the nucleus to inhibit Nrf2 activity. To gain a molecular basis understanding of the oxidative stress response mechanism, we have characterized the interaction between ProTα and the Kelch domain of Keap1 by using nuclear magnetic resonance spectroscopy, isothermal titration calorimetry, peptide array analysis, site-directed mutagenesis, and molecular dynamic simulations. The results of nuclear magnetic resonance chemical shift mapping, amide hydrogen exchange, and spin relaxation measurements revealed that ProTα retains a high level of flexibility, even in the bound state with Kelch. This finding is in agreement with the observations from the molecular dynamic simulations of the ProTα–Kelch complex. Mutational analysis of ProTα, guided by peptide array data and isothermal titration calorimetry, further pinpointed that the region 38NANEENGE45 of ProTα is crucial for the interaction with the Kelch domain, while the flanking residues play relatively minor roles in the affinity of binding.
[Display omitted]
► The mechanism of binding of ProTα with the Kelch domain of Keap1 was studied. ► Results revealed fuzzy complex formation between ProTα and Kelch. ► The 38NANEENGE45 region in ProTα is crucial for interaction with the Kelch domain. ► New insight into how ProTα interacts with the Kelch domain is gained. Kelch-like ECH-associated protein 1 (Keap1) is an inhibitor of nuclear factor erythroid 2-related factor 2 (Nrf2), a key transcription factor for cytoprotective gene activation in the oxidative stress response. Under unstressed conditions, Keap1 interacts with Nrf2 in the cytoplasm via its Kelch domain and suppresses the transcriptional activity of Nrf2. During oxidative stress, Nrf2 is released from Keap1 and is translocated into the nucleus, where it interacts with the small Maf protein to initiate gene transcription. Prothymosin α (ProTα), an intrinsically disordered protein, also interacts with the Kelch domain of Keap1 and mediates the import of Keap1 into the nucleus to inhibit Nrf2 activity. To gain a molecular basis understanding of the oxidative stress response mechanism, we have characterized the interaction between ProTα and the Kelch domain of Keap1 by using nuclear magnetic resonance spectroscopy, isothermal titration calorimetry, peptide array analysis, site-directed mutagenesis, and molecular dynamic simulations. The results of nuclear magnetic resonance chemical shift mapping, amide hydrogen exchange, and spin relaxation measurements revealed that ProTα retains a high level of flexibility, even in the bound state with Kelch. This finding is in agreement with the observations from the molecular dynamic simulations of the ProTα–Kelch complex. Mutational analysis of ProTα, guided by peptide array data and isothermal titration calorimetry, further pinpointed that the region ³⁸NANEENGE⁴⁵ of ProTα is crucial for the interaction with the Kelch domain, while the flanking residues play relatively minor roles in the affinity of binding. Kelch-like ECH-associated protein 1 (Keap1) is an inhibitor of nuclear factor erythroid 2-related factor 2 (Nrf2), a key transcription factor for cytoprotective gene activation in the oxidative stress response. Under unstressed conditions, Keap1 interacts with Nrf2 in the cytoplasm via its Kelch domain and suppresses the transcriptional activity of Nrf2. During oxidative stress, Nrf2 is released from Keap1 and is translocated into the nucleus, where it interacts with the small Maf protein to initiate gene transcription. Prothymosin α (ProTα), an intrinsically disordered protein, also interacts with the Kelch domain of Keap1 and mediates the import of Keap1 into the nucleus to inhibit Nrf2 activity. To gain a molecular basis understanding of the oxidative stress response mechanism, we have characterized the interaction between ProTα and the Kelch domain of Keap1 by using nuclear magnetic resonance spectroscopy, isothermal titration calorimetry, peptide array analysis, site-directed mutagenesis, and molecular dynamic simulations. The results of nuclear magnetic resonance chemical shift mapping, amide hydrogen exchange, and spin relaxation measurements revealed that ProTα retains a high level of flexibility, even in the bound state with Kelch. This finding is in agreement with the observations from the molecular dynamic simulations of the ProTα-Kelch complex. Mutational analysis of ProTα, guided by peptide array data and isothermal titration calorimetry, further pinpointed that the region (38)NANEENGE(45) of ProTα is crucial for the interaction with the Kelch domain, while the flanking residues play relatively minor roles in the affinity of binding. |
Author | Brickenden, Anne Choy, Wing-Yiu Cino, Elio A. Khan, Halema Fan, Jingsong Yang, Daiwen |
Author_xml | – sequence: 1 givenname: Halema surname: Khan fullname: Khan, Halema organization: Department of Biochemistry, The University of Western Ontario, London, Ontario, Canada N6A 5C1 – sequence: 2 givenname: Elio A. surname: Cino fullname: Cino, Elio A. organization: Department of Biochemistry, The University of Western Ontario, London, Ontario, Canada N6A 5C1 – sequence: 3 givenname: Anne surname: Brickenden fullname: Brickenden, Anne organization: Department of Biochemistry, The University of Western Ontario, London, Ontario, Canada N6A 5C1 – sequence: 4 givenname: Jingsong surname: Fan fullname: Fan, Jingsong organization: Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543, Republic of Singapore – sequence: 5 givenname: Daiwen surname: Yang fullname: Yang, Daiwen organization: Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543, Republic of Singapore – sequence: 6 givenname: Wing-Yiu surname: Choy fullname: Choy, Wing-Yiu email: jchoy4@uwo.ca organization: Department of Biochemistry, The University of Western Ontario, London, Ontario, Canada N6A 5C1 |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/23318954$$D View this record in MEDLINE/PubMed |
BookMark | eNp9kF1u1DAURi3Uik4HFsALeAMJ_kviiCc0ZWhFpSJKny0nvmE8SuzITqedboOVsJGuCQ8pfeyTda3zfdc-p-jIeQcIvaMkp4SWH7f5dmhyRijPCc0JKV6hBSWyzmTJ5RFaEMJYxiQvT9BpjFuSCC7ka3TCOKeyLsQC_V7fPjzs8coPYw_3eO3DoCfrHW5gugNweNoAvnBTsC7aVvf9Hp_Z6IOBAAZ_D37a7AcfrcOPf7B25h__Dfp2g8_8oNO979KsR5padr7fpZSdW6_urUm7doCvpwAx4h8QR-8ivEHHne4jvH06l-hm_eXn6jy7vPp6sfp8mbWCkSnjpBaSNiUHplkthDBSUtEKgJp1TSWIMRXVTVnyqmirWlSN5AXIklFZdEVd8CWic28bfIwBOjUGO-iwV5Sog2C1VUmwOghWhKqDviV6P2fG22YA85z4bzQBH2ag017pX8FGdXOdGopkXxQ1IYn4NBOQ_razEFRsLbgWjA3QTsp4-8ID_gIXWphk |
CitedBy_id | crossref_primary_10_1021_jp407536p crossref_primary_10_4161_idp_25496 crossref_primary_10_1038_nature25762 crossref_primary_10_1111_cas_13963 crossref_primary_10_1073_pnas_1619932114 crossref_primary_10_3389_fmolb_2021_794646 crossref_primary_10_1021_acs_jctc_5b00868 crossref_primary_10_1155_2020_8076105 crossref_primary_10_1042_BJ20140761 crossref_primary_10_1186_s13765_020_00545_7 crossref_primary_10_1021_acs_jpcb_8b03295 crossref_primary_10_1021_acs_jmedchem_9b01865 crossref_primary_10_1021_acs_jproteome_6b00101 crossref_primary_10_1038_s41598_020_58320_z crossref_primary_10_1016_j_jtbi_2015_08_009 crossref_primary_10_1016_j_toxlet_2017_11_031 crossref_primary_10_3390_ijms22147434 crossref_primary_10_1021_ac4039306 crossref_primary_10_1089_jmf_2018_4377 crossref_primary_10_1021_acs_jcim_9b00920 crossref_primary_10_1016_j_bbagen_2018_03_009 crossref_primary_10_1242_dmm_049258 crossref_primary_10_1371_journal_pone_0108217 crossref_primary_10_1016_j_febslet_2015_07_022 crossref_primary_10_1007_s10571_020_00950_y crossref_primary_10_1042_BSR20140149 crossref_primary_10_1016_j_bbapap_2019_07_005 crossref_primary_10_1016_j_freeradbiomed_2020_03_023 crossref_primary_10_3390_ijms23094591 crossref_primary_10_1021_bi501460a crossref_primary_10_1016_j_jmb_2018_02_015 crossref_primary_10_3389_fnagi_2021_673205 crossref_primary_10_1371_journal_pone_0078101 |
Cites_doi | 10.1093/embo-reports/kvf071 10.1002/jcb.22353 10.1016/j.taap.2009.06.009 10.1002/prot.1107 10.1073/pnas.0508955103 10.1196/annals.1415.043 10.1063/1.328693 10.1063/1.464397 10.1007/BF00211777 10.1073/pnas.90.20.9504 10.1073/pnas.88.1.253 10.1128/MCB.26.8.2887-2900.2006 10.1002/prot.340170110 10.1021/bi9002277 10.1128/MCB.25.3.1089-1099.2005 10.1021/bi7014822 10.1002/(SICI)1096-987X(199709)18:12<1463::AID-JCC4>3.0.CO;2-H 10.1073/pnas.93.25.14960 10.1111/j.1432-1033.1995.048_1.x 10.1038/sj.cdd.4400450 10.1016/j.jmb.2007.07.004 10.1128/MCB.00248-10 10.1016/j.urology.2008.05.031 10.1016/j.chemphyslip.2003.09.012 10.1107/S0907444904024825 10.1038/755 10.1074/jbc.272.42.26394 10.1177/002215540004801005 10.1016/j.freeradbiomed.2004.02.075 10.1021/bi00151a027 10.1006/jmbi.1999.3110 10.1007/s10858-011-9549-6 10.1002/prot.340170303 10.1021/ct700301q 10.1371/journal.pone.0027371 10.1007/s11883-005-0013-5 10.1016/j.str.2003.11.023 10.1016/S0014-5793(00)01139-X 10.1038/sj.emboj.7601243 10.1007/BF00239545 10.1074/jbc.M406139200 10.1126/science.1076807 10.1002/prot.340170111 10.1002/jcc.20090 10.1517/17460441.2012.686489 10.1007/s00249-004-0448-6 10.1016/j.tibtech.2006.07.005 10.1038/nprot.2007.406 10.1016/j.bbapap.2010.01.011 10.1016/S0959-8049(05)80433-2 10.1093/bioinformatics/btn195 10.1128/MCB.24.16.7130-7139.2004 10.1016/0167-4838(96)00072-6 10.1016/j.pep.2007.09.005 10.1016/0003-9861(86)90717-4 10.1007/978-1-4614-0659-4_1 10.1107/S1744309108004995 10.1021/bi00040a037 10.1016/j.jmb.2010.09.044 10.1101/gad.13.1.76 10.1016/S1357-2725(99)00094-1 10.1021/bi9022329 10.1016/j.jmb.2004.03.017 10.1038/nrm1589 10.1083/jcb.200608022 10.1073/pnas.0914870107 10.1110/ps.9.1.10 10.1021/ja900616b 10.1007/BF00197809 10.1016/j.febslet.2004.09.091 10.1006/bbrc.1999.2013 10.1038/sj.cdd.4401282 10.1016/j.molcel.2006.01.013 10.1038/labinvest.3700385 10.1021/ct300323g 10.1093/nar/26.13.3111 10.1016/j.sbi.2008.12.003 10.1038/cdd.2008.159 10.1021/bi990752+ 10.1073/pnas.0809222105 10.1038/nature05858 10.1146/annurev.pharmtox.45.120403.100010 10.1074/jbc.M410175200 10.1074/jbc.M808084200 10.1002/pro.5560031206 10.1016/0014-5793(94)00439-0 10.1093/bioinformatics/btp518 10.3390/ijms12053205 10.1110/ps.062465306 10.1016/S0014-5793(97)00824-7 10.1042/bj3310753 10.1039/C1MB05234A 10.1093/bioinformatics/bts209 10.1016/j.sbi.2005.01.002 10.1128/JVI.76.10.4699-4708.2002 10.1002/prot.340140210 10.1063/1.2408420 10.1016/j.jmb.2006.01.100 10.1515/BC.2006.164 10.1038/ncb2021 10.1073/pnas.81.4.1008 10.1006/bbrc.1997.6943 10.1016/S1054-3589(08)60989-8 |
ContentType | Journal Article |
Copyright | 2013 Elsevier Ltd Copyright © 2013 Elsevier Ltd. All rights reserved. |
Copyright_xml | – notice: 2013 Elsevier Ltd – notice: Copyright © 2013 Elsevier Ltd. All rights reserved. |
DBID | FBQ CGR CUY CVF ECM EIF NPM AAYXX CITATION |
DOI | 10.1016/j.jmb.2013.01.005 |
DatabaseName | AGRIS Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef |
DatabaseTitleList | MEDLINE |
Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database – sequence: 3 dbid: FBQ name: AGRIS url: http://www.fao.org/agris/Centre.asp?Menu_1ID=DB&Menu_2ID=DB1&Language=EN&Content=http://www.fao.org/agris/search?Language=EN sourceTypes: Publisher |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Chemistry Biology |
EISSN | 1089-8638 |
EndPage | 1027 |
ExternalDocumentID | 10_1016_j_jmb_2013_01_005 23318954 US201500045900 S0022283613000089 |
Genre | Research Support, Non-U.S. Gov't Journal Article |
GrantInformation_xml | – fundername: Canadian Institutes of Health Research grantid: MOP no. 74679 |
GroupedDBID | --- --K --M -DZ -ET -~X .~1 0R~ 186 1B1 1RT 1~. 1~5 4.4 457 4G. 53G 5GY 5RE 5VS 7-5 71M 85S 8P~ 9JM AAAJQ AABNK AACTN AAEDT AAEDW AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AARKO AAXUO ABFNM ABFRF ABGSF ABJNI ABLJU ABMAC ABOCM ABPPZ ABUDA ABXDB ABYKQ ACDAQ ACGFO ACGFS ACNCT ACRLP ADBBV ADEZE ADUVX AEBSH AEFWE AEHWI AEKER AENEX AFFNX AFKWA AFTJW AFXIZ AGEKW AGUBO AGYEJ AHHHB AIEXJ AIKHN AITUG AJBFU AJOXV ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ AXJTR BKOJK BLXMC CJTIS CS3 DM4 DOVZS DU5 EBS EFBJH EFLBG EJD EO8 EO9 EP2 EP3 F5P FDB FIRID FNPLU FYGXN G-Q GBLVA GX1 HLW HMG IH2 IHE J1W K-O KOM LG5 LUGTX LX2 LZ5 M41 MO0 N9A O-L O9- OAUVE OZT P-8 P-9 P2P PC. Q38 RIG RNS ROL RPZ SDF SDG SDP SES SPCBC SSI SSU SSZ T5K TWZ VQA WH7 XPP YQT ZMT ZU3 ~G- .55 .GJ 29L 3O- AAQXK ABEFU ABPIF ABPTK ACKIV ADFGL ADIYS ADMUD AEQTP AFMIJ AGHFR AGRDE AI. ASPBG AVWKF AZFZN CAG COF FBQ FEDTE FGOYB G-2 G8K HVGLF HX~ HZ~ H~9 MVM NEJ R2- SBG SEW SIN UQL VH1 WUQ X7M XJT XOL Y6R YYP ZGI ZKB ~KM AKRWK CGR CUY CVF ECM EIF NPM 0SF AAHBH AAXKI AAYXX ADVLN CITATION |
ID | FETCH-LOGICAL-c420t-309481b63e2a29444d8814c4ee92fb740dd71ab66375c7947b835e862185f5953 |
IEDL.DBID | .~1 |
ISSN | 0022-2836 |
IngestDate | Thu Sep 12 16:53:58 EDT 2024 Thu May 23 23:16:25 EDT 2024 Wed Dec 27 19:28:32 EST 2023 Fri Feb 23 02:26:03 EST 2024 |
IsDoiOpenAccess | false |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 6 |
Keywords | NOE protein dynamics protein–protein interaction molecular dynamic simulation nuclear magnetic resonance PDB HX SSP isothermal titration calorimetry IDP Nrf2 ProTα MD Keap1 ITC HSQC |
Language | English |
License | Copyright © 2013 Elsevier Ltd. All rights reserved. |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c420t-309481b63e2a29444d8814c4ee92fb740dd71ab66375c7947b835e862185f5953 |
Notes | http://dx.doi.org/10.1016/j.jmb.2013.01.005 |
OpenAccessLink | https://ir.lib.uwo.ca/cgi/viewcontent.cgi?article=1156&context=biochempub |
PMID | 23318954 |
PageCount | 17 |
ParticipantIDs | crossref_primary_10_1016_j_jmb_2013_01_005 pubmed_primary_23318954 fao_agris_US201500045900 elsevier_sciencedirect_doi_10_1016_j_jmb_2013_01_005 |
PublicationCentury | 2000 |
PublicationDate | 2013-03-25 |
PublicationDateYYYYMMDD | 2013-03-25 |
PublicationDate_xml | – month: 03 year: 2013 text: 2013-03-25 day: 25 |
PublicationDecade | 2010 |
PublicationPlace | England |
PublicationPlace_xml | – name: England |
PublicationTitle | Journal of molecular biology |
PublicationTitleAlternate | J Mol Biol |
PublicationYear | 2013 |
Publisher | Elsevier Ltd |
Publisher_xml | – name: Elsevier Ltd |
References | Diaz-Jullien, Perez-Estevez, Covelo, Freire (bb0020) 1996; 1296 Fujita, Ueda, Fujiwara, Ueda (bb0155) 2009; 16 Radford, Buck, Topping, Dobson, Evans (bb0425) 1992; 14 Dyson, Wright (bb0280) 2005; 6 Marsh, Singh, Jia, Forman-Kay (bb0400) 2006; 15 Karetsou, Sandaltzopoulos, Frangou-Lazaridis, Lai, Tsolas, Becker, Papamarcaki (bb0080) 1998; 26 Evstafieva, Belov, Kalkum, Chichkova, Bogdanov, Agol, Vartapetian (bb0075) 2000; 467 Connelly, Bai, Jeng, Englander (bb0475) 1993; 17 Wang, Cao, Zhao, Li (bb0360) 2011; 12 Kay (bb0405) 1998; 5 Wright, Dyson (bb0275) 2009; 19 Fuxreiter, Simon, Friedrich, Tompa (bb0315) 2004; 338 Yi, Boys, Brickenden, Konermann, Choy (bb0050) 2007; 46 Hess, Kutzner, Spoel (bb0485) 2008; 4 Komatsu, Kurokawa, Waguri, Taguchi, Kobayashi, Ichimura (bb0440) 2010; 12 Uversky, Gillespie, Millett, Khodyakova, Vasilenko, Vasiliev (bb0055) 2000; 267 In press. Kim, Guengerich (bb0205) 2005; 45 Mittag, Orlicky, Choy, Tang, Lin, Sicheri (bb0455) 2008; 105 Fuxreiter, Tompa (bb0340) 2012; 725 Mosoian, Teixeira, Burns, Sander, Gusella, He (bb0145) 2010; 107 Traub, Jost, Hess, Schorn, Menzel, Budde (bb0170) 2006; 86 Karetsou, Kretsovali, Murphy, Tsolas, Papamarcaki (bb0100) 2002; 3 Kobayashi, Kang, Okawa, Ohtsuji, Zenke, Chiba (bb0240) 2004; 24 Cino, E., Fan, J., Yang, D. & Choy, W. Y. (2012). H Enkemann, Ward, Berger (bb0130) 2000; 48 Primiano, Sutter, Kensler (bb0195) 1997; 38 Ishida, Kinoshita (bb0380) 2008; 24 Padmanabhan, Tong, Ohta, Nakamura, Scharlock, Ohtsuji (bb0270) 2006; 21 Malicet, Giroux, Vasseur, Dagorn, Neira, Iovanna (bb0125) 2006; 103 Niture, Jaiswal (bb0190) 2009; 284 Fan, Lim, Yu, Yang (bb0420) 2011; 51 Sburlati, Manrow, Berger (bb0065) 1991; 88 N and Haritos, Goodall, Horecker (bb0005) 1984; 81 Bai, Milne, Mayne, Englander (bb0480) 1993; 17 Piacentini, Evangelisti, Mastroberardino, Nardacci, Kroemer (bb0120) 2003; 10 Cino, Choy, Karttunen (bb0330) 2012; 8 Papamarcaki, Tsolas (bb0085) 1994; 345 Lo, Li, Henzl, Beamer, Hannink (bb0265) 2006; 25 Gast, Damaschun, Eckert, Schulze-Forster, Maurer, Muller-Frohne (bb0040) 1995; 34 Wishart, Bigam, Yao, Abildgaard, Dyson, Oldfield (bb0460) 1995; 6 Yi, Brickenden, Choy (bb0385) 2008; 57 Rodriguez, Vinuela, Alvarez-Fernandez, Gomez-Marquez (bb0070) 1999; 6 Lau, Wang, Zhao, Villeneuve, Wu, Jiang (bb0450) 2010; 30 Delaglio, Grzesiek, Vuister, Zhu, Pfeifer, Bax (bb0465) 1995; 6 Kim, Fuzery, Tonelli, Ta, Westler, Vickery, Markley (bb0430) 2009; 48 Itoh, Wakabayashi, Katoh, Ishii, Igarashi, Engel, Yamamoto (bb0230) 1999; 13 Karapetian, Evstafieva, Abaeva, Chichkova, Filonov, Rubtsov (bb0185) 2005; 25 Tong, Katoh, Kusunoki, Itoh, Tanaka, Yamamoto (bb0235) 2006; 26 Tsai, Ma, Sham, Kumar, Nussinov (bb0310) 2001; 44 Rubtsov, Zolotukhin, Vorobjev, Chichkova, Pavlov, Karger (bb0035) 1997; 413 Venugopal, Jaiswal (bb0220) 1996; 93 Uversky, Gillespie, Millett, Khodyakova, Vasiliev, Chernovskaya (bb0045) 1999; 38 Dosztanyi, Meszaros, Simon (bb0390) 2009; 25 Padmanabhan, Nakamura, Yokoyama (bb0260) 2008; 64 Johnson (bb0470) 2004; 278 Zhuo, Ilangovan, Schirf, Demeler, Sousa, Hinck, Lafer (bb0345) 2010; 404 Tong, Kobayashi, Katsuoka, Yamamoto (bb0250) 2006; 387 Itoh, Tong, Yamamoto (bb0225) 2004; 36 Cheng, LeGall, Oldfield, Mueller, Van, Romero (bb0365) 2006; 24 Rodriguez, Vinuela, Alvarez-Fernandez, Buceta, Vidal, Dominguez, Gomez-Marquez (bb0060) 1998; 331 Xue, Dunbrack, Williams, Dunker, Uversky (bb0375) 2010; 1804 Schulze, Lee (bb0210) 2005; 7 Niture, Kaspar, Shen, Jaiswal (bb0255) 2010; 244 Disfani, Hsu, Mizianty, Oldfield, Xue, Dunker (bb0395) 2012; 28 Jiang, Kim, Shu, Zhao, Zhang, Kofron (bb0110) 2003; 299 Oostenbrink, Soares, van der Vegt, van Gunsteren (bb0490) 2005; 34 Wright, Dyson (bb0285) 1999; 293 Bordelon, Montegudo, Pakhomova, Oldham, Newcomer (bb0305) 2004; 279 Tsitsiloni, Stiakakis, Koutselinis, Gogas, Markopoulos, Yialouris (bb0180) 1993; 90 Tsai, Jou, Lee, Chen, Shiau, Tsai (bb0165) 2009; 73 Oostenbrink, Villa, Mark, van Gunsteren (bb0495) 2004; 25 Segade, Gomez-Marquez (bb0025) 1999; 31 Peng, Wagner (bb0415) 1992; 31 Kumar, Ma, Tsai, Sinha, Nussinov (bb0320) 2000; 9 Brunger (bb0500) 2007; 2 C backbone resonance assignments of the Kelch domain of mouse Keap1. Martic, Karetsou, Kefala, Politou, Clapier, Straub, Papamarcaki (bb0090) 2005; 280 Cino, Wong-ekkabut, Karttunen, Choy (bb0325) 2011; 6 Itoh, Chiba, Takahashi, Ishii, Igarashi, Katoh (bb0200) 1997; 236 Pratico, Rokach, Lawson, FitzGerald (bb0215) 2004; 128 Subramanian, Hasan, Rowe, Hottiger, Orre, Robertson (bb0105) 2002; 76 Dominguez, Magdalena, Cancio, Roson, Paredes, Loidi (bb0175) 1993; 29A Li, Zhang, Hannink, Beamer (bb0245) 2004; 60 Frillingos, Frangou-Lazaridis, Seferiadis, Hulmes, Pan, Tsolas (bb0010) 1991; 108 Mosoian, Teixeira, Burns, Khitrov, Zhang, Gusella (bb0140) 2007; 1112 Fuxreiter (bb0335) 2012; 8 Meszaros, Tompa, Simon, Dosztanyi (bb0290) 2007; 372 Kubota, Adachi, Copeland, Oroszlan (bb0135) 1995; 233 Pan, Haritos, Wideman, Komiyama, Chang, Stein (bb0015) 1986; 250 Walma, Aelen, Nabuurs, Oostendorp, van den Berk, Hendriks, Vuister (bb0410) 2004; 12 van Ingen, Baltussen, Aelen, Vuister (bb0435) 2006; 358 Hutchinson, Thornton (bb0445) 1994; 3 Karetsou, Martic, Tavoulari, Christoforidis, Wilm, Gruss, Papamarcaki (bb0095) 2004; 577 Fink (bb0295) 2005; 15 Uversky (bb0355) 2012; 7 Ueda, Fujita, Yoshida, Matsunaga, Ueda (bb0150) 2007; 176 Sugase, Dyson, Wright (bb0300) 2007; 447 Hammoudeh, Follis, Prochownik, Metallo (bb0350) 2009; 131 Trumbore, Wang, Enkemann, Berger (bb0030) 1997; 272 Qi, Wang, Du (bb0115) 2010; 49 MacArthur, Thornton (bb0505) 1993; 17 Gou, Tong, Yan, Yuan, He, Wang (bb0160) 2009; 108 Dosztanyi (10.1016/j.jmb.2013.01.005_bb0390) 2009; 25 Mosoian (10.1016/j.jmb.2013.01.005_bb0145) 2010; 107 Tong (10.1016/j.jmb.2013.01.005_bb0235) 2006; 26 Frillingos (10.1016/j.jmb.2013.01.005_bb0010) 1991; 108 Enkemann (10.1016/j.jmb.2013.01.005_bb0130) 2000; 48 Zhuo (10.1016/j.jmb.2013.01.005_bb0345) 2010; 404 Lo (10.1016/j.jmb.2013.01.005_bb0265) 2006; 25 Cino (10.1016/j.jmb.2013.01.005_bb0325) 2011; 6 Cino (10.1016/j.jmb.2013.01.005_bb0330) 2012; 8 Trumbore (10.1016/j.jmb.2013.01.005_bb0030) 1997; 272 Venugopal (10.1016/j.jmb.2013.01.005_bb0220) 1996; 93 Cheng (10.1016/j.jmb.2013.01.005_bb0365) 2006; 24 Kim (10.1016/j.jmb.2013.01.005_bb0430) 2009; 48 Primiano (10.1016/j.jmb.2013.01.005_bb0195) 1997; 38 Schulze (10.1016/j.jmb.2013.01.005_bb0210) 2005; 7 Hutchinson (10.1016/j.jmb.2013.01.005_bb0445) 1994; 3 Bai (10.1016/j.jmb.2013.01.005_bb0480) 1993; 17 Tsai (10.1016/j.jmb.2013.01.005_bb0165) 2009; 73 Uversky (10.1016/j.jmb.2013.01.005_bb0355) 2012; 7 Darden (10.1016/j.jmb.2013.01.005_fr0025) 1993; 98 Rodriguez (10.1016/j.jmb.2013.01.005_bb0070) 1999; 6 Diaz-Jullien (10.1016/j.jmb.2013.01.005_bb0020) 1996; 1296 Wright (10.1016/j.jmb.2013.01.005_bb0275) 2009; 19 Walma (10.1016/j.jmb.2013.01.005_bb0410) 2004; 12 Hess (10.1016/j.jmb.2013.01.005_fr0020) 1997; 18 Komatsu (10.1016/j.jmb.2013.01.005_bb0440) 2010; 12 Hammoudeh (10.1016/j.jmb.2013.01.005_bb0350) 2009; 131 Kubota (10.1016/j.jmb.2013.01.005_bb0135) 1995; 233 Segade (10.1016/j.jmb.2013.01.005_bb0025) 1999; 31 Lau (10.1016/j.jmb.2013.01.005_bb0450) 2010; 30 Uversky (10.1016/j.jmb.2013.01.005_bb0055) 2000; 267 Gast (10.1016/j.jmb.2013.01.005_bb0040) 1995; 34 Malicet (10.1016/j.jmb.2013.01.005_bb0125) 2006; 103 Johnson (10.1016/j.jmb.2013.01.005_bb0470) 2004; 278 Tsai (10.1016/j.jmb.2013.01.005_bb0310) 2001; 44 Peng (10.1016/j.jmb.2013.01.005_bb0415) 1992; 31 Martic (10.1016/j.jmb.2013.01.005_bb0090) 2005; 280 Karetsou (10.1016/j.jmb.2013.01.005_bb0095) 2004; 577 Fuxreiter (10.1016/j.jmb.2013.01.005_bb0315) 2004; 338 Yi (10.1016/j.jmb.2013.01.005_bb0385) 2008; 57 van Ingen (10.1016/j.jmb.2013.01.005_bb0435) 2006; 358 Delaglio (10.1016/j.jmb.2013.01.005_bb0465) 1995; 6 Karapetian (10.1016/j.jmb.2013.01.005_bb0185) 2005; 25 MacArthur (10.1016/j.jmb.2013.01.005_bb0505) 1993; 17 Yi (10.1016/j.jmb.2013.01.005_bb0050) 2007; 46 Disfani (10.1016/j.jmb.2013.01.005_bb0395) 2012; 28 Meszaros (10.1016/j.jmb.2013.01.005_bb0290) 2007; 372 Ueda (10.1016/j.jmb.2013.01.005_bb0150) 2007; 176 Niture (10.1016/j.jmb.2013.01.005_bb0190) 2009; 284 Rodriguez (10.1016/j.jmb.2013.01.005_bb0060) 1998; 331 Itoh (10.1016/j.jmb.2013.01.005_bb0200) 1997; 236 Padmanabhan (10.1016/j.jmb.2013.01.005_bb0260) 2008; 64 Uversky (10.1016/j.jmb.2013.01.005_bb0045) 1999; 38 Brunger (10.1016/j.jmb.2013.01.005_bb0500) 2007; 2 Fuxreiter (10.1016/j.jmb.2013.01.005_bb0335) 2012; 8 Qi (10.1016/j.jmb.2013.01.005_bb0115) 2010; 49 10.1016/j.jmb.2013.01.005_bb0370 Evstafieva (10.1016/j.jmb.2013.01.005_bb0075) 2000; 467 Kay (10.1016/j.jmb.2013.01.005_bb0405) 1998; 5 Pan (10.1016/j.jmb.2013.01.005_bb0015) 1986; 250 Piacentini (10.1016/j.jmb.2013.01.005_bb0120) 2003; 10 Connelly (10.1016/j.jmb.2013.01.005_bb0475) 1993; 17 Wang (10.1016/j.jmb.2013.01.005_bb0360) 2011; 12 Itoh (10.1016/j.jmb.2013.01.005_bb0225) 2004; 36 Hess (10.1016/j.jmb.2013.01.005_bb0485) 2008; 4 Haritos (10.1016/j.jmb.2013.01.005_bb0005) 1984; 81 Gou (10.1016/j.jmb.2013.01.005_bb0160) 2009; 108 Itoh (10.1016/j.jmb.2013.01.005_bb0230) 1999; 13 Karetsou (10.1016/j.jmb.2013.01.005_bb0080) 1998; 26 Tong (10.1016/j.jmb.2013.01.005_bb0250) 2006; 387 Radford (10.1016/j.jmb.2013.01.005_bb0425) 1992; 14 Mosoian (10.1016/j.jmb.2013.01.005_bb0140) 2007; 1112 Dominguez (10.1016/j.jmb.2013.01.005_bb0175) 1993; 29A Oostenbrink (10.1016/j.jmb.2013.01.005_bb0490) 2005; 34 Oostenbrink (10.1016/j.jmb.2013.01.005_bb0495) 2004; 25 Bordelon (10.1016/j.jmb.2013.01.005_bb0305) 2004; 279 Marsh (10.1016/j.jmb.2013.01.005_bb0400) 2006; 15 Parrinello (10.1016/j.jmb.2013.01.005_fr0015) 1981; 52 Fuxreiter (10.1016/j.jmb.2013.01.005_bb0340) 2012; 725 Padmanabhan (10.1016/j.jmb.2013.01.005_bb0270) 2006; 21 Fink (10.1016/j.jmb.2013.01.005_bb0295) 2005; 15 Ishida (10.1016/j.jmb.2013.01.005_bb0380) 2008; 24 Sburlati (10.1016/j.jmb.2013.01.005_bb0065) 1991; 88 Wright (10.1016/j.jmb.2013.01.005_bb0285) 1999; 293 Sugase (10.1016/j.jmb.2013.01.005_bb0300) 2007; 447 Karetsou (10.1016/j.jmb.2013.01.005_bb0100) 2002; 3 Xue (10.1016/j.jmb.2013.01.005_bb0375) 2010; 1804 Pratico (10.1016/j.jmb.2013.01.005_bb0215) 2004; 128 Jiang (10.1016/j.jmb.2013.01.005_bb0110) 2003; 299 Dyson (10.1016/j.jmb.2013.01.005_bb0280) 2005; 6 Wishart (10.1016/j.jmb.2013.01.005_bb0460) 1995; 6 Li (10.1016/j.jmb.2013.01.005_bb0245) 2004; 60 Mittag (10.1016/j.jmb.2013.01.005_bb0455) 2008; 105 Kumar (10.1016/j.jmb.2013.01.005_bb0320) 2000; 9 Fan (10.1016/j.jmb.2013.01.005_bb0420) 2011; 51 Tsitsiloni (10.1016/j.jmb.2013.01.005_bb0180) 1993; 90 Bussi (10.1016/j.jmb.2013.01.005_fr0010) 2007; 126 Kobayashi (10.1016/j.jmb.2013.01.005_bb0240) 2004; 24 Kim (10.1016/j.jmb.2013.01.005_bb0205) 2005; 45 Subramanian (10.1016/j.jmb.2013.01.005_bb0105) 2002; 76 Papamarcaki (10.1016/j.jmb.2013.01.005_bb0085) 1994; 345 Traub (10.1016/j.jmb.2013.01.005_bb0170) 2006; 86 Rubtsov (10.1016/j.jmb.2013.01.005_bb0035) 1997; 413 Fujita (10.1016/j.jmb.2013.01.005_bb0155) 2009; 16 Niture (10.1016/j.jmb.2013.01.005_bb0255) 2010; 244 |
References_xml | – volume: 725 start-page: 1 year: 2012 end-page: 14 ident: bb0340 article-title: Fuzzy complexes: a more stochastic view of protein function publication-title: Adv. Exp. Med. Biol. contributor: fullname: Tompa – volume: 81 start-page: 1008 year: 1984 end-page: 1011 ident: bb0005 article-title: Prothymosin alpha: isolation and properties of the major immunoreactive form of thymosin alpha 1 in rat thymus publication-title: Proc. Natl Acad. Sci. USA contributor: fullname: Horecker – volume: 36 start-page: 1208 year: 2004 end-page: 1213 ident: bb0225 article-title: Molecular mechanism activating Nrf2-Keap1 pathway in regulation of adaptive response to electrophiles publication-title: Free Radical Biol. Med. contributor: fullname: Yamamoto – volume: 34 start-page: 13211 year: 1995 end-page: 13218 ident: bb0040 article-title: Prothymosin alpha: a biologically active protein with random coil conformation publication-title: Biochemistry contributor: fullname: Muller-Frohne – volume: 1804 start-page: 996 year: 2010 end-page: 1010 ident: bb0375 article-title: PONDR-FIT: a meta-predictor of intrinsically disordered amino acids publication-title: Biochim. Biophys. Acta contributor: fullname: Uversky – volume: 372 start-page: 549 year: 2007 end-page: 561 ident: bb0290 article-title: Molecular principles of the interactions of disordered proteins publication-title: J. Mol. Biol. contributor: fullname: Dosztanyi – volume: 413 start-page: 135 year: 1997 end-page: 141 ident: bb0035 article-title: Mutational analysis of human prothymosin alpha reveals a bipartite nuclear localization signal publication-title: FEBS Lett. contributor: fullname: Karger – volume: 272 start-page: 26394 year: 1997 end-page: 26404 ident: bb0030 article-title: Prothymosin alpha in vivo contains phosphorylated glutamic acid residues publication-title: J. Biol. Chem. contributor: fullname: Berger – volume: 60 start-page: 2346 year: 2004 end-page: 2348 ident: bb0245 article-title: Crystallization and initial crystallographic analysis of the Kelch domain from human Keap1 publication-title: Acta Crystallogr., Sect. D: Biol. Crystallogr. contributor: fullname: Beamer – volume: 278 start-page: 313 year: 2004 end-page: 352 ident: bb0470 article-title: Using NMRView to visualize and analyze the NMR spectra of macromolecules publication-title: Methods Mol. Biol. contributor: fullname: Johnson – volume: 12 start-page: 3205 year: 2011 end-page: 3219 ident: bb0360 article-title: Novel strategies for drug discovery based on intrinsically disordered proteins (IDPs) publication-title: Int. J. Mol. Sci. contributor: fullname: Li – volume: 17 start-page: 232 year: 1993 end-page: 251 ident: bb0505 article-title: Conformational analysis of protein structures derived from NMR data publication-title: Proteins contributor: fullname: Thornton – volume: 131 start-page: 7390 year: 2009 end-page: 7401 ident: bb0350 article-title: Multiple independent binding sites for small-molecule inhibitors on the oncoprotein c-Myc publication-title: J. Am. Chem. Soc. contributor: fullname: Metallo – volume: 244 start-page: 37 year: 2010 end-page: 42 ident: bb0255 article-title: Nrf2 signaling and cell survival publication-title: Toxicol. Appl. Pharmacol. contributor: fullname: Jaiswal – volume: 45 start-page: 27 year: 2005 end-page: 49 ident: bb0205 article-title: Cytochrome P450 activation of arylamines and heterocyclic amines publication-title: Annu. Rev. Pharmacol. Toxicol. contributor: fullname: Guengerich – volume: 29A start-page: 893 year: 1993 end-page: 897 ident: bb0175 article-title: Tissue concentrations of prothymosin alpha: a novel proliferation index of primary breast cancer publication-title: Eur. J. Cancer contributor: fullname: Loidi – volume: 280 start-page: 16143 year: 2005 end-page: 16150 ident: bb0090 article-title: Parathymosin affects the binding of linker histone H1 to nucleosomes and remodels chromatin structure publication-title: J. Biol. Chem. contributor: fullname: Papamarcaki – volume: 17 start-page: 75 year: 1993 end-page: 86 ident: bb0480 article-title: Primary structure effects on peptide group hydrogen exchange publication-title: Proteins contributor: fullname: Englander – volume: 6 start-page: 135 year: 1995 end-page: 140 ident: bb0460 article-title: H, publication-title: J. Biomol. NMR contributor: fullname: Oldfield – volume: 25 start-page: 1089 year: 2005 end-page: 1099 ident: bb0185 article-title: Nuclear oncoprotein prothymosin alpha is a partner of Keap1: implications for expression of oxidative stress-protecting genes publication-title: Mol. Cell. Biol. contributor: fullname: Rubtsov – volume: 9 start-page: 10 year: 2000 end-page: 19 ident: bb0320 article-title: Folding and binding cascades: dynamic landscapes and population shifts publication-title: Protein Sci. contributor: fullname: Nussinov – volume: 299 start-page: 223 year: 2003 end-page: 226 ident: bb0110 article-title: Distinctive roles of PHAP proteins and prothymosin-alpha in a death regulatory pathway publication-title: Science contributor: fullname: Kofron – volume: 1112 start-page: 269 year: 2007 end-page: 285 ident: bb0140 article-title: Influence of prothymosin-alpha on HIV-1 target cells publication-title: Ann. N. Y. Acad. Sci. contributor: fullname: Gusella – volume: 8 start-page: 168 year: 2012 end-page: 177 ident: bb0335 article-title: Fuzziness: linking regulation to protein dynamics publication-title: Mol. BioSyst. contributor: fullname: Fuxreiter – volume: 250 start-page: 197 year: 1986 end-page: 201 ident: bb0015 article-title: Human prothymosin alpha: amino acid sequence and immunologic properties publication-title: Arch. Biochem. Biophys. contributor: fullname: Stein – volume: 86 start-page: 246 year: 2006 end-page: 253 ident: bb0170 article-title: Peptidomic analysis of breast cancer reveals a putative surrogate marker for estrogen receptor-negative carcinomas publication-title: Lab. Invest. contributor: fullname: Budde – volume: 577 start-page: 496 year: 2004 end-page: 500 ident: bb0095 article-title: Prothymosin alpha associates with the oncoprotein SET and is involved in chromatin decondensation publication-title: FEBS Lett. contributor: fullname: Papamarcaki – volume: 38 start-page: 15009 year: 1999 end-page: 15016 ident: bb0045 article-title: Natively unfolded human prothymosin alpha adopts partially folded collapsed conformation at acidic pH publication-title: Biochemistry contributor: fullname: Chernovskaya – volume: 16 start-page: 349 year: 2009 end-page: 358 ident: bb0155 article-title: Prothymosin-alpha plays a defensive role in retinal ischemia through necrosis and apoptosis inhibition publication-title: Cell Death Differ. contributor: fullname: Ueda – volume: 103 start-page: 2671 year: 2006 end-page: 2676 ident: bb0125 article-title: Regulation of apoptosis by the p8/prothymosin alpha complex publication-title: Proc. Natl Acad. Sci. USA contributor: fullname: Iovanna – volume: 467 start-page: 150 year: 2000 end-page: 154 ident: bb0075 article-title: Prothymosin alpha fragmentation in apoptosis publication-title: FEBS Lett. contributor: fullname: Vartapetian – volume: 19 start-page: 31 year: 2009 end-page: 38 ident: bb0275 article-title: Linking folding and binding publication-title: Curr. Opin. Struct. Biol. contributor: fullname: Dyson – volume: 24 start-page: 435 year: 2006 end-page: 442 ident: bb0365 article-title: Rational drug design via intrinsically disordered protein publication-title: Trends Biotechnol. contributor: fullname: Romero – volume: 236 start-page: 313 year: 1997 end-page: 322 ident: bb0200 article-title: An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements publication-title: Biochem. Biophys. Res. Commun. contributor: fullname: Katoh – volume: 6 start-page: 197 year: 2005 end-page: 208 ident: bb0280 article-title: Intrinsically unstructured proteins and their functions publication-title: Nat. Rev., Mol. Cell Biol. contributor: fullname: Wright – volume: 12 start-page: 11 year: 2004 end-page: 20 ident: bb0410 article-title: A closed binding pocket and global destabilization modify the binding properties of an alternatively spliced form of the second PDZ domain of PTP-BL publication-title: Structure contributor: fullname: Vuister – volume: 293 start-page: 321 year: 1999 end-page: 331 ident: bb0285 article-title: Intrinsically unstructured proteins: re-assessing the protein structure–function paradigm publication-title: J. Mol. Biol. contributor: fullname: Dyson – volume: 14 start-page: 237 year: 1992 end-page: 248 ident: bb0425 article-title: Hydrogen exchange in native and denatured states of hen egg-white lysozyme publication-title: Proteins contributor: fullname: Evans – volume: 2 start-page: 2728 year: 2007 end-page: 2733 ident: bb0500 article-title: Version 1.2 of the Crystallography and NMR system publication-title: Nat. Protoc. contributor: fullname: Brunger – volume: 76 start-page: 4699 year: 2002 end-page: 4708 ident: bb0105 article-title: Epstein-Barr virus nuclear antigen 3C and prothymosin alpha interact with the p300 transcriptional coactivator at the CH1 and CH3/HAT domains and cooperate in regulation of transcription and histone acetylation publication-title: J. Virol. contributor: fullname: Robertson – volume: 88 start-page: 253 year: 1991 end-page: 257 ident: bb0065 article-title: Prothymosin alpha antisense oligomers inhibit myeloma cell division publication-title: Proc. Natl Acad. Sci. USA contributor: fullname: Berger – volume: 34 start-page: 273 year: 2005 end-page: 284 ident: bb0490 article-title: Validation of the 53A6 GROMOS force field publication-title: Eur. Biophys. J. contributor: fullname: van Gunsteren – volume: 57 start-page: 1 year: 2008 end-page: 8 ident: bb0385 article-title: A new protocol for high-yield purification of recombinant human prothymosin alpha expressed in publication-title: Protein Expression Purif. contributor: fullname: Choy – volume: 345 start-page: 71 year: 1994 end-page: 75 ident: bb0085 article-title: Prothymosin alpha binds to histone H1 in vitro publication-title: FEBS Lett. contributor: fullname: Tsolas – volume: 233 start-page: 48 year: 1995 end-page: 54 ident: bb0135 article-title: Binding of human prothymosin alpha to the leucine-motif/activation domains of HTLV-I Rex and HIV-1 Rev publication-title: Eur. J. Biochem. contributor: fullname: Oroszlan – volume: 90 start-page: 9504 year: 1993 end-page: 9507 ident: bb0180 article-title: Expression of alpha-thymosins in human tissues in normal and abnormal growth publication-title: Proc. Natl Acad. Sci. USA contributor: fullname: Yialouris – volume: 4 start-page: 435 year: 2008 end-page: 447 ident: bb0485 article-title: Algorithms for highly efficient, load-balanced, and scalable molecular simulation publication-title: J. Chem. Theory Comput. contributor: fullname: Spoel – volume: 13 start-page: 76 year: 1999 end-page: 86 ident: bb0230 article-title: Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain publication-title: Genes Dev. contributor: fullname: Yamamoto – volume: 46 start-page: 13120 year: 2007 end-page: 13130 ident: bb0050 article-title: Effects of zinc binding on the structure and dynamics of the intrinsically disordered protein prothymosin alpha: evidence for metalation as an entropic switch publication-title: Biochemistry contributor: fullname: Choy – volume: 15 start-page: 35 year: 2005 end-page: 41 ident: bb0295 article-title: Natively unfolded proteins publication-title: Curr. Opin. Struct. Biol. contributor: fullname: Fink – volume: 107 start-page: 10178 year: 2010 end-page: 10183 ident: bb0145 article-title: Prothymosin-alpha inhibits HIV-1 via Toll-like receptor 4-mediated type I interferon induction publication-title: Proc. Natl Acad. Sci. USA contributor: fullname: He – volume: 21 start-page: 689 year: 2006 end-page: 700 ident: bb0270 article-title: Structural basis for defects of Keap1 activity provoked by its point mutations in lung cancer publication-title: Mol. Cell contributor: fullname: Ohtsuji – volume: 1296 start-page: 219 year: 1996 end-page: 227 ident: bb0020 article-title: Prothymosin alpha binds histones in vitro and shows activity in nucleosome assembly assay publication-title: Biochim. Biophys. Acta contributor: fullname: Freire – volume: 176 start-page: 853 year: 2007 end-page: 862 ident: bb0150 article-title: Identification of prothymosin-alpha1, the necrosis-apoptosis switch molecule in cortical neuronal cultures publication-title: J. Cell Biol. contributor: fullname: Ueda – volume: 447 start-page: 1021 year: 2007 end-page: 1025 ident: bb0300 article-title: Mechanism of coupled folding and binding of an intrinsically disordered protein publication-title: Nature contributor: fullname: Wright – volume: 5 start-page: 513 year: 1998 end-page: 517 ident: bb0405 article-title: Protein dynamics from NMR publication-title: Nat. Struct. Biol. contributor: fullname: Kay – volume: 48 start-page: 1341 year: 2000 end-page: 1355 ident: bb0130 article-title: Mobility within the nucleus and neighboring cytosol is a key feature of prothymosin-alpha publication-title: J. Histochem. Cytochem. contributor: fullname: Berger – volume: 24 start-page: 1344 year: 2008 end-page: 1348 ident: bb0380 article-title: Prediction of disordered regions in proteins based on the meta approach publication-title: Bioinformatics contributor: fullname: Kinoshita – volume: 31 start-page: 8571 year: 1992 end-page: 8586 ident: bb0415 article-title: Mapping of the spectral densities of N–H bond motions in eglin c using heteronuclear relaxation experiments publication-title: Biochemistry contributor: fullname: Wagner – volume: 12 start-page: 213 year: 2010 end-page: 223 ident: bb0440 article-title: The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1 publication-title: Nat. Cell Biol. contributor: fullname: Ichimura – volume: 358 start-page: 485 year: 2006 end-page: 497 ident: bb0435 article-title: Role of structural and dynamical plasticity in Sin3: the free PAH2 domain is a folded module in mSin3B publication-title: J. Mol. Biol. contributor: fullname: Vuister – volume: 24 start-page: 7130 year: 2004 end-page: 7139 ident: bb0240 article-title: Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2 publication-title: Mol. Cell. Biol. contributor: fullname: Chiba – volume: 93 start-page: 14960 year: 1996 end-page: 14965 ident: bb0220 article-title: Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H:quinone oxidoreductase publication-title: Proc. Natl Acad. Sci. USA contributor: fullname: Jaiswal – volume: 25 start-page: 1656 year: 2004 end-page: 1676 ident: bb0495 article-title: A biomolecular force field based on the free enthalpy of hydration and solvation: the GROMOS force-field parameter sets 53A5 and 53A6 publication-title: J. Comput. Chem. contributor: fullname: van Gunsteren – volume: 49 start-page: 1923 year: 2010 end-page: 1930 ident: bb0115 article-title: Novel small molecules relieve prothymosin alpha-mediated inhibition of apoptosome formation by blocking its interaction with Apaf-1 publication-title: Biochemistry contributor: fullname: Du – volume: 128 start-page: 165 year: 2004 end-page: 171 ident: bb0215 article-title: F2-isoprostanes as indices of lipid peroxidation in inflammatory diseases publication-title: Chem. Phys. Lipids contributor: fullname: FitzGerald – volume: 25 start-page: 3605 year: 2006 end-page: 3617 ident: bb0265 article-title: Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling publication-title: EMBO J. contributor: fullname: Hannink – volume: 73 start-page: 188 year: 2009 end-page: 192 ident: bb0165 article-title: Aberrant prothymosin-alpha expression in human bladder cancer publication-title: Urology contributor: fullname: Tsai – volume: 25 start-page: 2745 year: 2009 end-page: 2746 ident: bb0390 article-title: ANCHOR: web server for predicting protein binding regions in disordered proteins publication-title: Bioinformatics contributor: fullname: Simon – volume: 108 start-page: 1211 year: 2009 end-page: 1219 ident: bb0160 article-title: Altered protein-expressing profile in hPNAS4-induced apoptosis in A549 human lung adenocarcinoma cells publication-title: J. Cell. Biochem. contributor: fullname: Wang – volume: 30 start-page: 3275 year: 2010 end-page: 3285 ident: bb0450 article-title: A noncanonical mechanism of Nrf2 activation by autophagy deficiency: direct interaction between Keap1 and p62 publication-title: Mol. Cell. Biol. contributor: fullname: Jiang – volume: 38 start-page: 293 year: 1997 end-page: 328 ident: bb0195 article-title: Antioxidant-inducible genes publication-title: Adv. Pharmacol. contributor: fullname: Kensler – volume: 331 start-page: 753 year: 1998 end-page: 761 ident: bb0060 article-title: Overexpression of prothymosin alpha accelerates proliferation and retards differentiation in HL-60 cells publication-title: Biochem. J. contributor: fullname: Gomez-Marquez – volume: 6 start-page: 3 year: 1999 end-page: 5 ident: bb0070 article-title: Prothymosin alpha antisense oligonucleotides induce apoptosis in HL-60 cells publication-title: Cell Death Differ. contributor: fullname: Gomez-Marquez – volume: 108 start-page: 85 year: 1991 end-page: 94 ident: bb0010 article-title: Isolation and partial sequence of goat spleen prothymosin alpha publication-title: Mol. Cell. Biochem. contributor: fullname: Tsolas – volume: 26 start-page: 3111 year: 1998 end-page: 3118 ident: bb0080 article-title: Prothymosin alpha modulates the interaction of histone H1 with chromatin publication-title: Nucleic Acids Res. contributor: fullname: Papamarcaki – volume: 17 start-page: 87 year: 1993 end-page: 92 ident: bb0475 article-title: Isotope effects in peptide group hydrogen exchange publication-title: Proteins contributor: fullname: Englander – volume: 44 start-page: 418 year: 2001 end-page: 427 ident: bb0310 article-title: Structured disorder and conformational selection publication-title: Proteins contributor: fullname: Nussinov – volume: 404 start-page: 274 year: 2010 end-page: 290 ident: bb0345 article-title: Dynamic interactions between clathrin and locally structured elements in a disordered protein mediate clathrin lattice assembly publication-title: J. Mol. Biol. contributor: fullname: Lafer – volume: 267 start-page: 663 year: 2000 end-page: 668 ident: bb0055 article-title: Zn publication-title: Biochem. Biophys. Res. Commun. contributor: fullname: Vasiliev – volume: 3 start-page: 2207 year: 1994 end-page: 2216 ident: bb0445 article-title: A revised set of potentials for beta-turn formation in proteins publication-title: Protein Sci. contributor: fullname: Thornton – volume: 338 start-page: 1015 year: 2004 end-page: 1026 ident: bb0315 article-title: Preformed structural elements feature in partner recognition by intrinsically unstructured proteins publication-title: J. Mol. Biol. contributor: fullname: Tompa – volume: 31 start-page: 1243 year: 1999 end-page: 1248 ident: bb0025 article-title: Prothymosin alpha publication-title: Int. J. Biochem. Cell Biol. contributor: fullname: Gomez-Marquez – volume: 28 start-page: i75 year: 2012 end-page: i83 ident: bb0395 article-title: MoRFpred, a computational tool for sequence-based prediction and characterization of short disorder-to-order transitioning binding regions in proteins publication-title: Bioinformatics contributor: fullname: Dunker – volume: 8 start-page: 2725 year: 2012 end-page: 2740 ident: bb0330 article-title: Comparison of secondary structure formation using 10 different force fields in microsecond molecular dynamics simulations publication-title: J. Chem. Theory Comput. contributor: fullname: Karttunen – volume: 64 start-page: 233 year: 2008 end-page: 238 ident: bb0260 article-title: Structural analysis of the complex of Keap1 with a prothymosin alpha peptide publication-title: Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. contributor: fullname: Yokoyama – volume: 387 start-page: 1311 year: 2006 end-page: 1320 ident: bb0250 article-title: Two-site substrate recognition model for the Keap1-Nrf2 system: a hinge and latch mechanism publication-title: Biol. Chem. contributor: fullname: Yamamoto – volume: 7 start-page: 475 year: 2012 end-page: 488 ident: bb0355 article-title: Intrinsically disordered proteins and novel strategies for drug discovery publication-title: Expert Opin. Drug Discovery contributor: fullname: Uversky – volume: 10 start-page: 937 year: 2003 end-page: 939 ident: bb0120 article-title: Does prothymosin-alpha act as molecular switch between apoptosis and autophagy? publication-title: Cell Death Differ. contributor: fullname: Kroemer – volume: 279 start-page: 43085 year: 2004 end-page: 43091 ident: bb0305 article-title: A disorder to order transition accompanies catalysis in retinaldehyde dehydrogenase type II publication-title: J. Biol. Chem. contributor: fullname: Newcomer – volume: 105 start-page: 17772 year: 2008 end-page: 17777 ident: bb0455 article-title: Dynamic equilibrium engagement of a polyvalent ligand with a single-site receptor publication-title: Proc. Natl Acad. Sci. USA contributor: fullname: Sicheri – volume: 6 start-page: 277 year: 1995 end-page: 293 ident: bb0465 article-title: NMRPipe: a multidimensional spectral processing system based on UNIX pipes publication-title: J. Biomol. NMR contributor: fullname: Bax – volume: 284 start-page: 13856 year: 2009 end-page: 13868 ident: bb0190 article-title: Prothymosin-alpha mediates nuclear import of the INrf2/Cul3 Rbx1 complex to degrade nuclear Nrf2 publication-title: J. Biol. Chem. contributor: fullname: Jaiswal – volume: 6 start-page: e27371 year: 2011 ident: bb0325 article-title: Microsecond molecular dynamics simulations of intrinsically disordered proteins involved in the oxidative stress response publication-title: PLoS One contributor: fullname: Choy – volume: 3 start-page: 361 year: 2002 end-page: 366 ident: bb0100 article-title: Prothymosin alpha interacts with the CREB-binding protein and potentiates transcription publication-title: EMBO Rep. contributor: fullname: Papamarcaki – volume: 48 start-page: 6062 year: 2009 end-page: 6071 ident: bb0430 article-title: Structure and dynamics of the iron-sulfur cluster assembly scaffold protein IscU and its interaction with the cochaperone HscB publication-title: Biochemistry contributor: fullname: Markley – volume: 7 start-page: 242 year: 2005 end-page: 248 ident: bb0210 article-title: Oxidative stress and atherosclerosis publication-title: Curr. Atheroscler. Rep. contributor: fullname: Lee – volume: 26 start-page: 2887 year: 2006 end-page: 2900 ident: bb0235 article-title: Keap1 recruits Neh2 through binding to ETGE and DLG motifs: characterization of the two-site molecular recognition model publication-title: Mol. Cell. Biol. contributor: fullname: Yamamoto – volume: 15 start-page: 2795 year: 2006 end-page: 2804 ident: bb0400 article-title: Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: implications for fibrillation publication-title: Protein Sci. contributor: fullname: Forman-Kay – volume: 51 start-page: 151 year: 2011 end-page: 162 ident: bb0420 article-title: Measurement of amide hydrogen exchange rates with the use of radiation damping publication-title: J. Biomol. NMR contributor: fullname: Yang – volume: 3 start-page: 361 year: 2002 ident: 10.1016/j.jmb.2013.01.005_bb0100 article-title: Prothymosin alpha interacts with the CREB-binding protein and potentiates transcription publication-title: EMBO Rep. doi: 10.1093/embo-reports/kvf071 contributor: fullname: Karetsou – volume: 108 start-page: 1211 year: 2009 ident: 10.1016/j.jmb.2013.01.005_bb0160 article-title: Altered protein-expressing profile in hPNAS4-induced apoptosis in A549 human lung adenocarcinoma cells publication-title: J. Cell. Biochem. doi: 10.1002/jcb.22353 contributor: fullname: Gou – volume: 244 start-page: 37 year: 2010 ident: 10.1016/j.jmb.2013.01.005_bb0255 article-title: Nrf2 signaling and cell survival publication-title: Toxicol. Appl. Pharmacol. doi: 10.1016/j.taap.2009.06.009 contributor: fullname: Niture – volume: 44 start-page: 418 year: 2001 ident: 10.1016/j.jmb.2013.01.005_bb0310 article-title: Structured disorder and conformational selection publication-title: Proteins doi: 10.1002/prot.1107 contributor: fullname: Tsai – volume: 103 start-page: 2671 year: 2006 ident: 10.1016/j.jmb.2013.01.005_bb0125 article-title: Regulation of apoptosis by the p8/prothymosin alpha complex publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.0508955103 contributor: fullname: Malicet – volume: 1112 start-page: 269 year: 2007 ident: 10.1016/j.jmb.2013.01.005_bb0140 article-title: Influence of prothymosin-alpha on HIV-1 target cells publication-title: Ann. N. Y. Acad. Sci. doi: 10.1196/annals.1415.043 contributor: fullname: Mosoian – volume: 52 start-page: 7182 year: 1981 ident: 10.1016/j.jmb.2013.01.005_fr0015 article-title: Polymorphic transitions in single crystals: a new molecular dynamics method publication-title: J. Appl. Phys. doi: 10.1063/1.328693 contributor: fullname: Parrinello – volume: 98 start-page: 10089 year: 1993 ident: 10.1016/j.jmb.2013.01.005_fr0025 article-title: Particle mesh Ewald: an N⋅log(N) method for Ewald sums in large systems publication-title: J. Chem. Phys. doi: 10.1063/1.464397 contributor: fullname: Darden – volume: 6 start-page: 135 year: 1995 ident: 10.1016/j.jmb.2013.01.005_bb0460 article-title: 1H, 13C and 15N chemical shift referencing in biomolecular NMR publication-title: J. Biomol. NMR doi: 10.1007/BF00211777 contributor: fullname: Wishart – volume: 90 start-page: 9504 year: 1993 ident: 10.1016/j.jmb.2013.01.005_bb0180 article-title: Expression of alpha-thymosins in human tissues in normal and abnormal growth publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.90.20.9504 contributor: fullname: Tsitsiloni – volume: 88 start-page: 253 year: 1991 ident: 10.1016/j.jmb.2013.01.005_bb0065 article-title: Prothymosin alpha antisense oligomers inhibit myeloma cell division publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.88.1.253 contributor: fullname: Sburlati – volume: 26 start-page: 2887 year: 2006 ident: 10.1016/j.jmb.2013.01.005_bb0235 article-title: Keap1 recruits Neh2 through binding to ETGE and DLG motifs: characterization of the two-site molecular recognition model publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.26.8.2887-2900.2006 contributor: fullname: Tong – volume: 17 start-page: 75 year: 1993 ident: 10.1016/j.jmb.2013.01.005_bb0480 article-title: Primary structure effects on peptide group hydrogen exchange publication-title: Proteins doi: 10.1002/prot.340170110 contributor: fullname: Bai – volume: 48 start-page: 6062 year: 2009 ident: 10.1016/j.jmb.2013.01.005_bb0430 article-title: Structure and dynamics of the iron-sulfur cluster assembly scaffold protein IscU and its interaction with the cochaperone HscB publication-title: Biochemistry doi: 10.1021/bi9002277 contributor: fullname: Kim – volume: 25 start-page: 1089 year: 2005 ident: 10.1016/j.jmb.2013.01.005_bb0185 article-title: Nuclear oncoprotein prothymosin alpha is a partner of Keap1: implications for expression of oxidative stress-protecting genes publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.25.3.1089-1099.2005 contributor: fullname: Karapetian – volume: 46 start-page: 13120 year: 2007 ident: 10.1016/j.jmb.2013.01.005_bb0050 article-title: Effects of zinc binding on the structure and dynamics of the intrinsically disordered protein prothymosin alpha: evidence for metalation as an entropic switch publication-title: Biochemistry doi: 10.1021/bi7014822 contributor: fullname: Yi – volume: 18 start-page: 1463 year: 1997 ident: 10.1016/j.jmb.2013.01.005_fr0020 article-title: A linear constraint solver for molecular simulations publication-title: J. Comput. Chem. doi: 10.1002/(SICI)1096-987X(199709)18:12<1463::AID-JCC4>3.0.CO;2-H contributor: fullname: Hess – volume: 93 start-page: 14960 year: 1996 ident: 10.1016/j.jmb.2013.01.005_bb0220 article-title: Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H:quinone oxidoreductase1 gene publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.93.25.14960 contributor: fullname: Venugopal – volume: 233 start-page: 48 year: 1995 ident: 10.1016/j.jmb.2013.01.005_bb0135 article-title: Binding of human prothymosin alpha to the leucine-motif/activation domains of HTLV-I Rex and HIV-1 Rev publication-title: Eur. J. Biochem. doi: 10.1111/j.1432-1033.1995.048_1.x contributor: fullname: Kubota – volume: 6 start-page: 3 year: 1999 ident: 10.1016/j.jmb.2013.01.005_bb0070 article-title: Prothymosin alpha antisense oligonucleotides induce apoptosis in HL-60 cells publication-title: Cell Death Differ. doi: 10.1038/sj.cdd.4400450 contributor: fullname: Rodriguez – volume: 372 start-page: 549 year: 2007 ident: 10.1016/j.jmb.2013.01.005_bb0290 article-title: Molecular principles of the interactions of disordered proteins publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2007.07.004 contributor: fullname: Meszaros – volume: 30 start-page: 3275 year: 2010 ident: 10.1016/j.jmb.2013.01.005_bb0450 article-title: A noncanonical mechanism of Nrf2 activation by autophagy deficiency: direct interaction between Keap1 and p62 publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.00248-10 contributor: fullname: Lau – volume: 73 start-page: 188 year: 2009 ident: 10.1016/j.jmb.2013.01.005_bb0165 article-title: Aberrant prothymosin-alpha expression in human bladder cancer publication-title: Urology doi: 10.1016/j.urology.2008.05.031 contributor: fullname: Tsai – volume: 128 start-page: 165 year: 2004 ident: 10.1016/j.jmb.2013.01.005_bb0215 article-title: F2-isoprostanes as indices of lipid peroxidation in inflammatory diseases publication-title: Chem. Phys. Lipids doi: 10.1016/j.chemphyslip.2003.09.012 contributor: fullname: Pratico – volume: 60 start-page: 2346 year: 2004 ident: 10.1016/j.jmb.2013.01.005_bb0245 article-title: Crystallization and initial crystallographic analysis of the Kelch domain from human Keap1 publication-title: Acta Crystallogr., Sect. D: Biol. Crystallogr. doi: 10.1107/S0907444904024825 contributor: fullname: Li – volume: 5 start-page: 513 issue: Suppl. year: 1998 ident: 10.1016/j.jmb.2013.01.005_bb0405 article-title: Protein dynamics from NMR publication-title: Nat. Struct. Biol. doi: 10.1038/755 contributor: fullname: Kay – volume: 272 start-page: 26394 year: 1997 ident: 10.1016/j.jmb.2013.01.005_bb0030 article-title: Prothymosin alpha in vivo contains phosphorylated glutamic acid residues publication-title: J. Biol. Chem. doi: 10.1074/jbc.272.42.26394 contributor: fullname: Trumbore – volume: 48 start-page: 1341 year: 2000 ident: 10.1016/j.jmb.2013.01.005_bb0130 article-title: Mobility within the nucleus and neighboring cytosol is a key feature of prothymosin-alpha publication-title: J. Histochem. Cytochem. doi: 10.1177/002215540004801005 contributor: fullname: Enkemann – volume: 36 start-page: 1208 year: 2004 ident: 10.1016/j.jmb.2013.01.005_bb0225 article-title: Molecular mechanism activating Nrf2-Keap1 pathway in regulation of adaptive response to electrophiles publication-title: Free Radical Biol. Med. doi: 10.1016/j.freeradbiomed.2004.02.075 contributor: fullname: Itoh – volume: 31 start-page: 8571 year: 1992 ident: 10.1016/j.jmb.2013.01.005_bb0415 article-title: Mapping of the spectral densities of N–H bond motions in eglin c using heteronuclear relaxation experiments publication-title: Biochemistry doi: 10.1021/bi00151a027 contributor: fullname: Peng – volume: 293 start-page: 321 year: 1999 ident: 10.1016/j.jmb.2013.01.005_bb0285 article-title: Intrinsically unstructured proteins: re-assessing the protein structure–function paradigm publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1999.3110 contributor: fullname: Wright – volume: 51 start-page: 151 year: 2011 ident: 10.1016/j.jmb.2013.01.005_bb0420 article-title: Measurement of amide hydrogen exchange rates with the use of radiation damping publication-title: J. Biomol. NMR doi: 10.1007/s10858-011-9549-6 contributor: fullname: Fan – volume: 17 start-page: 232 year: 1993 ident: 10.1016/j.jmb.2013.01.005_bb0505 article-title: Conformational analysis of protein structures derived from NMR data publication-title: Proteins doi: 10.1002/prot.340170303 contributor: fullname: MacArthur – volume: 4 start-page: 435 year: 2008 ident: 10.1016/j.jmb.2013.01.005_bb0485 article-title: Algorithms for highly efficient, load-balanced, and scalable molecular simulation publication-title: J. Chem. Theory Comput. doi: 10.1021/ct700301q contributor: fullname: Hess – volume: 6 start-page: e27371 year: 2011 ident: 10.1016/j.jmb.2013.01.005_bb0325 article-title: Microsecond molecular dynamics simulations of intrinsically disordered proteins involved in the oxidative stress response publication-title: PLoS One doi: 10.1371/journal.pone.0027371 contributor: fullname: Cino – volume: 7 start-page: 242 year: 2005 ident: 10.1016/j.jmb.2013.01.005_bb0210 article-title: Oxidative stress and atherosclerosis publication-title: Curr. Atheroscler. Rep. doi: 10.1007/s11883-005-0013-5 contributor: fullname: Schulze – volume: 12 start-page: 11 year: 2004 ident: 10.1016/j.jmb.2013.01.005_bb0410 article-title: A closed binding pocket and global destabilization modify the binding properties of an alternatively spliced form of the second PDZ domain of PTP-BL publication-title: Structure doi: 10.1016/j.str.2003.11.023 contributor: fullname: Walma – volume: 467 start-page: 150 year: 2000 ident: 10.1016/j.jmb.2013.01.005_bb0075 article-title: Prothymosin alpha fragmentation in apoptosis publication-title: FEBS Lett. doi: 10.1016/S0014-5793(00)01139-X contributor: fullname: Evstafieva – volume: 25 start-page: 3605 year: 2006 ident: 10.1016/j.jmb.2013.01.005_bb0265 article-title: Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling publication-title: EMBO J. doi: 10.1038/sj.emboj.7601243 contributor: fullname: Lo – volume: 108 start-page: 85 year: 1991 ident: 10.1016/j.jmb.2013.01.005_bb0010 article-title: Isolation and partial sequence of goat spleen prothymosin alpha publication-title: Mol. Cell. Biochem. doi: 10.1007/BF00239545 contributor: fullname: Frillingos – volume: 279 start-page: 43085 year: 2004 ident: 10.1016/j.jmb.2013.01.005_bb0305 article-title: A disorder to order transition accompanies catalysis in retinaldehyde dehydrogenase type II publication-title: J. Biol. Chem. doi: 10.1074/jbc.M406139200 contributor: fullname: Bordelon – volume: 299 start-page: 223 year: 2003 ident: 10.1016/j.jmb.2013.01.005_bb0110 article-title: Distinctive roles of PHAP proteins and prothymosin-alpha in a death regulatory pathway publication-title: Science doi: 10.1126/science.1076807 contributor: fullname: Jiang – volume: 17 start-page: 87 year: 1993 ident: 10.1016/j.jmb.2013.01.005_bb0475 article-title: Isotope effects in peptide group hydrogen exchange publication-title: Proteins doi: 10.1002/prot.340170111 contributor: fullname: Connelly – volume: 25 start-page: 1656 year: 2004 ident: 10.1016/j.jmb.2013.01.005_bb0495 article-title: A biomolecular force field based on the free enthalpy of hydration and solvation: the GROMOS force-field parameter sets 53A5 and 53A6 publication-title: J. Comput. Chem. doi: 10.1002/jcc.20090 contributor: fullname: Oostenbrink – volume: 7 start-page: 475 year: 2012 ident: 10.1016/j.jmb.2013.01.005_bb0355 article-title: Intrinsically disordered proteins and novel strategies for drug discovery publication-title: Expert Opin. Drug Discovery doi: 10.1517/17460441.2012.686489 contributor: fullname: Uversky – volume: 34 start-page: 273 year: 2005 ident: 10.1016/j.jmb.2013.01.005_bb0490 article-title: Validation of the 53A6 GROMOS force field publication-title: Eur. Biophys. J. doi: 10.1007/s00249-004-0448-6 contributor: fullname: Oostenbrink – volume: 24 start-page: 435 year: 2006 ident: 10.1016/j.jmb.2013.01.005_bb0365 article-title: Rational drug design via intrinsically disordered protein publication-title: Trends Biotechnol. doi: 10.1016/j.tibtech.2006.07.005 contributor: fullname: Cheng – volume: 2 start-page: 2728 year: 2007 ident: 10.1016/j.jmb.2013.01.005_bb0500 article-title: Version 1.2 of the Crystallography and NMR system publication-title: Nat. Protoc. doi: 10.1038/nprot.2007.406 contributor: fullname: Brunger – volume: 1804 start-page: 996 year: 2010 ident: 10.1016/j.jmb.2013.01.005_bb0375 article-title: PONDR-FIT: a meta-predictor of intrinsically disordered amino acids publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbapap.2010.01.011 contributor: fullname: Xue – volume: 29A start-page: 893 year: 1993 ident: 10.1016/j.jmb.2013.01.005_bb0175 article-title: Tissue concentrations of prothymosin alpha: a novel proliferation index of primary breast cancer publication-title: Eur. J. Cancer doi: 10.1016/S0959-8049(05)80433-2 contributor: fullname: Dominguez – volume: 24 start-page: 1344 year: 2008 ident: 10.1016/j.jmb.2013.01.005_bb0380 article-title: Prediction of disordered regions in proteins based on the meta approach publication-title: Bioinformatics doi: 10.1093/bioinformatics/btn195 contributor: fullname: Ishida – volume: 24 start-page: 7130 year: 2004 ident: 10.1016/j.jmb.2013.01.005_bb0240 article-title: Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2 publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.24.16.7130-7139.2004 contributor: fullname: Kobayashi – volume: 1296 start-page: 219 year: 1996 ident: 10.1016/j.jmb.2013.01.005_bb0020 article-title: Prothymosin alpha binds histones in vitro and shows activity in nucleosome assembly assay publication-title: Biochim. Biophys. Acta doi: 10.1016/0167-4838(96)00072-6 contributor: fullname: Diaz-Jullien – volume: 57 start-page: 1 year: 2008 ident: 10.1016/j.jmb.2013.01.005_bb0385 article-title: A new protocol for high-yield purification of recombinant human prothymosin alpha expressed in Escherichia coli for NMR studies publication-title: Protein Expression Purif. doi: 10.1016/j.pep.2007.09.005 contributor: fullname: Yi – volume: 250 start-page: 197 year: 1986 ident: 10.1016/j.jmb.2013.01.005_bb0015 article-title: Human prothymosin alpha: amino acid sequence and immunologic properties publication-title: Arch. Biochem. Biophys. doi: 10.1016/0003-9861(86)90717-4 contributor: fullname: Pan – volume: 725 start-page: 1 year: 2012 ident: 10.1016/j.jmb.2013.01.005_bb0340 article-title: Fuzzy complexes: a more stochastic view of protein function publication-title: Adv. Exp. Med. Biol. doi: 10.1007/978-1-4614-0659-4_1 contributor: fullname: Fuxreiter – volume: 64 start-page: 233 year: 2008 ident: 10.1016/j.jmb.2013.01.005_bb0260 article-title: Structural analysis of the complex of Keap1 with a prothymosin alpha peptide publication-title: Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. doi: 10.1107/S1744309108004995 contributor: fullname: Padmanabhan – volume: 34 start-page: 13211 year: 1995 ident: 10.1016/j.jmb.2013.01.005_bb0040 article-title: Prothymosin alpha: a biologically active protein with random coil conformation publication-title: Biochemistry doi: 10.1021/bi00040a037 contributor: fullname: Gast – volume: 404 start-page: 274 year: 2010 ident: 10.1016/j.jmb.2013.01.005_bb0345 article-title: Dynamic interactions between clathrin and locally structured elements in a disordered protein mediate clathrin lattice assembly publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2010.09.044 contributor: fullname: Zhuo – volume: 13 start-page: 76 year: 1999 ident: 10.1016/j.jmb.2013.01.005_bb0230 article-title: Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain publication-title: Genes Dev. doi: 10.1101/gad.13.1.76 contributor: fullname: Itoh – volume: 31 start-page: 1243 year: 1999 ident: 10.1016/j.jmb.2013.01.005_bb0025 article-title: Prothymosin alpha publication-title: Int. J. Biochem. Cell Biol. doi: 10.1016/S1357-2725(99)00094-1 contributor: fullname: Segade – volume: 49 start-page: 1923 year: 2010 ident: 10.1016/j.jmb.2013.01.005_bb0115 article-title: Novel small molecules relieve prothymosin alpha-mediated inhibition of apoptosome formation by blocking its interaction with Apaf-1 publication-title: Biochemistry doi: 10.1021/bi9022329 contributor: fullname: Qi – volume: 338 start-page: 1015 year: 2004 ident: 10.1016/j.jmb.2013.01.005_bb0315 article-title: Preformed structural elements feature in partner recognition by intrinsically unstructured proteins publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2004.03.017 contributor: fullname: Fuxreiter – volume: 6 start-page: 197 year: 2005 ident: 10.1016/j.jmb.2013.01.005_bb0280 article-title: Intrinsically unstructured proteins and their functions publication-title: Nat. Rev., Mol. Cell Biol. doi: 10.1038/nrm1589 contributor: fullname: Dyson – volume: 176 start-page: 853 year: 2007 ident: 10.1016/j.jmb.2013.01.005_bb0150 article-title: Identification of prothymosin-alpha1, the necrosis-apoptosis switch molecule in cortical neuronal cultures publication-title: J. Cell Biol. doi: 10.1083/jcb.200608022 contributor: fullname: Ueda – volume: 107 start-page: 10178 year: 2010 ident: 10.1016/j.jmb.2013.01.005_bb0145 article-title: Prothymosin-alpha inhibits HIV-1 via Toll-like receptor 4-mediated type I interferon induction publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.0914870107 contributor: fullname: Mosoian – volume: 9 start-page: 10 year: 2000 ident: 10.1016/j.jmb.2013.01.005_bb0320 article-title: Folding and binding cascades: dynamic landscapes and population shifts publication-title: Protein Sci. doi: 10.1110/ps.9.1.10 contributor: fullname: Kumar – volume: 131 start-page: 7390 year: 2009 ident: 10.1016/j.jmb.2013.01.005_bb0350 article-title: Multiple independent binding sites for small-molecule inhibitors on the oncoprotein c-Myc publication-title: J. Am. Chem. Soc. doi: 10.1021/ja900616b contributor: fullname: Hammoudeh – volume: 6 start-page: 277 year: 1995 ident: 10.1016/j.jmb.2013.01.005_bb0465 article-title: NMRPipe: a multidimensional spectral processing system based on UNIX pipes publication-title: J. Biomol. NMR doi: 10.1007/BF00197809 contributor: fullname: Delaglio – volume: 577 start-page: 496 year: 2004 ident: 10.1016/j.jmb.2013.01.005_bb0095 article-title: Prothymosin alpha associates with the oncoprotein SET and is involved in chromatin decondensation publication-title: FEBS Lett. doi: 10.1016/j.febslet.2004.09.091 contributor: fullname: Karetsou – volume: 267 start-page: 663 year: 2000 ident: 10.1016/j.jmb.2013.01.005_bb0055 article-title: Zn2+-mediated structure formation and compaction of the “natively unfolded” human prothymosin alpha publication-title: Biochem. Biophys. Res. Commun. doi: 10.1006/bbrc.1999.2013 contributor: fullname: Uversky – volume: 10 start-page: 937 year: 2003 ident: 10.1016/j.jmb.2013.01.005_bb0120 article-title: Does prothymosin-alpha act as molecular switch between apoptosis and autophagy? publication-title: Cell Death Differ. doi: 10.1038/sj.cdd.4401282 contributor: fullname: Piacentini – volume: 21 start-page: 689 year: 2006 ident: 10.1016/j.jmb.2013.01.005_bb0270 article-title: Structural basis for defects of Keap1 activity provoked by its point mutations in lung cancer publication-title: Mol. Cell doi: 10.1016/j.molcel.2006.01.013 contributor: fullname: Padmanabhan – volume: 86 start-page: 246 year: 2006 ident: 10.1016/j.jmb.2013.01.005_bb0170 article-title: Peptidomic analysis of breast cancer reveals a putative surrogate marker for estrogen receptor-negative carcinomas publication-title: Lab. Invest. doi: 10.1038/labinvest.3700385 contributor: fullname: Traub – volume: 8 start-page: 2725 year: 2012 ident: 10.1016/j.jmb.2013.01.005_bb0330 article-title: Comparison of secondary structure formation using 10 different force fields in microsecond molecular dynamics simulations publication-title: J. Chem. Theory Comput. doi: 10.1021/ct300323g contributor: fullname: Cino – volume: 26 start-page: 3111 year: 1998 ident: 10.1016/j.jmb.2013.01.005_bb0080 article-title: Prothymosin alpha modulates the interaction of histone H1 with chromatin publication-title: Nucleic Acids Res. doi: 10.1093/nar/26.13.3111 contributor: fullname: Karetsou – volume: 19 start-page: 31 year: 2009 ident: 10.1016/j.jmb.2013.01.005_bb0275 article-title: Linking folding and binding publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2008.12.003 contributor: fullname: Wright – volume: 16 start-page: 349 year: 2009 ident: 10.1016/j.jmb.2013.01.005_bb0155 article-title: Prothymosin-alpha plays a defensive role in retinal ischemia through necrosis and apoptosis inhibition publication-title: Cell Death Differ. doi: 10.1038/cdd.2008.159 contributor: fullname: Fujita – volume: 38 start-page: 15009 year: 1999 ident: 10.1016/j.jmb.2013.01.005_bb0045 article-title: Natively unfolded human prothymosin alpha adopts partially folded collapsed conformation at acidic pH publication-title: Biochemistry doi: 10.1021/bi990752+ contributor: fullname: Uversky – volume: 105 start-page: 17772 year: 2008 ident: 10.1016/j.jmb.2013.01.005_bb0455 article-title: Dynamic equilibrium engagement of a polyvalent ligand with a single-site receptor publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.0809222105 contributor: fullname: Mittag – volume: 447 start-page: 1021 year: 2007 ident: 10.1016/j.jmb.2013.01.005_bb0300 article-title: Mechanism of coupled folding and binding of an intrinsically disordered protein publication-title: Nature doi: 10.1038/nature05858 contributor: fullname: Sugase – volume: 45 start-page: 27 year: 2005 ident: 10.1016/j.jmb.2013.01.005_bb0205 article-title: Cytochrome P450 activation of arylamines and heterocyclic amines publication-title: Annu. Rev. Pharmacol. Toxicol. doi: 10.1146/annurev.pharmtox.45.120403.100010 contributor: fullname: Kim – volume: 280 start-page: 16143 year: 2005 ident: 10.1016/j.jmb.2013.01.005_bb0090 article-title: Parathymosin affects the binding of linker histone H1 to nucleosomes and remodels chromatin structure publication-title: J. Biol. Chem. doi: 10.1074/jbc.M410175200 contributor: fullname: Martic – volume: 284 start-page: 13856 year: 2009 ident: 10.1016/j.jmb.2013.01.005_bb0190 article-title: Prothymosin-alpha mediates nuclear import of the INrf2/Cul3 Rbx1 complex to degrade nuclear Nrf2 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M808084200 contributor: fullname: Niture – volume: 3 start-page: 2207 year: 1994 ident: 10.1016/j.jmb.2013.01.005_bb0445 article-title: A revised set of potentials for beta-turn formation in proteins publication-title: Protein Sci. doi: 10.1002/pro.5560031206 contributor: fullname: Hutchinson – volume: 345 start-page: 71 year: 1994 ident: 10.1016/j.jmb.2013.01.005_bb0085 article-title: Prothymosin alpha binds to histone H1 in vitro publication-title: FEBS Lett. doi: 10.1016/0014-5793(94)00439-0 contributor: fullname: Papamarcaki – volume: 25 start-page: 2745 year: 2009 ident: 10.1016/j.jmb.2013.01.005_bb0390 article-title: ANCHOR: web server for predicting protein binding regions in disordered proteins publication-title: Bioinformatics doi: 10.1093/bioinformatics/btp518 contributor: fullname: Dosztanyi – volume: 12 start-page: 3205 year: 2011 ident: 10.1016/j.jmb.2013.01.005_bb0360 article-title: Novel strategies for drug discovery based on intrinsically disordered proteins (IDPs) publication-title: Int. J. Mol. Sci. doi: 10.3390/ijms12053205 contributor: fullname: Wang – volume: 15 start-page: 2795 year: 2006 ident: 10.1016/j.jmb.2013.01.005_bb0400 article-title: Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: implications for fibrillation publication-title: Protein Sci. doi: 10.1110/ps.062465306 contributor: fullname: Marsh – volume: 413 start-page: 135 year: 1997 ident: 10.1016/j.jmb.2013.01.005_bb0035 article-title: Mutational analysis of human prothymosin alpha reveals a bipartite nuclear localization signal publication-title: FEBS Lett. doi: 10.1016/S0014-5793(97)00824-7 contributor: fullname: Rubtsov – volume: 331 start-page: 753 year: 1998 ident: 10.1016/j.jmb.2013.01.005_bb0060 article-title: Overexpression of prothymosin alpha accelerates proliferation and retards differentiation in HL-60 cells publication-title: Biochem. J. doi: 10.1042/bj3310753 contributor: fullname: Rodriguez – ident: 10.1016/j.jmb.2013.01.005_bb0370 – volume: 8 start-page: 168 year: 2012 ident: 10.1016/j.jmb.2013.01.005_bb0335 article-title: Fuzziness: linking regulation to protein dynamics publication-title: Mol. BioSyst. doi: 10.1039/C1MB05234A contributor: fullname: Fuxreiter – volume: 28 start-page: i75 year: 2012 ident: 10.1016/j.jmb.2013.01.005_bb0395 article-title: MoRFpred, a computational tool for sequence-based prediction and characterization of short disorder-to-order transitioning binding regions in proteins publication-title: Bioinformatics doi: 10.1093/bioinformatics/bts209 contributor: fullname: Disfani – volume: 15 start-page: 35 year: 2005 ident: 10.1016/j.jmb.2013.01.005_bb0295 article-title: Natively unfolded proteins publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2005.01.002 contributor: fullname: Fink – volume: 278 start-page: 313 year: 2004 ident: 10.1016/j.jmb.2013.01.005_bb0470 article-title: Using NMRView to visualize and analyze the NMR spectra of macromolecules publication-title: Methods Mol. Biol. contributor: fullname: Johnson – volume: 76 start-page: 4699 year: 2002 ident: 10.1016/j.jmb.2013.01.005_bb0105 article-title: Epstein-Barr virus nuclear antigen 3C and prothymosin alpha interact with the p300 transcriptional coactivator at the CH1 and CH3/HAT domains and cooperate in regulation of transcription and histone acetylation publication-title: J. Virol. doi: 10.1128/JVI.76.10.4699-4708.2002 contributor: fullname: Subramanian – volume: 14 start-page: 237 year: 1992 ident: 10.1016/j.jmb.2013.01.005_bb0425 article-title: Hydrogen exchange in native and denatured states of hen egg-white lysozyme publication-title: Proteins doi: 10.1002/prot.340140210 contributor: fullname: Radford – volume: 126 start-page: 014101 year: 2007 ident: 10.1016/j.jmb.2013.01.005_fr0010 article-title: Canonical sampling through velocity rescaling publication-title: J. Chem. Phys. doi: 10.1063/1.2408420 contributor: fullname: Bussi – volume: 358 start-page: 485 year: 2006 ident: 10.1016/j.jmb.2013.01.005_bb0435 article-title: Role of structural and dynamical plasticity in Sin3: the free PAH2 domain is a folded module in mSin3B publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2006.01.100 contributor: fullname: van Ingen – volume: 387 start-page: 1311 year: 2006 ident: 10.1016/j.jmb.2013.01.005_bb0250 article-title: Two-site substrate recognition model for the Keap1-Nrf2 system: a hinge and latch mechanism publication-title: Biol. Chem. doi: 10.1515/BC.2006.164 contributor: fullname: Tong – volume: 12 start-page: 213 year: 2010 ident: 10.1016/j.jmb.2013.01.005_bb0440 article-title: The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1 publication-title: Nat. Cell Biol. doi: 10.1038/ncb2021 contributor: fullname: Komatsu – volume: 81 start-page: 1008 year: 1984 ident: 10.1016/j.jmb.2013.01.005_bb0005 article-title: Prothymosin alpha: isolation and properties of the major immunoreactive form of thymosin alpha 1 in rat thymus publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.81.4.1008 contributor: fullname: Haritos – volume: 236 start-page: 313 year: 1997 ident: 10.1016/j.jmb.2013.01.005_bb0200 article-title: An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements publication-title: Biochem. Biophys. Res. Commun. doi: 10.1006/bbrc.1997.6943 contributor: fullname: Itoh – volume: 38 start-page: 293 year: 1997 ident: 10.1016/j.jmb.2013.01.005_bb0195 article-title: Antioxidant-inducible genes publication-title: Adv. Pharmacol. doi: 10.1016/S1054-3589(08)60989-8 contributor: fullname: Primiano |
SSID | ssj0005348 |
Score | 2.3108902 |
Snippet | Kelch-like ECH-associated protein 1 (Keap1) is an inhibitor of nuclear factor erythroid 2-related factor 2 (Nrf2), a key transcription factor for... |
SourceID | crossref pubmed fao elsevier |
SourceType | Aggregation Database Index Database Publisher |
StartPage | 1011 |
SubjectTerms | Amino Acid Sequence binding capacity Binding Sites calorimetry Cell Nucleus - metabolism cytoplasm gene activation Humans hydrogen Intracellular Signaling Peptides and Proteins - chemistry Intracellular Signaling Peptides and Proteins - metabolism isothermal titration calorimetry Kelch-Like ECH-Associated Protein 1 molecular dynamic simulation Molecular Dynamics Simulation Molecular Sequence Data nuclear magnetic resonance nuclear magnetic resonance spectroscopy Nuclear Magnetic Resonance, Biomolecular Oxidative Stress protein dynamics Protein Interaction Domains and Motifs Protein Precursors - chemistry Protein Precursors - metabolism Protein Structure, Tertiary protein–protein interaction site-directed mutagenesis stress response Thymosin - analogs & derivatives Thymosin - chemistry Thymosin - metabolism titration transcription (genetics) transcription factors |
Title | Fuzzy Complex Formation between the Intrinsically Disordered Prothymosin α and the Kelch Domain of Keap1 Involved in the Oxidative Stress Response |
URI | https://dx.doi.org/10.1016/j.jmb.2013.01.005 https://www.ncbi.nlm.nih.gov/pubmed/23318954 |
Volume | 425 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3NbtQwEB6VIgQXBAXahVL50BNSaGI7u8mxWrratqJUlJV6s_zbptpNVssWdXvgJXgSXoRnYuzEiCLEgWMs_0T-xjNfnPkB2KWMuyxTOpGF1gmXOU8KaV1iZOlMn1mtQqDw-5P-eMKPzvPzNRjGWBjvVtnp_lanB23dtex1u7k3ryof4-tvL5gnwN6S-SA-jsYIZfrt19_cPBgvYsZw3zv-2Qw-Xlcz5b27WMjc6SvY_d023XOy-YN2BvMzegKPO95I9ttXewprtt6AB20lydUGPBzGwm3P4Nvo-vZ2RfxJn9obMorhiaTzySLI-chhvVxUdYBouiIxB6c15HThsZs1n6ua_PhOZG1C_2M71ZfkXTOT2N44fJbzDGdB7fYFR1XtrB9uKhMyiZOzEINCPrYuuPY5TEYHn4bjpKu9kGhO02XCUp_GRSFaVNKSc26KIuOaW1tSpwY8NWaQSYV8ZZBrPNMDhVTO4ucR2n-Xlzl7Aet1U9stIDK1TMl-qVEmUF24glrruKSFRG7kmOnBm7jrYt6m2BDR9-xKIETCQyTSTCBEPeARF3FHTgSagH8N20IMhbxAzSkmZ9Tf83g2W6ZpDzZbYH8tThkqujLnL_9vrVfwiIaaGSyh-TasLxfX9jUyl6XaCaK5A_f3D4_HJz8BEIrsEw |
link.rule.ids | 315,786,790,4521,24144,27957,27958,45620,45714 |
linkProvider | Elsevier |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3LbtQwFL1qi1DZICiPDk8vWCGFJrYzkyzRwGhKHyDakbqz_IRUM8lomKJOF_2Jfkl_pN_EtRMjQIgFy1h-RD7X95449wHwijLuskzpRBZaJ1zmPCmkdYmRpTN9ZrUKgcIHh_3xhH84yU_WYBhjYbxbZaf7W50etHXXstPt5s68qnyMr7-9YJ4Ae0tWrsMtT-d9_YY3l7_4eTBexJThvnv8tRmcvE5nyrt3sZC605ew-7txWney-YN3Bvszugd3O-JI3rbvdh_WbL0Ft9tSkqst2BzGym0P4Gp0dnGxIv6oT-05GcX4RNI5ZREkfWS3Xi6qOmA0XZGYhNMa8mnhwZs136qa3FwTWZvQf89O9VfyrplJbG8cPst5hrOgevuOo6p21o_nlQmpxMlRCEIhn1sfXPsQJqP3x8Nx0hVfSDSn6TJhqc_johAuKmnJOTdFkXHNrS2pUwOeGjPIpELCMsg1HuqBQi5n8fsICYDLy5w9go26qe02EJlapmS_1CgUqC9cQa11XNJCIjlyzPTgddx1MW9zbIjofHYqECLhIRJpJhCiHvCIi_hNUATagH8N20YMhfyCqlNMjqi_6PF0tkzTHjxugf25OGWo6cqcP_m_tV7C5vj4YF_s7x7uPYU7NBTQYAnNn8HGcnFmnyONWaoXQUx_AIwt7aU |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Fuzzy+Complex+Formation+between+the+Intrinsically+Disordered+Prothymosin+%CE%B1+and+the+Kelch+Domain+of+Keap1+Involved+in+the+Oxidative+Stress+Response&rft.jtitle=Journal+of+molecular+biology&rft.au=Khan%2C+Halema&rft.au=Cino%2C+Elio+A.&rft.au=Brickenden%2C+Anne&rft.au=Fan%2C+Jingsong&rft.date=2013-03-25&rft.issn=0022-2836&rft.volume=425&rft.issue=6&rft.spage=1011&rft.epage=1027&rft_id=info:doi/10.1016%2Fj.jmb.2013.01.005&rft.externalDBID=n%2Fa&rft.externalDocID=10_1016_j_jmb_2013_01_005 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0022-2836&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0022-2836&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0022-2836&client=summon |