Intrinsic disorder in proteins: Relevance to protein assemblies, drug design and host-pathogen interactions
Intrinsic disorder in proteins resulting in considerable variation in structure can lead to multiple functions including multi-specificity and diverse pathologies. Protein interfaces can involve disordered regions that assemble through a concerted-fold-and-bind mechanism. The binding involves both e...
Saved in:
| Published in | Progress in biophysics and molecular biology Vol. 156; pp. 34 - 42 |
|---|---|
| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
Elsevier Ltd
01.10.2020
|
| Subjects | |
| Online Access | Get full text |
Cover
Loading…
| Abstract | Intrinsic disorder in proteins resulting in considerable variation in structure can lead to multiple functions including multi-specificity and diverse pathologies. Protein interfaces can involve disordered regions that assemble through a concerted-fold-and-bind mechanism. The binding involves both enthalpic and entropic gains by exploiting ‘hot spots’ on the partner and displacing water molecules placed in thermodynamically unfavorable situations. The examples of Rad51-BRCA2 and Artemis-DNA-PKCs/LigIV complexes illustrate this in the context of drug design. This overview tracks the seamless involvement of protein disorder in multi-specificity of biocatalysts, protein assembly formations and host-pathogen interactions, where intrinsic disorder can in Mycobacteria, compensate for genome reduction by carrying out multiple functions and in some RNA viruses facilitate adaption to the host. These present challenging opportunities for designing new drugs and interventions. |
|---|---|
| AbstractList | Intrinsic disorder in proteins resulting in considerable variation in structure can lead to multiple functions including multi-specificity and diverse pathologies. Protein interfaces can involve disordered regions that assemble through a concerted-fold-and-bind mechanism. The binding involves both enthalpic and entropic gains by exploiting ‘hot spots’ on the partner and displacing water molecules placed in thermodynamically unfavorable situations. The examples of Rad51-BRCA2 and Artemis-DNA-PKCs/LigIV complexes illustrate this in the context of drug design. This overview tracks the seamless involvement of protein disorder in multi-specificity of biocatalysts, protein assembly formations and host-pathogen interactions, where intrinsic disorder can in Mycobacteria, compensate for genome reduction by carrying out multiple functions and in some RNA viruses facilitate adaption to the host. These present challenging opportunities for designing new drugs and interventions. Intrinsic disorder in proteins resulting in considerable variation in structure can lead to multiple functions including multi-specificity and diverse pathologies. Protein interfaces can involve disordered regions that assemble through a concerted-fold-and-bind mechanism. The binding involves both enthalpic and entropic gains by exploiting 'hot spots' on the partner and displacing water molecules placed in thermodynamically unfavorable situations. The examples of Rad51-BRCA2 and Artemis-DNA-PKCs/LigIV complexes illustrate this in the context of drug design. This overview tracks the seamless involvement of protein disorder in multi-specificity of biocatalysts, protein assembly formations and host-pathogen interactions, where intrinsic disorder can in Mycobacteria, compensate for genome reduction by carrying out multiple functions and in some RNA viruses facilitate adaption to the host. These present challenging opportunities for designing new drugs and interventions.Intrinsic disorder in proteins resulting in considerable variation in structure can lead to multiple functions including multi-specificity and diverse pathologies. Protein interfaces can involve disordered regions that assemble through a concerted-fold-and-bind mechanism. The binding involves both enthalpic and entropic gains by exploiting 'hot spots' on the partner and displacing water molecules placed in thermodynamically unfavorable situations. The examples of Rad51-BRCA2 and Artemis-DNA-PKCs/LigIV complexes illustrate this in the context of drug design. This overview tracks the seamless involvement of protein disorder in multi-specificity of biocatalysts, protein assembly formations and host-pathogen interactions, where intrinsic disorder can in Mycobacteria, compensate for genome reduction by carrying out multiple functions and in some RNA viruses facilitate adaption to the host. These present challenging opportunities for designing new drugs and interventions. |
| Author | Blundell, Tom L. Hasnain, Seyed E. Gupta, Munishwar N. |
| Author_xml | – sequence: 1 givenname: Tom L. surname: Blundell fullname: Blundell, Tom L. organization: Department of Biochemistry, University of Cambridge, Cambridge, CB21GA, UK – sequence: 2 givenname: Munishwar N. surname: Gupta fullname: Gupta, Munishwar N. organization: Department of Biochemical Engineering & Biotechnology, Indian Institute of Technology Delhi, New Delhi, India – sequence: 3 givenname: Seyed E. surname: Hasnain fullname: Hasnain, Seyed E. email: seyedhasnain@gmail.com organization: Jamia Hamdard Institute of Molecular Medicine, Jamia Hamdard, Hamdard Nagar, New Delhi, India |
| BookMark | eNqNkE1rGzEQhkVJoU7a_6BjD93tjPbL7qGQhLYJBAqlPQutNOvIWUuuRg7k31fGCYFc0ssIXuZ9GD2n4iTEQEJIhBoB-8-bejf6uI1zmbUCBTX0NUD7RixwOTQVDo06EQuAYVX1CMM7ccq8AQCFQ78Qd9chJx_YW-k8x-QoSR_kLsVMJf4if9FM9yZYkjk-xdIw03acPfEn6dJ-LR2xX5c8OHkbOVc7k2_jmkJhZUrGZh8DvxdvJzMzfXh8z8Sf799-X15VNz9_XF-e31S2BcxVo0Zle-PM0sAI6JTr7BLbsUPoWoMTNE6Bw9XYdi1NU--6sQRdZ7E0OlLNmfh45JZz_-6Js956tjTPJlDcs1atQlRqhauyujyu2hSZE016l_zWpAeNoA9-9UY_-9UHvxp6XfyW6tcXVeuzOXw0J-Pn_wFcHAFUXNx7Spqtp2La-UQ2axf965B_X8Oing |
| CitedBy_id | crossref_primary_10_1016_j_ijbiomac_2023_125455 crossref_primary_10_1016_j_ijbiomac_2023_128646 crossref_primary_10_1016_j_ijmm_2021_151544 crossref_primary_10_3390_cells11071097 crossref_primary_10_1021_acsomega_2c04076 crossref_primary_10_1039_D3SU00174A crossref_primary_10_3390_ijms23010525 crossref_primary_10_1039_D3RA00977G crossref_primary_10_3389_fimmu_2021_696491 crossref_primary_10_3390_ijms24032424 crossref_primary_10_1002_adbi_202400174 crossref_primary_10_1016_j_pbiomolbio_2020_09_002 crossref_primary_10_3389_fimmu_2021_636644 crossref_primary_10_2174_0115748871271420240213064251 crossref_primary_10_1002_pro_4968 crossref_primary_10_3389_fnmol_2023_983108 crossref_primary_10_1080_0889311X_2023_2208518 crossref_primary_10_1016_j_ijmm_2021_151495 crossref_primary_10_1080_15548627_2021_2021495 crossref_primary_10_3390_ijms22179390 crossref_primary_10_1515_pp_2023_0003 crossref_primary_10_1016_j_pbiomolbio_2022_03_001 crossref_primary_10_1134_S0006297924140104 crossref_primary_10_3390_biom10071080 crossref_primary_10_3389_fimmu_2025_1517822 crossref_primary_10_1093_nar_gkad330 crossref_primary_10_1080_14789450_2025_2451715 crossref_primary_10_3389_fimmu_2021_706081 |
| Cites_doi | 10.1021/cr400525m 10.1371/journal.pone.0060724 10.1038/mt.2015.157 10.1093/molbev/msx249 10.1038/nrd706 10.1021/cr4005082 10.1016/j.biochi.2020.05.004 10.1016/j.pbiomolbio.2015.01.009 10.1016/j.ijbiomac.2016.11.014 10.1042/BST20160172 10.1093/protein/gzx060 10.1016/j.jmb.2013.10.030 10.1016/S0959-440X(02)00289-0 10.1002/2211-5463.12749 10.1073/pnas.160259697 10.1039/C6MB00741D 10.3389/fgene.2015.00211 10.1002/cbic.201200521 10.1016/j.febslet.2009.07.016 10.1016/j.sbi.2015.08.009 10.1110/ps.072983507 10.1016/j.tibs.2015.09.002 10.1016/j.tibtech.2007.03.002 10.1016/j.str.2010.01.020 10.1021/bi0606445 10.1038/nature01230 10.1016/j.tibs.2005.07.008 10.1016/j.sbi.2010.04.003 10.1371/journal.pone.0150288 10.1016/j.drudis.2018.09.017 10.1002/cmdc.201402428 10.1016/j.biochi.2011.09.026 10.1016/j.celrep.2014.04.052 10.1038/nbt0901-805 10.1074/jbc.M117.800466 10.1016/j.tibs.2007.10.003 10.1038/s41522-018-0075-0 10.1038/257751a0 10.1186/s12859-015-0657-2 10.1007/s10930-007-9108-x 10.1146/annurev.biophys.37.032807.125924 10.1016/j.jmb.2004.03.017 10.1038/nrmicro1889 10.1021/bi050736e 10.1073/pnas.1306145110 10.1002/(SICI)1521-3773(19981102)37:20<2754::AID-ANIE2754>3.0.CO;2-3 10.1002/bies.200800151 10.1371/journal.pcbi.0030164 10.1016/S0065-3233(02)62004-2 10.4103/ijmr.IJMR_2192_18 10.1016/j.sbi.2010.10.002 10.1002/pro.2261 10.1021/pr060171o 10.3389/fmolb.2018.00039 10.1002/prot.22639 10.1039/C6MB00122J 10.1007/s11224-016-0841-7 10.1146/annurev-biochem-072711-164947 10.1016/j.btre.2015.04.001 10.3389/fphy.2019.00010 10.1016/j.ijmm.2017.09.016 10.1016/j.sbi.2018.09.008 10.1371/journal.pcbi.1000316 10.1016/j.jmb.2004.10.077 10.1073/pnas.93.1.13 10.1016/j.jmb.2018.07.017 10.1186/s40035-017-0077-5 |
| ContentType | Journal Article |
| Copyright | 2020 The Authors Copyright © 2020 The Authors. Published by Elsevier Ltd.. All rights reserved. |
| Copyright_xml | – notice: 2020 The Authors – notice: Copyright © 2020 The Authors. Published by Elsevier Ltd.. All rights reserved. |
| DBID | 6I. AAFTH AAYXX CITATION 7X8 |
| DOI | 10.1016/j.pbiomolbio.2020.06.004 |
| DatabaseName | ScienceDirect Open Access Titles Elsevier:ScienceDirect:Open Access CrossRef MEDLINE - Academic |
| DatabaseTitle | CrossRef MEDLINE - Academic |
| DatabaseTitleList | MEDLINE - Academic |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Biology |
| EISSN | 1873-1732 |
| EndPage | 42 |
| ExternalDocumentID | 10_1016_j_pbiomolbio_2020_06_004 S0079610720300614 |
| GroupedDBID | --- --K --M -~X .GJ .~1 0R~ 123 1B1 1RT 1~. 1~5 29P 3O- 4.4 457 4G. 53G 5RE 5VS 6I. 7-5 71M 8P~ 9JM AACTN AAEDT AAEDW AAFTH AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AAQXK AAXUO ABEFU ABFNM ABFRF ABGSF ABJNI ABLJU ABMAC ABTAH ABUDA ABXDB ABYKQ ACDAQ ACGFO ACGFS ACIUM ACRLP ADBBV ADEZE ADMUD ADUVX AEBSH AEFWE AEHWI AEKER AENEX AFFNX AFKWA AFTJW AFXIZ AGHFR AGRDE AGUBO AGYEJ AHHHB AIEXJ AIKHN AITUG AJBFU AJOXV ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ ASPBG AVWKF AXJTR AZFZN BKOJK BLXMC CS3 DOVZS DU5 EBS EFJIC EFLBG EJD EO8 EO9 EP2 EP3 F20 F5P FDB FEDTE FGOYB FIRID FNPLU FYGXN G-2 G-Q G8K GBLVA HLW HVGLF HX~ HZ~ IHE J1W KOM LX3 M41 MO0 MVM N9A O-L O9- OAUVE OZT P-8 P-9 P2P PC. Q38 R2- RIG ROL RPZ SBG SDF SDG SDP SES SEW SPCBC SPD SSU SSZ T5K UNMZH UQL VQP WUQ XFK ZGI ZY4 ~G- AATTM AAXKI AAYWO AAYXX ABDPE ABWVN ACRPL ACVFH ADCNI ADNMO ADVLN AEIPS AEUPX AFJKZ AFPUW AGCQF AGQPQ AGRNS AIGII AIIUN AKBMS AKRWK AKYEP ANKPU APXCP BNPGV CITATION SSH 7X8 |
| ID | FETCH-LOGICAL-c401t-32b2c6ada8a0b01d2d5c814b51054a1f03d20d19b454eff6d5bd2055c1a8a5e23 |
| IEDL.DBID | .~1 |
| ISSN | 0079-6107 1873-1732 |
| IngestDate | Fri Jul 11 09:00:13 EDT 2025 Tue Jul 01 00:42:40 EDT 2025 Thu Apr 24 23:07:01 EDT 2025 Fri Feb 23 02:47:26 EST 2024 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Keywords | Mycobacterium tuberculosis Protein promiscuity Short linear motifs Intrinsic disordered proteins Artemis Rad51-BRCA2 PE/PPE Protein structure Regulatory proteins |
| Language | English |
| License | This is an open access article under the CC BY license. |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c401t-32b2c6ada8a0b01d2d5c814b51054a1f03d20d19b454eff6d5bd2055c1a8a5e23 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 ObjectType-Review-3 content type line 23 |
| OpenAccessLink | https://www.sciencedirect.com/science/article/pii/S0079610720300614 |
| PQID | 2421122919 |
| PQPubID | 23479 |
| PageCount | 9 |
| ParticipantIDs | proquest_miscellaneous_2421122919 crossref_primary_10_1016_j_pbiomolbio_2020_06_004 crossref_citationtrail_10_1016_j_pbiomolbio_2020_06_004 elsevier_sciencedirect_doi_10_1016_j_pbiomolbio_2020_06_004 |
| ProviderPackageCode | CITATION AAYXX |
| PublicationCentury | 2000 |
| PublicationDate | October 2020 2020-10-00 20201001 |
| PublicationDateYYYYMMDD | 2020-10-01 |
| PublicationDate_xml | – month: 10 year: 2020 text: October 2020 |
| PublicationDecade | 2020 |
| PublicationTitle | Progress in biophysics and molecular biology |
| PublicationYear | 2020 |
| Publisher | Elsevier Ltd |
| Publisher_xml | – name: Elsevier Ltd |
| References | Uversky (bib67) 2013; 22 Xue, Uversky (bib73) 2014; 426 Petsko, Ringe (bib51) 2009 Whelan, Reddy, Uversky, Teng (bib72) 2016; 12 Hagai, Azia, Babu, Andino (bib27) 2014; 7 Brandon, Tooze (bib7) 1991 Blundell, Jhoti, Abell (bib6) 2002; 1 Carugo (bib8) 2017; 30 Murray, Blundell (bib46) 2010; 20 Tompa, Fuxreiter (bib63) 2008; 33 Uversky, Fink (bib69) 2007 Mukherjee, Gupta (bib45) 2017; 9 Ahmed, Dobrindt, Hacker, Hasnain (bib2) 2008; 6 deForte, Uversky (bib13) 2017; 13 van der Lee (bib71) 2014; 114 Scott (bib58) 2015; 10 Malen, Berven, Fladmark, Wiker (bib41) 2007; 7 Humphris, Kortemme (bib30) 2007; 3 Shoemaker, Portman, Wolynes (bib59) 2000; 97 Pandey (bib49) 2016; 11 Dyson, Wright (bib17) 2002; 12 Sweeney, Park, Baumann (bib61) 2017; 6 Chakravarty, Jarosz (bib9) 2018; 430 Gupta, Mukherjee (bib24) 2013; 104 Ruan, Sun, Zhang, Liu, Lai (bib54) 2019; 24 Kornev, Taylor (bib36) 2015; 40 Kumar, Alam, Rani, Ehtesham, Hasnain (bib37) 2017; 307 Jeffery (bib31) 2015; 6 Dunker, Brown, Obradovic (bib16) 2002; 62 Suragani (bib60) 2013; 110 Mukherjee, Gupta (bib44) 2015; 6 Kumar (bib38) 2019; 5 Ahmad (bib1) 2020; 10 Sasaki, Dockeril, Adamiak, Tickle, Blundell (bib55) 1975; 257 Chi, Kim, Lee, Chiang, Han (bib12) 2007; 10 Tompa, Szasz, Bunday L (bib64) 2005; 30 Uversky (bib68) 2019; 7 Goh, Dunker, Uversky (bib23) 2012; 2012 Schreiber, Keating (bib56) 2011; 21 Jubb, Blundell, Ascher (bib33) 2015; 119 Fuxreiter, Simon, Freidrich, Tompa (bib22) 2004; 338 Chaudhary, Patel, Patel, Joshi, Roy (bib11) 2015; 23 Dosztanyi, Chen, Dunker, Simon, Tompa (bib14) 2006; 5 Xue, Uversky (bib74) 2014; 426 Frades, Resjö, Andreasson (bib20) 2015; 16 Tompa (bib62) 2014; 114 Yan, Wu, Jernigan, Dobbs, Honavar (bib75) 2008; 27 Pushker, Mooney, Davey, Jacque, Shields (bib52) 2013; 8 Tompa, Schad, Tantos, Kalmar (bib66) 2015; 35 Dunker, Obradovic (bib15) 2011; 19 Gupta, Alam, Hasnain (bib26) 2020; 175 Fuxreiter (bib21) 2019; 54 Charon (bib10) 2017; 35 Mammen, Choi, Whitesides (bib42) 1998; 37 Scott (bib57) 2013; 14 Hult, Burglund (bib29) 2007; 25 Akhter, Ehebauer, Mukhopadhyay, Hasnain (bib3) 2012; 94 Kawabata (bib34) 2010; 78 Liang (bib39) 2016; 28 Gupta, Pandey, Ehtesham, Hasnain (bib25) 2019; 149 Lin, Currie, Rosen (bib40) 2017; 292 Keskin, Ma, Nussinov (bib35) 2005; 345 Oldfield, Cheng, Cortese, Romero, Uversky, Dunker (bib48) 2005; 44 Arbesu, Iruela, Fuentes, Teixeira, Pons (bib4) 2018; 5 Oldfield, Dunker (bib47) 2014; 83 Tompa (bib65) 2009; 31 Fong (bib19) 2009; 5 Uversky, Oldfield, Dunker (bib70) 2008; 37 Mittag (bib43) 2010; 18 Pellegrini (bib50) 2002; 420 Hammerstrom (bib28) 2009; 583 Babu (bib5) 2016; 44 Jones, Thornton (bib32) 1996; 93 Qamra, Prakash, Aruna, Hasnain, Mande (bib53) 2006; 45 Fuxreiter (10.1016/j.pbiomolbio.2020.06.004_bib21) 2019; 54 Pandey (10.1016/j.pbiomolbio.2020.06.004_bib49) 2016; 11 Suragani (10.1016/j.pbiomolbio.2020.06.004_bib60) 2013; 110 Chakravarty (10.1016/j.pbiomolbio.2020.06.004_bib9) 2018; 430 Charon (10.1016/j.pbiomolbio.2020.06.004_bib10) 2017; 35 Sasaki (10.1016/j.pbiomolbio.2020.06.004_bib55) 1975; 257 Xue (10.1016/j.pbiomolbio.2020.06.004_bib73) 2014; 426 Dosztanyi (10.1016/j.pbiomolbio.2020.06.004_bib14) 2006; 5 Qamra (10.1016/j.pbiomolbio.2020.06.004_bib53) 2006; 45 Kawabata (10.1016/j.pbiomolbio.2020.06.004_bib34) 2010; 78 Kumar (10.1016/j.pbiomolbio.2020.06.004_bib38) 2019; 5 Yan (10.1016/j.pbiomolbio.2020.06.004_bib75) 2008; 27 Liang (10.1016/j.pbiomolbio.2020.06.004_bib39) 2016; 28 Oldfield (10.1016/j.pbiomolbio.2020.06.004_bib47) 2014; 83 Blundell (10.1016/j.pbiomolbio.2020.06.004_bib6) 2002; 1 Gupta (10.1016/j.pbiomolbio.2020.06.004_bib24) 2013; 104 Uversky (10.1016/j.pbiomolbio.2020.06.004_bib69) 2007 Xue (10.1016/j.pbiomolbio.2020.06.004_bib74) 2014; 426 Jeffery (10.1016/j.pbiomolbio.2020.06.004_bib31) 2015; 6 Frades (10.1016/j.pbiomolbio.2020.06.004_bib20) 2015; 16 Kumar (10.1016/j.pbiomolbio.2020.06.004_bib37) 2017; 307 Scott (10.1016/j.pbiomolbio.2020.06.004_bib58) 2015; 10 Tompa (10.1016/j.pbiomolbio.2020.06.004_bib62) 2014; 114 Arbesu (10.1016/j.pbiomolbio.2020.06.004_bib4) 2018; 5 Uversky (10.1016/j.pbiomolbio.2020.06.004_bib67) 2013; 22 Tompa (10.1016/j.pbiomolbio.2020.06.004_bib65) 2009; 31 Ahmad (10.1016/j.pbiomolbio.2020.06.004_bib1) 2020; 10 Mammen (10.1016/j.pbiomolbio.2020.06.004_bib42) 1998; 37 Goh (10.1016/j.pbiomolbio.2020.06.004_bib23) 2012; 2012 Oldfield (10.1016/j.pbiomolbio.2020.06.004_bib48) 2005; 44 Fong (10.1016/j.pbiomolbio.2020.06.004_bib19) 2009; 5 Kornev (10.1016/j.pbiomolbio.2020.06.004_bib36) 2015; 40 Jubb (10.1016/j.pbiomolbio.2020.06.004_bib33) 2015; 119 Malen (10.1016/j.pbiomolbio.2020.06.004_bib41) 2007; 7 Sweeney (10.1016/j.pbiomolbio.2020.06.004_bib61) 2017; 6 Akhter (10.1016/j.pbiomolbio.2020.06.004_bib3) 2012; 94 Whelan (10.1016/j.pbiomolbio.2020.06.004_bib72) 2016; 12 Fuxreiter (10.1016/j.pbiomolbio.2020.06.004_bib22) 2004; 338 Uversky (10.1016/j.pbiomolbio.2020.06.004_bib70) 2008; 37 van der Lee (10.1016/j.pbiomolbio.2020.06.004_bib71) 2014; 114 Brandon (10.1016/j.pbiomolbio.2020.06.004_bib7) 1991 deForte (10.1016/j.pbiomolbio.2020.06.004_bib13) 2017; 13 Mukherjee (10.1016/j.pbiomolbio.2020.06.004_bib45) 2017; 97 Gupta (10.1016/j.pbiomolbio.2020.06.004_bib25) 2019; 149 Hult (10.1016/j.pbiomolbio.2020.06.004_bib29) 2007; 25 Ruan (10.1016/j.pbiomolbio.2020.06.004_bib54) 2019; 24 Chaudhary (10.1016/j.pbiomolbio.2020.06.004_bib11) 2015; 23 Jones (10.1016/j.pbiomolbio.2020.06.004_bib32) 1996; 93 Chi (10.1016/j.pbiomolbio.2020.06.004_bib12) 2007; 10 Dyson (10.1016/j.pbiomolbio.2020.06.004_bib17) 2002; 12 Lin (10.1016/j.pbiomolbio.2020.06.004_bib40) 2017; 292 Hammerstrom (10.1016/j.pbiomolbio.2020.06.004_bib28) 2009; 583 Pellegrini (10.1016/j.pbiomolbio.2020.06.004_bib50) 2002; 420 Murray (10.1016/j.pbiomolbio.2020.06.004_bib46) 2010; 20 Keskin (10.1016/j.pbiomolbio.2020.06.004_bib35) 2005; 345 Tompa (10.1016/j.pbiomolbio.2020.06.004_bib64) 2005; 30 Ahmed (10.1016/j.pbiomolbio.2020.06.004_bib2) 2008; 6 Humphris (10.1016/j.pbiomolbio.2020.06.004_bib30) 2007; 3 Scott (10.1016/j.pbiomolbio.2020.06.004_bib57) 2013; 14 Shoemaker (10.1016/j.pbiomolbio.2020.06.004_bib59) 2000; 97 Mukherjee (10.1016/j.pbiomolbio.2020.06.004_bib44) 2015; 6 Mittag (10.1016/j.pbiomolbio.2020.06.004_bib43) 2010; 18 Tompa (10.1016/j.pbiomolbio.2020.06.004_bib63) 2008; 33 Petsko (10.1016/j.pbiomolbio.2020.06.004_bib51) 2009 Carugo (10.1016/j.pbiomolbio.2020.06.004_bib8) 2017; 30 Babu (10.1016/j.pbiomolbio.2020.06.004_bib5) 2016; 44 Dunker (10.1016/j.pbiomolbio.2020.06.004_bib16) 2002; 62 Uversky (10.1016/j.pbiomolbio.2020.06.004_bib68) 2019; 7 Tompa (10.1016/j.pbiomolbio.2020.06.004_bib66) 2015; 35 Hagai (10.1016/j.pbiomolbio.2020.06.004_bib27) 2014; 7 Pushker (10.1016/j.pbiomolbio.2020.06.004_bib52) 2013; 8 Schreiber (10.1016/j.pbiomolbio.2020.06.004_bib56) 2011; 21 Dunker (10.1016/j.pbiomolbio.2020.06.004_bib15) 2011; 19 Gupta (10.1016/j.pbiomolbio.2020.06.004_bib26) 2020; 175 |
| References_xml | – volume: 20 start-page: 497 year: 2010 end-page: 507 ident: bib46 article-title: Structural biology in fragment-based drug design publication-title: Curr. Opin. Struct. Biol. – volume: 31 start-page: 328 year: 2009 end-page: 335 ident: bib65 article-title: Close encounters of the third kind: disordered domains and the interaction of proteins publication-title: Bioessays – volume: 37 start-page: 2754 year: 1998 end-page: 2794 ident: bib42 article-title: Polyvalent interactions in biological systems: implications for design and use of multivalent ligands and inhibitors publication-title: Angew Chem. Int. Ed. Engl. – volume: 104 start-page: 1178 year: 2013 end-page: 1186 ident: bib24 article-title: Enzymology: some paradigm shifts over the years publication-title: Curr. Sci. – volume: 28 start-page: 161 year: 2016 end-page: 171 ident: bib39 article-title: Achieving selectivity in space and time with DNA double-strand-break response and repair: molecular stages and scaffolds come with strings attached publication-title: J. Struct. Chem. – volume: 345 start-page: 1281 year: 2005 end-page: 1294 ident: bib35 article-title: Hot regions in protein-protein interactions: the organization and contribution of structurally conserved hot spot residues publication-title: J. Mol. Biol. – volume: 35 start-page: 38 year: 2017 end-page: 49 ident: bib10 article-title: First experimental assessment of protein intrinsic disorder involvement in an RNA virus natural adaptive process publication-title: Mol. Biol. Evol. – start-page: 18 year: 1991 end-page: 19 ident: bib7 article-title: Introduction to Protein Structure – volume: 23 start-page: 1912 year: 2015 end-page: 1926 ident: bib11 article-title: Inhibition of aggregation of mutant Huntingtin by nucleic acid aptamers in vitro and in a yeast model of Huntington’s disease publication-title: Mol. Ther. – volume: 10 start-page: 2108 year: 2007 end-page: 2117 ident: bib12 article-title: Pre-structured motifs in the natively unstructured preS1 surface antigen of hepatitis B virus publication-title: Protein Sci. – volume: 583 start-page: 2579 year: 2009 end-page: 2699 ident: bib28 article-title: [ed] Protein folding, misfolding and disease publication-title: FEBS Lett. – volume: 5 start-page: 2985 year: 2006 end-page: 2995 ident: bib14 article-title: Disorder and sequence repeats in hub proteins and their implications for network evolution publication-title: J. Proteome Res. – volume: 6 start-page: 119 year: 2015 end-page: 123 ident: bib44 article-title: Increasing importance of protein flexibility in designing biocatalytic processes publication-title: Biotechnol. Rep. (Amst). – volume: 94 start-page: 110 year: 2012 end-page: 116 ident: bib3 article-title: The PE/PPE multi gene family codes for virulence factors and is a possible source of mycobacterial antigenic variation: perhaps more publication-title: Biochemie – volume: 22 start-page: 693 year: 2013 end-page: 724 ident: bib67 article-title: A decade and a half of protein intrinsic order: biology still waits for physics publication-title: Protein Sci. – volume: 5 start-page: 39 year: 2018 ident: bib4 article-title: Intramolecular fuzzy interactions involving intrinsically disordered domains publication-title: Front. Mol. Biosci. – volume: 3 start-page: e164 year: 2007 ident: bib30 article-title: Design of multi-specificity in protein interfaces publication-title: PLoS Comput. Biol. – volume: 44 start-page: 12454 year: 2005 end-page: 12470 ident: bib48 article-title: Coupled folding and binding with alpha-helix-forming molecular recognition elements publication-title: Biochemistry – volume: 11 year: 2016 ident: bib49 article-title: Mycobacterium tuberculosis Peptidyl-Prolyl Isomerases also exhibit chaperone like activity in-vitro and in-vivo publication-title: PloS One – volume: 21 start-page: 50 year: 2011 end-page: 61 ident: bib56 article-title: Protein binding specificity versus promiscuity publication-title: Curr. Opin. Struct. Biol. – volume: 7 start-page: 1729 year: 2014 end-page: 1739 ident: bib27 article-title: Use of host-like peptide motifs in viral proteins is a prevalent strategy in host-virus interactions publication-title: Cell Rep. – volume: 6 start-page: 211 year: 2015 ident: bib31 article-title: Why study moonlighting proteins? publication-title: Front. Genet. – volume: 30 start-page: 781 year: 2017 end-page: 784 ident: bib8 article-title: Hydrophobicity diversity in globular and nonglobular proteins measured with the Gini index publication-title: Protein Eng. Des. Sel. – volume: 14 start-page: 332 year: 2013 end-page: 342 ident: bib57 article-title: Using a fragment-based approach to target protein-protein interactions publication-title: Chembiochem – volume: 83 start-page: 553 year: 2014 end-page: 584 ident: bib47 article-title: Intrinsically disordered proteins and intrinsically disordered protein regions publication-title: Annu. Rev. Biochem. – volume: 30 start-page: 484 year: 2005 end-page: 489 ident: bib64 article-title: Structural disorder throws new light on moonlighting publication-title: Biochem Sci – year: 2009 ident: bib51 article-title: Protein Structure and Function – volume: 97 start-page: 8868 year: 2000 end-page: 8873 ident: bib59 article-title: Speeding molecular recognition by using the folding funnel: the fly-casting mechanism publication-title: Proc. Natl. Acad. Sci. U.S.A. – volume: 114 start-page: 6715 year: 2014 end-page: 6732 ident: bib62 article-title: Multisteric regulation by structural disorder in modular signaling proteins: an extension of the concept of allostery publication-title: Chem. Rev. – volume: 24 start-page: 217 year: 2019 end-page: 227 ident: bib54 article-title: Targeting intrinsically disordered proteins at the edge of chaos publication-title: Drug Discov. Today – volume: 5 start-page: 3 year: 2019 ident: bib38 article-title: Peptidyl-prolyl isomerase-B is involved in Mycobacterium tuberculosis biofilm formation and a generic target for drug repurposing-based intervention publication-title: npj Biofilms Microbiomes – volume: 175 start-page: 50 year: 2020 end-page: 57 ident: bib26 article-title: Protein promiscuity in drug discovery, drug-repurposing and antibiotic resistance publication-title: Biochimie – volume: 114 start-page: 6589 year: 2014 end-page: 6631 ident: bib71 article-title: Classification of intrinsically disordered regions and proteins publication-title: Chem. Rev. – volume: 62 start-page: 25 year: 2002 end-page: 49 ident: bib16 article-title: Identification and function of usefully disordered proteins publication-title: Adv. Protein Chem. – volume: 25 start-page: 231 year: 2007 end-page: 238 ident: bib29 article-title: Enzyme promiscuity: mechanism and applications publication-title: Trends Biotechnol. – volume: 10 start-page: 70 year: 2020 end-page: 85 ident: bib1 article-title: Disorder-to-order transition in PE-PPE proteins of Mycobacterium tuberculosis augments the pro-pathogen immune response publication-title: FEBS Open Bio – volume: 16 start-page: 239 year: 2015 ident: bib20 article-title: Comparison of phosphorylation patterns across eukaryotes by discriminative N-gram analysis publication-title: BMC Bioinf. – volume: 5 year: 2009 ident: bib19 article-title: Intrinsic disorder in protein interactions: insights from a comprehensive structural analysis publication-title: PLoS Comput. Biol. – volume: 338 start-page: 1015 year: 2004 end-page: 1026 ident: bib22 article-title: Preformed structural elements feature in partner recognition by intrinsically unstructured proteins publication-title: J. Mol. Biol. – volume: 426 start-page: 1322 year: 2014 end-page: 1350 ident: bib73 article-title: Intrinsic disorder in protein in the innate antiviral immunity: another flexible side of a molecular arms race publication-title: J. Mol. Biol. – volume: 33 start-page: 2 year: 2008 end-page: 8 ident: bib63 article-title: Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions publication-title: Trends Biochem. Sci. – volume: 6 start-page: 387 year: 2008 end-page: 394 ident: bib2 article-title: Genomic fluidity and pathogenic bacteria: applications in diagnostics, epidemiology and intervention publication-title: Nat. Rev. Microbiol. – volume: 12 start-page: 1507 year: 2016 end-page: 1526 ident: bib72 article-title: Functional correlations of respiratory syncytial virus proteins to intrinsic disorder publication-title: Mol. Biosyst. – volume: 430 start-page: 4607 year: 2018 end-page: 4618 ident: bib9 article-title: More than just a phase: prions at the crossroads of epigenetic inheritance and evolutionary change publication-title: J. Mol. Biol. – volume: 35 start-page: 49 year: 2015 end-page: 59 ident: bib66 article-title: Intrinsically disordered proteins: emerging interaction specialists publication-title: Curr. Opin. Struct. Biol. – volume: 6 start-page: 6 year: 2017 ident: bib61 article-title: Protein misfolding in neurodegenerative diseases: implications and strategies publication-title: Transl. Neurodegener. – volume: 1 start-page: 45 year: 2002 end-page: 54 ident: bib6 article-title: High-throughput crystallography for lead discovery in drug design publication-title: Nat. Rev. Drug Discov. – volume: 40 start-page: 628 year: 2015 end-page: 647 ident: bib36 article-title: Dynamics-driven allostery in protein kinases publication-title: Trends Biochem. Sci. – volume: 45 start-page: 6997 year: 2006 end-page: 7005 ident: bib53 article-title: The 2.15 A crystal structure of Mycobacterium tuberculosis chorismate mutase reveals an unexpected gene duplication and suggests a role in host-pathogen interactions publication-title: Biochemistry – volume: 257 start-page: 751 year: 1975 end-page: 757 ident: bib55 article-title: X-ray analysis of glucagon and its relationship to receptor binding publication-title: Nature – volume: 13 start-page: 463 year: 2017 end-page: 469 ident: bib13 article-title: Not an exception to the rule: the functional significance of intrinsically disordered protein regions in enzymes publication-title: Mol. Biosyst. – volume: 37 start-page: 215 year: 2008 end-page: 246 ident: bib70 article-title: Intrinsically disordered proteins in human diseases: introducing the D2 concept publication-title: Annu. Rev. Biophys. – volume: 2012 start-page: 738590 year: 2012 ident: bib23 article-title: Understanding viral transmission behavior via protein intrinsic disorder prediction: Coronaviruses publication-title: J. Pathogens – year: 2007 ident: bib69 article-title: Protein Misfolding, Aggregation and Conformational Diseases. Part B: Molecular Mechanisms of Conformational Diseases – volume: 420 start-page: 287 year: 2002 end-page: 293 ident: bib50 article-title: Insights into DNA recombination from the structure of a RAD51-BRCA2 complex publication-title: Nature – volume: 7 start-page: 10 year: 2019 ident: bib68 article-title: Intrinsically disordered proteins and their ‘mysterious’ (meta) physics publication-title: Front. Physiol. – volume: 426 start-page: 1322 year: 2014 end-page: 1350 ident: bib74 article-title: Intrinsic disorder in protein in the innate antiviral immunity: another flexible side of a molecular arms race publication-title: J. Mol. Biol. – volume: 7 start-page: 1702 year: 2007 end-page: 1718 ident: bib41 article-title: Comprehensive analysis of exported proteins from publication-title: Mycobacterium tuberculosis H37Rv. – volume: 19 start-page: 805 year: 2011 end-page: 806 ident: bib15 article-title: The protein trinity-linking function and disorder publication-title: Nat. Biotechnol. – volume: 18 start-page: 494 year: 2010 end-page: 506 ident: bib43 article-title: Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase publication-title: Structure – volume: 9 start-page: 778 year: 2017 end-page: 789 ident: bib45 article-title: Protein aggregates: forms, functions and applications publication-title: J. Biol. Macromol. – volume: 8 year: 2013 ident: bib52 article-title: Marked variability in the extent of protein disorder within and between viral families publication-title: PloS One – volume: 292 start-page: 19110 year: 2017 end-page: 19120 ident: bib40 article-title: Intrinsically disordered sequences enable modulation of protein phase separation through distributed tyrosine motifs publication-title: J. Biol. Chem. – volume: 307 start-page: 481 year: 2017 end-page: 489 ident: bib37 article-title: Biofilms: survival and defense strategy for pathogens publication-title: Int. J. Med. Microbiol. – volume: 10 start-page: 296 year: 2015 end-page: 303 ident: bib58 article-title: Small-molecule inhibitors that target protein-protein interactions in the RAD51 family of recombinases publication-title: ChemMedChem – volume: 78 start-page: 1195 year: 2010 end-page: 1211 ident: bib34 article-title: Detection of multiscale pockets on protein surfaces using mathematical morphology publication-title: Proteins – volume: 12 start-page: 54 year: 2002 end-page: 60 ident: bib17 article-title: Coupling of folding and binding for unstructured proteins publication-title: Curr. Opin. Struct. Biol. – volume: 93 start-page: 13 year: 1996 end-page: 20 ident: bib32 article-title: Principles of protein-protein interactions publication-title: Proc. Natl. Acad. Sci. U.S.A. – volume: 27 start-page: 59 year: 2008 end-page: 70 ident: bib75 article-title: Characterization of protein-protein interfaces publication-title: Protein J. – volume: 149 start-page: 322 year: 2019 end-page: 325 ident: bib25 article-title: Medical implications of protein moonlighting publication-title: Indian J. Med. Res. – volume: 110 start-page: 20467 year: 2013 end-page: 20472 ident: bib60 article-title: Human resistin, a proinflammatory cytokine, shows chaperone-like activity publication-title: Proc. Natl. Acad. Sci. U.S.A. – volume: 44 start-page: 1185 year: 2016 end-page: 1200 ident: bib5 article-title: The contribution of intrinsically disordered regions to protein function, cellular complexity, and human disease publication-title: Biochem. Soc. Trans. – volume: 119 start-page: 2 year: 2015 end-page: 9 ident: bib33 article-title: Flexibility and small pockets at protein- protein interfaces: new insights into druggability publication-title: Prog. Biophys. Mol. Biol. – volume: 54 start-page: 19 year: 2019 end-page: 25 ident: bib21 article-title: Fold or not to fold upon binding-does it really matter publication-title: Curr. Opin. Struct. Biol. – volume: 114 start-page: 6589 year: 2014 ident: 10.1016/j.pbiomolbio.2020.06.004_bib71 article-title: Classification of intrinsically disordered regions and proteins publication-title: Chem. Rev. doi: 10.1021/cr400525m – start-page: 18 year: 1991 ident: 10.1016/j.pbiomolbio.2020.06.004_bib7 – volume: 8 year: 2013 ident: 10.1016/j.pbiomolbio.2020.06.004_bib52 article-title: Marked variability in the extent of protein disorder within and between viral families publication-title: PloS One doi: 10.1371/journal.pone.0060724 – volume: 23 start-page: 1912 year: 2015 ident: 10.1016/j.pbiomolbio.2020.06.004_bib11 article-title: Inhibition of aggregation of mutant Huntingtin by nucleic acid aptamers in vitro and in a yeast model of Huntington’s disease publication-title: Mol. Ther. doi: 10.1038/mt.2015.157 – volume: 35 start-page: 38 year: 2017 ident: 10.1016/j.pbiomolbio.2020.06.004_bib10 article-title: First experimental assessment of protein intrinsic disorder involvement in an RNA virus natural adaptive process publication-title: Mol. Biol. Evol. doi: 10.1093/molbev/msx249 – volume: 1 start-page: 45 year: 2002 ident: 10.1016/j.pbiomolbio.2020.06.004_bib6 article-title: High-throughput crystallography for lead discovery in drug design publication-title: Nat. Rev. Drug Discov. doi: 10.1038/nrd706 – volume: 104 start-page: 1178 year: 2013 ident: 10.1016/j.pbiomolbio.2020.06.004_bib24 article-title: Enzymology: some paradigm shifts over the years publication-title: Curr. Sci. – volume: 114 start-page: 6715 year: 2014 ident: 10.1016/j.pbiomolbio.2020.06.004_bib62 article-title: Multisteric regulation by structural disorder in modular signaling proteins: an extension of the concept of allostery publication-title: Chem. Rev. doi: 10.1021/cr4005082 – volume: 175 start-page: 50 year: 2020 ident: 10.1016/j.pbiomolbio.2020.06.004_bib26 article-title: Protein promiscuity in drug discovery, drug-repurposing and antibiotic resistance publication-title: Biochimie doi: 10.1016/j.biochi.2020.05.004 – volume: 119 start-page: 2 year: 2015 ident: 10.1016/j.pbiomolbio.2020.06.004_bib33 article-title: Flexibility and small pockets at protein- protein interfaces: new insights into druggability publication-title: Prog. Biophys. Mol. Biol. doi: 10.1016/j.pbiomolbio.2015.01.009 – volume: 97 start-page: 778 year: 2017 ident: 10.1016/j.pbiomolbio.2020.06.004_bib45 article-title: Protein aggregates: forms, functions and applications publication-title: J. Biol. Macromol. doi: 10.1016/j.ijbiomac.2016.11.014 – volume: 44 start-page: 1185 year: 2016 ident: 10.1016/j.pbiomolbio.2020.06.004_bib5 article-title: The contribution of intrinsically disordered regions to protein function, cellular complexity, and human disease publication-title: Biochem. Soc. Trans. doi: 10.1042/BST20160172 – volume: 30 start-page: 781 year: 2017 ident: 10.1016/j.pbiomolbio.2020.06.004_bib8 article-title: Hydrophobicity diversity in globular and nonglobular proteins measured with the Gini index publication-title: Protein Eng. Des. Sel. doi: 10.1093/protein/gzx060 – volume: 426 start-page: 1322 year: 2014 ident: 10.1016/j.pbiomolbio.2020.06.004_bib73 article-title: Intrinsic disorder in protein in the innate antiviral immunity: another flexible side of a molecular arms race publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2013.10.030 – volume: 12 start-page: 54 year: 2002 ident: 10.1016/j.pbiomolbio.2020.06.004_bib17 article-title: Coupling of folding and binding for unstructured proteins publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/S0959-440X(02)00289-0 – year: 2009 ident: 10.1016/j.pbiomolbio.2020.06.004_bib51 – volume: 10 start-page: 70 year: 2020 ident: 10.1016/j.pbiomolbio.2020.06.004_bib1 article-title: Disorder-to-order transition in PE-PPE proteins of Mycobacterium tuberculosis augments the pro-pathogen immune response publication-title: FEBS Open Bio doi: 10.1002/2211-5463.12749 – volume: 97 start-page: 8868 year: 2000 ident: 10.1016/j.pbiomolbio.2020.06.004_bib59 article-title: Speeding molecular recognition by using the folding funnel: the fly-casting mechanism publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.160259697 – volume: 13 start-page: 463 year: 2017 ident: 10.1016/j.pbiomolbio.2020.06.004_bib13 article-title: Not an exception to the rule: the functional significance of intrinsically disordered protein regions in enzymes publication-title: Mol. Biosyst. doi: 10.1039/C6MB00741D – volume: 6 start-page: 211 year: 2015 ident: 10.1016/j.pbiomolbio.2020.06.004_bib31 article-title: Why study moonlighting proteins? publication-title: Front. Genet. doi: 10.3389/fgene.2015.00211 – volume: 14 start-page: 332 year: 2013 ident: 10.1016/j.pbiomolbio.2020.06.004_bib57 article-title: Using a fragment-based approach to target protein-protein interactions publication-title: Chembiochem doi: 10.1002/cbic.201200521 – volume: 583 start-page: 2579 year: 2009 ident: 10.1016/j.pbiomolbio.2020.06.004_bib28 article-title: [ed] Protein folding, misfolding and disease publication-title: FEBS Lett. doi: 10.1016/j.febslet.2009.07.016 – volume: 35 start-page: 49 year: 2015 ident: 10.1016/j.pbiomolbio.2020.06.004_bib66 article-title: Intrinsically disordered proteins: emerging interaction specialists publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2015.08.009 – volume: 10 start-page: 2108 year: 2007 ident: 10.1016/j.pbiomolbio.2020.06.004_bib12 article-title: Pre-structured motifs in the natively unstructured preS1 surface antigen of hepatitis B virus publication-title: Protein Sci. doi: 10.1110/ps.072983507 – volume: 40 start-page: 628 year: 2015 ident: 10.1016/j.pbiomolbio.2020.06.004_bib36 article-title: Dynamics-driven allostery in protein kinases publication-title: Trends Biochem. Sci. doi: 10.1016/j.tibs.2015.09.002 – volume: 2012 start-page: 738590 year: 2012 ident: 10.1016/j.pbiomolbio.2020.06.004_bib23 article-title: Understanding viral transmission behavior via protein intrinsic disorder prediction: Coronaviruses publication-title: J. Pathogens – volume: 25 start-page: 231 year: 2007 ident: 10.1016/j.pbiomolbio.2020.06.004_bib29 article-title: Enzyme promiscuity: mechanism and applications publication-title: Trends Biotechnol. doi: 10.1016/j.tibtech.2007.03.002 – volume: 18 start-page: 494 year: 2010 ident: 10.1016/j.pbiomolbio.2020.06.004_bib43 article-title: Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase publication-title: Structure doi: 10.1016/j.str.2010.01.020 – volume: 45 start-page: 6997 year: 2006 ident: 10.1016/j.pbiomolbio.2020.06.004_bib53 article-title: The 2.15 A crystal structure of Mycobacterium tuberculosis chorismate mutase reveals an unexpected gene duplication and suggests a role in host-pathogen interactions publication-title: Biochemistry doi: 10.1021/bi0606445 – volume: 420 start-page: 287 year: 2002 ident: 10.1016/j.pbiomolbio.2020.06.004_bib50 article-title: Insights into DNA recombination from the structure of a RAD51-BRCA2 complex publication-title: Nature doi: 10.1038/nature01230 – volume: 30 start-page: 484 year: 2005 ident: 10.1016/j.pbiomolbio.2020.06.004_bib64 article-title: Structural disorder throws new light on moonlighting Trends publication-title: Biochem Sci doi: 10.1016/j.tibs.2005.07.008 – volume: 20 start-page: 497 year: 2010 ident: 10.1016/j.pbiomolbio.2020.06.004_bib46 article-title: Structural biology in fragment-based drug design publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2010.04.003 – volume: 11 year: 2016 ident: 10.1016/j.pbiomolbio.2020.06.004_bib49 article-title: Mycobacterium tuberculosis Peptidyl-Prolyl Isomerases also exhibit chaperone like activity in-vitro and in-vivo publication-title: PloS One doi: 10.1371/journal.pone.0150288 – volume: 24 start-page: 217 year: 2019 ident: 10.1016/j.pbiomolbio.2020.06.004_bib54 article-title: Targeting intrinsically disordered proteins at the edge of chaos publication-title: Drug Discov. Today doi: 10.1016/j.drudis.2018.09.017 – volume: 10 start-page: 296 year: 2015 ident: 10.1016/j.pbiomolbio.2020.06.004_bib58 article-title: Small-molecule inhibitors that target protein-protein interactions in the RAD51 family of recombinases publication-title: ChemMedChem doi: 10.1002/cmdc.201402428 – volume: 94 start-page: 110 year: 2012 ident: 10.1016/j.pbiomolbio.2020.06.004_bib3 article-title: The PE/PPE multi gene family codes for virulence factors and is a possible source of mycobacterial antigenic variation: perhaps more publication-title: Biochemie doi: 10.1016/j.biochi.2011.09.026 – volume: 7 start-page: 1729 year: 2014 ident: 10.1016/j.pbiomolbio.2020.06.004_bib27 article-title: Use of host-like peptide motifs in viral proteins is a prevalent strategy in host-virus interactions publication-title: Cell Rep. doi: 10.1016/j.celrep.2014.04.052 – volume: 19 start-page: 805 year: 2011 ident: 10.1016/j.pbiomolbio.2020.06.004_bib15 article-title: The protein trinity-linking function and disorder publication-title: Nat. Biotechnol. doi: 10.1038/nbt0901-805 – volume: 292 start-page: 19110 year: 2017 ident: 10.1016/j.pbiomolbio.2020.06.004_bib40 article-title: Intrinsically disordered sequences enable modulation of protein phase separation through distributed tyrosine motifs publication-title: J. Biol. Chem. doi: 10.1074/jbc.M117.800466 – volume: 33 start-page: 2 year: 2008 ident: 10.1016/j.pbiomolbio.2020.06.004_bib63 article-title: Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions publication-title: Trends Biochem. Sci. doi: 10.1016/j.tibs.2007.10.003 – volume: 5 start-page: 3 year: 2019 ident: 10.1016/j.pbiomolbio.2020.06.004_bib38 article-title: Peptidyl-prolyl isomerase-B is involved in Mycobacterium tuberculosis biofilm formation and a generic target for drug repurposing-based intervention publication-title: npj Biofilms Microbiomes doi: 10.1038/s41522-018-0075-0 – volume: 257 start-page: 751 year: 1975 ident: 10.1016/j.pbiomolbio.2020.06.004_bib55 article-title: X-ray analysis of glucagon and its relationship to receptor binding publication-title: Nature doi: 10.1038/257751a0 – volume: 16 start-page: 239 year: 2015 ident: 10.1016/j.pbiomolbio.2020.06.004_bib20 article-title: Comparison of phosphorylation patterns across eukaryotes by discriminative N-gram analysis publication-title: BMC Bioinf. doi: 10.1186/s12859-015-0657-2 – volume: 27 start-page: 59 year: 2008 ident: 10.1016/j.pbiomolbio.2020.06.004_bib75 article-title: Characterization of protein-protein interfaces publication-title: Protein J. doi: 10.1007/s10930-007-9108-x – volume: 37 start-page: 215 year: 2008 ident: 10.1016/j.pbiomolbio.2020.06.004_bib70 article-title: Intrinsically disordered proteins in human diseases: introducing the D2 concept publication-title: Annu. Rev. Biophys. doi: 10.1146/annurev.biophys.37.032807.125924 – volume: 338 start-page: 1015 year: 2004 ident: 10.1016/j.pbiomolbio.2020.06.004_bib22 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 – volume: 6 start-page: 387 year: 2008 ident: 10.1016/j.pbiomolbio.2020.06.004_bib2 article-title: Genomic fluidity and pathogenic bacteria: applications in diagnostics, epidemiology and intervention publication-title: Nat. Rev. Microbiol. doi: 10.1038/nrmicro1889 – volume: 44 start-page: 12454 year: 2005 ident: 10.1016/j.pbiomolbio.2020.06.004_bib48 article-title: Coupled folding and binding with alpha-helix-forming molecular recognition elements publication-title: Biochemistry doi: 10.1021/bi050736e – volume: 110 start-page: 20467 year: 2013 ident: 10.1016/j.pbiomolbio.2020.06.004_bib60 article-title: Human resistin, a proinflammatory cytokine, shows chaperone-like activity publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.1306145110 – volume: 37 start-page: 2754 year: 1998 ident: 10.1016/j.pbiomolbio.2020.06.004_bib42 article-title: Polyvalent interactions in biological systems: implications for design and use of multivalent ligands and inhibitors publication-title: Angew Chem. Int. Ed. Engl. doi: 10.1002/(SICI)1521-3773(19981102)37:20<2754::AID-ANIE2754>3.0.CO;2-3 – volume: 31 start-page: 328 year: 2009 ident: 10.1016/j.pbiomolbio.2020.06.004_bib65 article-title: Close encounters of the third kind: disordered domains and the interaction of proteins publication-title: Bioessays doi: 10.1002/bies.200800151 – volume: 426 start-page: 1322 year: 2014 ident: 10.1016/j.pbiomolbio.2020.06.004_bib74 article-title: Intrinsic disorder in protein in the innate antiviral immunity: another flexible side of a molecular arms race publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2013.10.030 – volume: 3 start-page: e164 year: 2007 ident: 10.1016/j.pbiomolbio.2020.06.004_bib30 article-title: Design of multi-specificity in protein interfaces publication-title: PLoS Comput. Biol. doi: 10.1371/journal.pcbi.0030164 – volume: 7 start-page: 1702 year: 2007 ident: 10.1016/j.pbiomolbio.2020.06.004_bib41 article-title: Comprehensive analysis of exported proteins from publication-title: Mycobacterium tuberculosis H37Rv. Proteomics – volume: 62 start-page: 25 year: 2002 ident: 10.1016/j.pbiomolbio.2020.06.004_bib16 article-title: Identification and function of usefully disordered proteins publication-title: Adv. Protein Chem. doi: 10.1016/S0065-3233(02)62004-2 – volume: 149 start-page: 322 year: 2019 ident: 10.1016/j.pbiomolbio.2020.06.004_bib25 article-title: Medical implications of protein moonlighting publication-title: Indian J. Med. Res. doi: 10.4103/ijmr.IJMR_2192_18 – volume: 21 start-page: 50 year: 2011 ident: 10.1016/j.pbiomolbio.2020.06.004_bib56 article-title: Protein binding specificity versus promiscuity publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2010.10.002 – volume: 22 start-page: 693 year: 2013 ident: 10.1016/j.pbiomolbio.2020.06.004_bib67 article-title: A decade and a half of protein intrinsic order: biology still waits for physics publication-title: Protein Sci. doi: 10.1002/pro.2261 – volume: 5 start-page: 2985 year: 2006 ident: 10.1016/j.pbiomolbio.2020.06.004_bib14 article-title: Disorder and sequence repeats in hub proteins and their implications for network evolution publication-title: J. Proteome Res. doi: 10.1021/pr060171o – year: 2007 ident: 10.1016/j.pbiomolbio.2020.06.004_bib69 – volume: 5 start-page: 39 year: 2018 ident: 10.1016/j.pbiomolbio.2020.06.004_bib4 article-title: Intramolecular fuzzy interactions involving intrinsically disordered domains publication-title: Front. Mol. Biosci. doi: 10.3389/fmolb.2018.00039 – volume: 78 start-page: 1195 year: 2010 ident: 10.1016/j.pbiomolbio.2020.06.004_bib34 article-title: Detection of multiscale pockets on protein surfaces using mathematical morphology publication-title: Proteins doi: 10.1002/prot.22639 – volume: 12 start-page: 1507 year: 2016 ident: 10.1016/j.pbiomolbio.2020.06.004_bib72 article-title: Functional correlations of respiratory syncytial virus proteins to intrinsic disorder publication-title: Mol. Biosyst. doi: 10.1039/C6MB00122J – volume: 28 start-page: 161 year: 2016 ident: 10.1016/j.pbiomolbio.2020.06.004_bib39 article-title: Achieving selectivity in space and time with DNA double-strand-break response and repair: molecular stages and scaffolds come with strings attached publication-title: J. Struct. Chem. doi: 10.1007/s11224-016-0841-7 – volume: 83 start-page: 553 year: 2014 ident: 10.1016/j.pbiomolbio.2020.06.004_bib47 article-title: Intrinsically disordered proteins and intrinsically disordered protein regions publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev-biochem-072711-164947 – volume: 6 start-page: 119 year: 2015 ident: 10.1016/j.pbiomolbio.2020.06.004_bib44 article-title: Increasing importance of protein flexibility in designing biocatalytic processes publication-title: Biotechnol. Rep. (Amst). doi: 10.1016/j.btre.2015.04.001 – volume: 7 start-page: 10 year: 2019 ident: 10.1016/j.pbiomolbio.2020.06.004_bib68 article-title: Intrinsically disordered proteins and their ‘mysterious’ (meta) physics publication-title: Front. Physiol. doi: 10.3389/fphy.2019.00010 – volume: 307 start-page: 481 year: 2017 ident: 10.1016/j.pbiomolbio.2020.06.004_bib37 article-title: Biofilms: survival and defense strategy for pathogens publication-title: Int. J. Med. Microbiol. doi: 10.1016/j.ijmm.2017.09.016 – volume: 54 start-page: 19 year: 2019 ident: 10.1016/j.pbiomolbio.2020.06.004_bib21 article-title: Fold or not to fold upon binding-does it really matter publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2018.09.008 – volume: 5 year: 2009 ident: 10.1016/j.pbiomolbio.2020.06.004_bib19 article-title: Intrinsic disorder in protein interactions: insights from a comprehensive structural analysis publication-title: PLoS Comput. Biol. doi: 10.1371/journal.pcbi.1000316 – volume: 345 start-page: 1281 year: 2005 ident: 10.1016/j.pbiomolbio.2020.06.004_bib35 article-title: Hot regions in protein-protein interactions: the organization and contribution of structurally conserved hot spot residues publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2004.10.077 – volume: 93 start-page: 13 year: 1996 ident: 10.1016/j.pbiomolbio.2020.06.004_bib32 article-title: Principles of protein-protein interactions publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.93.1.13 – volume: 430 start-page: 4607 year: 2018 ident: 10.1016/j.pbiomolbio.2020.06.004_bib9 article-title: More than just a phase: prions at the crossroads of epigenetic inheritance and evolutionary change publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2018.07.017 – volume: 6 start-page: 6 year: 2017 ident: 10.1016/j.pbiomolbio.2020.06.004_bib61 article-title: Protein misfolding in neurodegenerative diseases: implications and strategies publication-title: Transl. Neurodegener. doi: 10.1186/s40035-017-0077-5 |
| SSID | ssj0002176 |
| Score | 2.4424727 |
| SecondaryResourceType | review_article |
| Snippet | Intrinsic disorder in proteins resulting in considerable variation in structure can lead to multiple functions including multi-specificity and diverse... |
| SourceID | proquest crossref elsevier |
| SourceType | Aggregation Database Enrichment Source Index Database Publisher |
| StartPage | 34 |
| SubjectTerms | Artemis Intrinsic disordered proteins Mycobacterium tuberculosis PE/PPE Protein promiscuity Protein structure Rad51-BRCA2 Regulatory proteins Short linear motifs |
| Title | Intrinsic disorder in proteins: Relevance to protein assemblies, drug design and host-pathogen interactions |
| URI | https://dx.doi.org/10.1016/j.pbiomolbio.2020.06.004 https://www.proquest.com/docview/2421122919 |
| Volume | 156 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1LS8QwEA6iCF7EJ76J4NG62zRpUz0t4rIq7kEUvIW0SWV1bZdu9-DF3-5MmyqKhwUvhYZMWybTmUnmmxlCTmQEey7T1V4mtPC4SOCXkox7lulAZkyLJMOjgbthOHjkN0_iaYFctrkwCKt0ur_R6bW2diMdx83OZDTCHN8oBuOPcUQ0xFgTlPMIpfzs4xvmAS53Ha-EyR7OdmieBuM1wRz3YgxX2Cmybl3J07Vs-8NE_VLWtQXqr5FV5zrSXvN162TB5htkuWkm-b5JXq_zqhzlwHVqXElNOsppXYgBhs_pPaaS4yLTqmiHKfjO9i0BR3R6Sk05e6amhnRQnRuKCSAetiwuQMooFpYomzSI6RZ57F89XA4810rBS2EDVXkBS1gaaqOlxpNPw4xIpc8TdK-49rNuYFjX-HHCBbdZFhqRwIAQqQ8UwrJgmyzmRW53CJVBGPBISzwL4ZlkWlt4ShoGNpDaxOkuiVruqdTVGcd2F2PVAspe1DffFfJd1dg6vkv8L8pJU2tjDpqLdoHUD7lRYBLmoD5u11TBb4WxEp3bYjZVGCn3GYv9eO9fb9gnK3jXwP8OyGJVzuwhuDFVclTL6RFZ6l3fDoafki_09g |
| linkProvider | Elsevier |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3dT9swED9BEYIXxDbQysfmSXtcROPYqQNPFQK1A_owtRJvlhM7qNAlVZs-7L_fXeIwMfGAxEseLrkkOtt3Z9_d7wC-qz7uuWzPBLk0MhAyxSWluAgcN5HKuZFpTkcDd-N4OBU_7-X9Bly2tTCUVul1f6PTa23tKWdemmeL2YxqfPsJGn-KI5IhFpuwRehUsgNbg9HNcPyskNHrrkOW-HxADD6hp0nzWlCZeznHK24Wea8G8_Rd216xUv_p69oIXe_Dnvce2aD5wQ-w4YqPsN30k_zzCZ5GRbWcFSh4Zj2qJpsVrMZiQPI5-0XV5DTOrCpbMkP32f1O0Rdd_WB2uX5gts7qYKawjGpAAupaXOJEY4QtsWwqIVYHML2-mlwOA99NIchwD1UFEU95FhtrlKHDT8utzFQoUvKwhAnzXmR5z4ZJikJ0eR5bmSJByixEDul4dAidoizcZ2AqiiPRN4qOQ0SuuDEO35LFkYuUsUnWhX4rPZ15qHHqeDHXbU7Zo_4nd01y13V6nehC-My5aOA23sBz0Q6QfjF1NFqFN3B_a8dU48qicIkpXLleaQqWh5wnYXL0ri98hZ3h5O5W347GN8ewS3eabMAT6FTLtTtFr6ZKv_hZ-xfvoven |
| 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=Intrinsic+disorder+in+proteins%3A+Relevance+to+protein+assemblies%2C+drug+design+and+host-pathogen+interactions&rft.jtitle=Progress+in+biophysics+and+molecular+biology&rft.au=Blundell%2C+Tom+L.&rft.au=Gupta%2C+Munishwar+N.&rft.au=Hasnain%2C+Seyed+E.&rft.date=2020-10-01&rft.pub=Elsevier+Ltd&rft.issn=0079-6107&rft.eissn=1873-1732&rft.volume=156&rft.spage=34&rft.epage=42&rft_id=info:doi/10.1016%2Fj.pbiomolbio.2020.06.004&rft.externalDocID=S0079610720300614 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0079-6107&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0079-6107&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0079-6107&client=summon |