Structural Determinants of G-protein α Subunit Selectivity by Regulator of G-protein Signaling 2 (RGS2)

“Regulator of G-protein signaling” (RGS) proteins facilitate the termination of G protein-coupled receptor (GPCR) signaling via their ability to increase the intrinsic GTP hydrolysis rate of Gα subunits (known as GTPase-accelerating protein or “GAP” activity). RGS2 is unique in its in vitro potency...

Full description

Saved in:
Bibliographic Details
Published inThe Journal of biological chemistry Vol. 284; no. 29; pp. 19402 - 19411
Main Authors Kimple, Adam J., Soundararajan, Meera, Hutsell, Stephanie Q., Roos, Annette K., Urban, Daniel J., Setola, Vincent, Temple, Brenda R.S., Roth, Bryan L., Knapp, Stefan, Willard, Francis S., Siderovski, David P.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 17.07.2009
American Society for Biochemistry and Molecular Biology
Subjects
Online AccessGet full text

Cover

Loading…
Abstract “Regulator of G-protein signaling” (RGS) proteins facilitate the termination of G protein-coupled receptor (GPCR) signaling via their ability to increase the intrinsic GTP hydrolysis rate of Gα subunits (known as GTPase-accelerating protein or “GAP” activity). RGS2 is unique in its in vitro potency and selectivity as a GAP for Gαq subunits. As many vasoconstrictive hormones signal via Gq heterotrimer-coupled receptors, it is perhaps not surprising that RGS2-deficient mice exhibit constitutive hypertension. However, to date the particular structural features within RGS2 determining its selectivity for Gαq over Gαi/o substrates have not been completely characterized. Here, we examine a trio of point mutations to RGS2 that elicits Gαi-directed binding and GAP activities without perturbing its association with Gαq. Using x-ray crystallography, we determined a model of the triple mutant RGS2 in complex with a transition state mimetic form of Gαi at 2.8-Å resolution. Structural comparison with unliganded, wild type RGS2 and of other RGS domain/Gα complexes highlighted the roles of these residues in wild type RGS2 that weaken Gαi subunit association. Moreover, these three amino acids are seen to be evolutionarily conserved among organisms with modern cardiovascular systems, suggesting that RGS2 arose from the R4-subfamily of RGS proteins to have specialized activity as a potent and selective Gαq GAP that modulates cardiovascular function.
AbstractList “Regulator of G-protein signaling” (RGS) proteins facilitate the termination of G protein-coupled receptor (GPCR) signaling via their ability to increase the intrinsic GTP hydrolysis rate of Gα subunits (known as GTPase-accelerating protein or “GAP” activity). RGS2 is unique in its in vitro potency and selectivity as a GAP for Gα q subunits. As many vasoconstrictive hormones signal via G q heterotrimer-coupled receptors, it is perhaps not surprising that RGS2-deficient mice exhibit constitutive hypertension. However, to date the particular structural features within RGS2 determining its selectivity for Gα q over Gα i/o substrates have not been completely characterized. Here, we examine a trio of point mutations to RGS2 that elicits Gα i -directed binding and GAP activities without perturbing its association with Gα q . Using x-ray crystallography, we determined a model of the triple mutant RGS2 in complex with a transition state mimetic form of Gα i at 2.8-Å resolution. Structural comparison with unliganded, wild type RGS2 and of other RGS domain/Gα complexes highlighted the roles of these residues in wild type RGS2 that weaken Gα i subunit association. Moreover, these three amino acids are seen to be evolutionarily conserved among organisms with modern cardiovascular systems, suggesting that RGS2 arose from the R4-subfamily of RGS proteins to have specialized activity as a potent and selective Gα q GAP that modulates cardiovascular function.
"Regulator of G-protein signaling" (RGS) proteins facilitate the termination of G protein-coupled receptor (GPCR) signaling via their ability to increase the intrinsic GTP hydrolysis rate of Gα subunits (known as GTPase-accelerating protein or "GAP" activity). RGS2 is unique in its in vitro potency and selectivity as a GAP for Gαq subunits. As many vasoconstrictive hormones signal via Gq heterotrimer-coupled receptors, it is perhaps not surprising that RGS2-deficient mice exhibit constitutive hypertension. However, to date the particular structural features within RGS2 determining its selectivity for Gαq over Gαi/o substrates have not been completely characterized. Here, we examine a trio of point mutations to RGS2 that elicits Gαi-directed binding and GAP activities without perturbing its association with Gαq. Using x-ray crystallography, we determined a model of the triple mutant RGS2 in complex with a transition state mimetic form of Gαi at 2.8-Å resolution. Structural comparison with unliganded, wild type RGS2 and of other RGS domain/Gα complexes highlighted the roles of these residues in wild type RGS2 that weaken Gαi subunit association. Moreover, these three amino acids are seen to be evolutionarily conserved among organisms with modern cardiovascular systems, suggesting that RGS2 arose from the R4-subfamily of RGS proteins to have specialized activity as a potent and selective Gαq GAP that modulates cardiovascular function.
"Regulator of G-protein signaling" (RGS) proteins facilitate the termination of G protein-coupled receptor (GPCR) signaling via their ability to increase the intrinsic GTP hydrolysis rate of Galpha subunits (known as GTPase-accelerating protein or "GAP" activity). RGS2 is unique in its in vitro potency and selectivity as a GAP for Galpha(q) subunits. As many vasoconstrictive hormones signal via G(q) heterotrimer-coupled receptors, it is perhaps not surprising that RGS2-deficient mice exhibit constitutive hypertension. However, to date the particular structural features within RGS2 determining its selectivity for Galpha(q) over Galpha(i/o) substrates have not been completely characterized. Here, we examine a trio of point mutations to RGS2 that elicits Galpha(i)-directed binding and GAP activities without perturbing its association with Galpha(q). Using x-ray crystallography, we determined a model of the triple mutant RGS2 in complex with a transition state mimetic form of Galpha(i) at 2.8-A resolution. Structural comparison with unliganded, wild type RGS2 and of other RGS domain/Galpha complexes highlighted the roles of these residues in wild type RGS2 that weaken Galpha(i) subunit association. Moreover, these three amino acids are seen to be evolutionarily conserved among organisms with modern cardiovascular systems, suggesting that RGS2 arose from the R4-subfamily of RGS proteins to have specialized activity as a potent and selective Galpha(q) GAP that modulates cardiovascular function.
Author Knapp, Stefan
Urban, Daniel J.
Willard, Francis S.
Kimple, Adam J.
Roth, Bryan L.
Hutsell, Stephanie Q.
Soundararajan, Meera
Roos, Annette K.
Setola, Vincent
Temple, Brenda R.S.
Siderovski, David P.
Author_xml – sequence: 1
  givenname: Adam J.
  surname: Kimple
  fullname: Kimple, Adam J.
  organization: Department of Pharmacology, University of North Carolina, Chapel Hill, North Carolina 27599
– sequence: 2
  givenname: Meera
  surname: Soundararajan
  fullname: Soundararajan, Meera
  organization: Structural Genomics Consortium, Oxford OX3 7DQ, United Kingdom
– sequence: 3
  givenname: Stephanie Q.
  surname: Hutsell
  fullname: Hutsell, Stephanie Q.
  organization: Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599
– sequence: 4
  givenname: Annette K.
  surname: Roos
  fullname: Roos, Annette K.
  organization: Structural Genomics Consortium, Oxford OX3 7DQ, United Kingdom
– sequence: 5
  givenname: Daniel J.
  surname: Urban
  fullname: Urban, Daniel J.
  organization: Department of Pharmacology, University of North Carolina, Chapel Hill, North Carolina 27599
– sequence: 6
  givenname: Vincent
  surname: Setola
  fullname: Setola, Vincent
  organization: Department of Pharmacology, University of North Carolina, Chapel Hill, North Carolina 27599
– sequence: 7
  givenname: Brenda R.S.
  surname: Temple
  fullname: Temple, Brenda R.S.
  organization: Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599
– sequence: 8
  givenname: Bryan L.
  surname: Roth
  fullname: Roth, Bryan L.
  organization: Department of Pharmacology, University of North Carolina, Chapel Hill, North Carolina 27599
– sequence: 9
  givenname: Stefan
  surname: Knapp
  fullname: Knapp, Stefan
  organization: Structural Genomics Consortium, Oxford OX3 7DQ, United Kingdom
– sequence: 10
  givenname: Francis S.
  surname: Willard
  fullname: Willard, Francis S.
  organization: Department of Pharmacology, University of North Carolina, Chapel Hill, North Carolina 27599
– sequence: 11
  givenname: David P.
  surname: Siderovski
  fullname: Siderovski, David P.
  email: dsiderov@med.unc.edu
  organization: Department of Pharmacology, University of North Carolina, Chapel Hill, North Carolina 27599
BackLink https://www.ncbi.nlm.nih.gov/pubmed/19478087$$D View this record in MEDLINE/PubMed
BookMark eNp1kU9rFDEYh4NU7LZ69qY5iR5mm7-TmYsgVVehInQseAuZJDNNmU3WJLOwH8sv4mcyZRa1B3MJJM_7e9_kOQMnPngLwHOM1hgJdnHX6_UXjNo1Ikxg_AisMGpoRTn-fgJWCBFctYQ3p-AspTtUFmvxE3CKWyYa1IgVuO1ynHWeo5rge5tt3DqvfE4wDHBT7WLI1nn46yfs5n72LsPOTlZnt3f5APsDvLbjPKkc4sOCzo1eTc6PkMDX15uOvHkKHg9qSvbZcT8HNx8_fLv8VF193Xy-fHdVaVbzXLHBKCzMYChpeI2pKAecGN00mFLSDpqxXut24NTwpm4wMkTruiVUc0KMMvQcvF1yd3O_tUZbn8vb5C66rYoHGZSTD2-8u5Vj2EsiGOI1LwGvjgEx_JhtynLrkrbTpLwNc5K1YKJmNSrgxQLqGFKKdvjTBCN5b0cWO_LejlzslIoX_872lz_qKMDLBRhUkGqMLsmbjiBMES6TIUwK0S6ELX-4dzbKpJ312hoXixdpgvtv-9-AMas8
CitedBy_id crossref_primary_10_1016_j_cell_2020_08_052
crossref_primary_10_1371_journal_pone_0159535
crossref_primary_10_1071_RD13269
crossref_primary_10_1124_mol_114_093393
crossref_primary_10_1124_mol_110_064394
crossref_primary_10_1002_lary_24326
crossref_primary_10_1073_pnas_1110226108
crossref_primary_10_1016_j_str_2013_02_011
crossref_primary_10_1074_jbc_M112_423806
crossref_primary_10_1371_journal_pone_0162273
crossref_primary_10_1016_j_jsb_2013_03_004
crossref_primary_10_1186_1471_2164_15_167
crossref_primary_10_1002_cmdc_202100039
crossref_primary_10_1016_j_theriogenology_2017_12_046
crossref_primary_10_3389_fgene_2022_702366
crossref_primary_10_1152_physiolgenomics_00075_2023
crossref_primary_10_1021_acssynbio_8b00065
crossref_primary_10_3390_membranes11030222
crossref_primary_10_1002_jcp_24470
crossref_primary_10_1186_s13223_018_0266_5
crossref_primary_10_1002_jcb_24472
crossref_primary_10_1152_physiolgenomics_00037_2018
crossref_primary_10_1038_nature11085
crossref_primary_10_1371_journal_pone_0070701
crossref_primary_10_1371_journal_ppat_1002553
crossref_primary_10_1155_2014_789591
crossref_primary_10_1007_s00018_021_03898_4
crossref_primary_10_1124_jpet_113_204586
crossref_primary_10_3390_genes14091801
crossref_primary_10_1016_j_ajhg_2012_04_002
crossref_primary_10_1021_acs_jmedchem_6b01208
crossref_primary_10_1093_function_zqae003
crossref_primary_10_1146_annurev_pharmtox_010510_100553
crossref_primary_10_1126_scisignal_aan3677
crossref_primary_10_1038_nsmb_2068
crossref_primary_10_1042_BCJ20180285
crossref_primary_10_1016_j_gene_2010_12_001
crossref_primary_10_1016_j_redox_2024_103253
crossref_primary_10_1111_bph_13628
crossref_primary_10_1038_npp_2012_251
crossref_primary_10_1016_j_str_2012_12_016
crossref_primary_10_1074_jbc_M115_712075
crossref_primary_10_1152_ajpheart_00026_2011
crossref_primary_10_1074_jbc_M117_797134
crossref_primary_10_1074_jbc_RA120_014726
crossref_primary_10_2174_0929867329666220308112424
crossref_primary_10_1073_pnas_1104807108
crossref_primary_10_1093_chemse_bjab048
crossref_primary_10_1371_journal_pone_0065420
crossref_primary_10_1161_CIRCRESAHA_110_231423
crossref_primary_10_1016_j_pharmthera_2021_107818
crossref_primary_10_1074_jbc_RA118_006059
crossref_primary_10_1074_jbc_M111_332130
crossref_primary_10_1124_pr_110_003038
crossref_primary_10_7554_eLife_33432
crossref_primary_10_1126_scisignal_abc1940
Cites_doi 10.1038/nrm908
10.1097/01.hjh.0000226202.80689.8f
10.1038/nm958
10.1126/science.1118890
10.1016/j.bbapap.2007.06.002
10.1073/pnas.0801508105
10.1073/pnas.94.24.12851
10.1073/pnas.0801569105
10.1074/jbc.274.13.8770
10.1093/bioinformatics/btg180
10.1016/j.semcdb.2006.12.007
10.1016/j.ab.2006.02.004
10.1038/sj.onc.1204182
10.1074/jbc.273.3.1529
10.1016/j.pep.2007.01.013
10.1073/pnas.94.2.428
10.1074/jbc.M004187200
10.1146/annurev.biochem.70.1.281
10.1107/S0907444904019158
10.1073/pnas.220414397
10.1016/j.ab.2005.02.015
10.1074/jbc.273.21.12794
10.1016/S0960-9822(02)00454-2
10.1074/jbc.274.48.34253
10.1107/S0907444903028956
10.1001/archgenpsychiatry.2007.48
10.1172/JCI15598
10.1161/01.HYP.0000035397.73223.CE
10.1107/S0907444906005270
10.1006/geno.2002.6693
10.1073/pnas.0405529101
10.1038/sj.npp.1301557
10.1073/pnas.94.14.7216
10.1016/S0092-8674(00)80204-4
10.1016/j.cellsig.2006.07.013
10.1007/s00018-004-4462-3
10.1107/S090744499900846X
10.1016/S0079-6107(03)00052-X
10.2108/zsj.21.285
10.1038/35059104
10.1126/science.280.5363.574
10.1007/PL00006508
10.1016/S0167-4889(97)00121-3
10.1124/mol.107.044214
10.1016/S0076-6879(04)89005-0
10.1093/bioinformatics/17.8.754
10.1124/mi.2.3.168
10.1038/nm1101-1236
10.1124/mol.62.3.654
10.1242/jeb.198.10.2185
10.1124/pr.54.3.527
10.1038/ng1450
10.1016/S0076-6879(04)89004-9
10.1126/stke.3702007pe2
10.1016/0300-9084(96)84768-7
10.1006/jmbi.2000.4042
10.1107/S0907444996012255
10.1523/JNEUROSCI.18-18-07178.1998
10.1126/science.1147554
ContentType Journal Article
Copyright 2009 © 2009 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.
2009 by The American Society for Biochemistry and Molecular Biology, Inc.
Copyright_xml – notice: 2009 © 2009 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.
– notice: 2009 by The American Society for Biochemistry and Molecular Biology, Inc.
DBID 6I.
AAFTH
FBQ
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
7X8
5PM
DOI 10.1074/jbc.M109.024711
DatabaseName ScienceDirect Open Access Titles
Elsevier:ScienceDirect:Open Access
AGRIS
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
CrossRef
MEDLINE - Academic
PubMed Central (Full Participant titles)
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
CrossRef
MEDLINE - Academic
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 Anatomy & Physiology
Chemistry
EISSN 1083-351X
EndPage 19411
ExternalDocumentID 10_1074_jbc_M109_024711
19478087
US201301653012
S002192581981147X
Genre Research Support, Non-U.S. Gov't
Journal Article
Research Support, N.I.H., Extramural
GrantInformation_xml – fundername: NIMH NIH HHS
  grantid: F30 MH074266
– fundername: NIMH NIH HHS
  grantid: U19 MH082441
– fundername: NIGMS NIH HHS
  grantid: R01 GM082892
– fundername: NIGMS NIH HHS
  grantid: T32 GM008570
– fundername: NIGMS NIH HHS
  grantid: T32 GM008719
– fundername: National Institutes of Health
  grantid: R01 GM082892; T32 GM008570; T32 GM008719; F30 MH074266
GroupedDBID ---
-DZ
-ET
-~X
.55
0SF
18M
29J
2WC
34G
39C
4.4
53G
5BI
5GY
5RE
5VS
6I.
79B
85S
AAEDW
AAFTH
AAFWJ
AARDX
AAXUO
ABDNZ
ABOCM
ABPPZ
ABRJW
ACGFO
ACNCT
ADBBV
ADIYS
ADNWM
AENEX
AEXQZ
AFFNX
AFMIJ
AFOSN
AFPKN
ALMA_UNASSIGNED_HOLDINGS
AMRAJ
AOIJS
BAWUL
BTFSW
C1A
CJ0
CS3
DIK
DU5
E3Z
EBS
EJD
F20
F5P
FDB
FRP
GROUPED_DOAJ
GX1
HH5
HYE
IH2
KQ8
L7B
MVM
N9A
OK1
P-O
P0W
P2P
R.V
RHF
RHI
RNS
ROL
RPM
SJN
TBC
TN5
TR2
UHB
UKR
UPT
VQA
W8F
WH7
WOQ
X7M
XFK
XSW
YQT
YSK
YWH
YZZ
ZA5
ZE2
~02
~KM
.GJ
186
3O-
41~
6TJ
AAYJJ
AAYOK
ABFSI
ABPTK
ABTAH
ACSFO
ACYGS
AEQTP
AFDAS
AI.
E.L
FA8
FBQ
J5H
NHB
OHT
QZG
UQL
VH1
WHG
XJT
Y6R
YYP
ZGI
ZY4
0R~
AALRI
ADVLN
AITUG
AKRWK
CGR
CUY
CVF
ECM
EIF
H13
NPM
AAYXX
CITATION
7X8
5PM
ID FETCH-LOGICAL-c465t-4fda17dfd328561374fd52dc8813329fc44bcc9f53d586810d2cc6923c522dad3
IEDL.DBID RPM
ISSN 0021-9258
IngestDate Tue Sep 17 21:26:40 EDT 2024
Fri Oct 25 04:49:35 EDT 2024
Fri Dec 06 01:40:45 EST 2024
Sat Sep 28 08:40:24 EDT 2024
Wed Dec 27 19:18:40 EST 2023
Fri Feb 23 02:45:19 EST 2024
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 29
Language English
License This is an open access article under the CC BY license.
http://creativecommons.org/licenses/by/4.0
https://www.elsevier.com/tdm/userlicense/1.0
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c465t-4fda17dfd328561374fd52dc8813329fc44bcc9f53d586810d2cc6923c522dad3
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Co-senior authors who contributed equally to this work.
Present address: Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN 46285.
OpenAccessLink https://dx.doi.org/10.1074/jbc.M109.024711
PMID 19478087
PQID 67476460
PQPubID 23479
PageCount 10
ParticipantIDs pubmedcentral_primary_oai_pubmedcentral_nih_gov_2740565
proquest_miscellaneous_67476460
crossref_primary_10_1074_jbc_M109_024711
pubmed_primary_19478087
fao_agris_US201301653012
elsevier_sciencedirect_doi_10_1074_jbc_M109_024711
PublicationCentury 2000
PublicationDate 2009-07-17
PublicationDateYYYYMMDD 2009-07-17
PublicationDate_xml – month: 07
  year: 2009
  text: 2009-07-17
  day: 17
PublicationDecade 2000
PublicationPlace United States
PublicationPlace_xml – name: United States
– name: 9650 Rockville Pike, Bethesda, MD 20814, U.S.A
PublicationTitle The Journal of biological chemistry
PublicationTitleAlternate J Biol Chem
PublicationYear 2009
Publisher Elsevier Inc
American Society for Biochemistry and Molecular Biology
Publisher_xml – name: Elsevier Inc
– name: American Society for Biochemistry and Molecular Biology
References Tesmer, Kawano, Shankaranarayanan, Kozasa, Tesmer (bib8) 2005; 310
Tesmer, Berman, Gilman, Sprang (bib42) 1997; 89
Wieland, Bahtijari, Zhou, Kleuss, Simon (bib40) 2000; 275
Srinivasa, Watson, Overton, Blumer (bib44) 1998; 273
Gu, Tirgari, Heximer (bib14) 2008; 73
Chiba, Sasaki, Nakayama, Takamura, Satoh (bib51) 2004; 21
Emsley, Cowtan (bib35) 2004; 60
Willard, Willard, Siderovski (bib10) 2009
Stols, Zhou, Eschenfeldt, Millard, Abdullah, Collart, Kim, Donnelly (bib27) 2007; 53
Sunahara, Taussig (bib4) 2002; 2
Heximer, Knutsen, Sun, Kaltenbronn, Rhee, Peng, Oliveira-dos-Santos, Penninger, Muslin, Steinberg, Wyss, Mecham, Blumer (bib12) 2003; 111
Evans, Claiborne (bib56) 2006
Storoni, McCoy, Read (bib33) 2004; 60
Sierra, Gilbert, Householder, Grishin, Yu, Ukidwe, Barker, He, Wensel, Otero, Brown, Copeland, Jenkins, Wilkie (bib50) 2002; 79
Willard, Siderovski (bib30) 2006; 353
Oliveira-Dos-Santos, Matsumoto, Snow, Bai, Houston, Whishaw, Mariathasan, Sasaki, Wakeham, Ohashi, Roder, Barnes, Siderovski, Penninger (bib16) 2000; 97
Akhter, Luttrell, Rockman, Iaccarino, Lefkowitz, Koch (bib24) 1998; 280
Willard, Low, McCudden, Siderovski (bib29) 2007; 19
Tang, Wang, Lu, Karas, Aronovitz, Heximer, Kaltenbronn, Blumer, Siderovski, Zhu, Mendelsohn, Tang, Wang (bib13) 2003; 9
Soundararajan, Willard, Kimple, Turnbull, Ball, Schoch, Gileadi, Fedorov, Dowler, Higman, Hutsell, Sundström, Doyle, Siderovski (bib20) 2008; 105
Skiba, Yang, Huang, Bae, Hamm (bib46) 1999; 274
Willard, Kimple, Johnston, Siderovski (bib38) 2005; 340
Pancer, Mayer, Klein, Cooper (bib53) 2004; 101
Takimoto, Koitabashi, Hsu, Ketner, Zhang, Nagayama, Bedja, Gabrielson, Blanton, Siderovski, Mendelsohn, Kass (bib23) 2009; 119
Leslie (bib31) 1999; 55
Slep, Kercher, Wieland, Chen, Simon, Sigler (bib45) 2008; 105
Ingi, Krumins, Chidiac, Brothers, Chung, Snow, Barnes, Lanahan, Siderovski, Ross, Gilman, Worley (bib57) 1998; 18
Yalcin, Willis-Owen, Fullerton, Meesaq, Deacon, Rawlins, Copley, Morris, Flint, Mott (bib17) 2004; 36
McCudden, Hains, Kimple, Siderovski, Willard (bib3) 2005; 62
Rhee (bib6) 2001; 70
Heximer, Blumer (bib60) 2007; 2007
Lutz, Shankaranarayanan, Coco, Ridilla, Nance, Vettel, Baltus, Evelyn, Neubig, Wieland, Tesmer (bib7) 2007; 318
Sinnarajah, Dessauer, Srikumar, Chen, Yuen, Yilma, Dennis, Morrison, Vodyanoy, Kehrl (bib37) 2001; 409
Seack, Kruse, Müller (bib48) 1998; 1401
Siderovski, Hessel, Chung, Mak, Tyers (bib11) 1996; 6
Druey, Kehrl (bib43) 1997; 94
Notredame, Higgins, Heringa (bib61) 2000; 302
Offermanns (bib2) 2003; 83
Willard, Kimple, Kimple, Johnston, Siderovski (bib28) 2004; 389
Hepler, Berman, Gilman, Kozasa (bib47) 1997; 94
Davison, Wright, DeMont (bib55) 1995; 198
Wettschureck, Rütten, Zywietz, Gehring, Wilkie, Chen, Chien, Offermanns (bib25) 2001; 7
Fukuhara, Chikumi, Gutkind (bib5) 2001; 20
Cui, Nishiguchi, Ivleva, Yanagi, Fukutake, Nushida, Ueno, Kitamura, Maeda, Shirakawa (bib18) 2008; 33
Heximer, Srinivasa, Bernstein, Bernard, Linder, Hepler, Blumer (bib21) 1999; 274
Lan, Sarvazyan, Taussig, Mackenzie, DiBello, Dohlman, Neubig (bib41) 1998; 273
Suga, Koyanagi, Hoshiyama, Ono, Iwabe, Kuma, Miyata (bib49) 1999; 48
Ronquist, Huelsenbeck (bib64) 2003; 19
Hollinger, Hepler (bib9) 2002; 54
Hains, Siderovski, Harden (bib59) 2004; 389
Painter, Merritt (bib36) 2006; 62
Kimple, Willard, Giguère, Johnston, Mocanu, Siderovski (bib26) 2007; 1774
Evans (bib32) 1993
Davidson (bib52) 2007; 18
Galtier, Gouy, Gautier (bib62) 1996; 12
Semplicini, Lenzini, Sartori, Papparella, Calò, Pagnin, Strapazzon, Benna, Costa, Avogaro, Ceolotto, Pessina (bib15) 2006; 24
Keys, Greene, Koch, Eckhart (bib22) 2002; 40
Murshudov, Vagin, Dodson (bib34) 1997; 53
Perrière, Gouy (bib65) 1996; 78
Pierce, Premont, Lefkowitz (bib1) 2002; 3
McKenzie, Farrell, Brauner (bib54) 2007
Smoller, Paulus, Fagerness, Purcell, Yamaki, Hirshfeld-Becker, Biederman, Rosenbaum, Gelernter, Stein (bib19) 2008; 65
Popov, Yu, Kozasa, Wilkie (bib39) 1997; 94
Huelsenbeck, Ronquist (bib63) 2001; 17
Heximer (10.1074/jbc.M109.024711_bib21) 1999; 274
Skiba (10.1074/jbc.M109.024711_bib46) 1999; 274
Smoller (10.1074/jbc.M109.024711_bib19) 2008; 65
Murshudov (10.1074/jbc.M109.024711_bib34) 1997; 53
Cladman (10.1074/jbc.M109.024711_bib58) 2002; 62
Willard (10.1074/jbc.M109.024711_bib30) 2006; 353
Davison (10.1074/jbc.M109.024711_bib55) 1995; 198
Lutz (10.1074/jbc.M109.024711_bib7) 2007; 318
Keys (10.1074/jbc.M109.024711_bib22) 2002; 40
McCudden (10.1074/jbc.M109.024711_bib3) 2005; 62
Srinivasa (10.1074/jbc.M109.024711_bib44) 1998; 273
Evans (10.1074/jbc.M109.024711_bib56) 2006
Kimple (10.1074/jbc.M109.024711_bib26) 2007; 1774
Lan (10.1074/jbc.M109.024711_bib41) 1998; 273
Perrière (10.1074/jbc.M109.024711_bib65) 1996; 78
Seack (10.1074/jbc.M109.024711_bib48) 1998; 1401
Yalcin (10.1074/jbc.M109.024711_bib17) 2004; 36
Stols (10.1074/jbc.M109.024711_bib27) 2007; 53
Semplicini (10.1074/jbc.M109.024711_bib15) 2006; 24
Chiba (10.1074/jbc.M109.024711_bib51) 2004; 21
Soundararajan (10.1074/jbc.M109.024711_bib20) 2008; 105
Wettschureck (10.1074/jbc.M109.024711_bib25) 2001; 7
Takimoto (10.1074/jbc.M109.024711_bib23) 2009; 119
Willard (10.1074/jbc.M109.024711_bib28) 2004; 389
Siderovski (10.1074/jbc.M109.024711_bib11) 1996; 6
Heximer (10.1074/jbc.M109.024711_bib12) 2003; 111
Willard (10.1074/jbc.M109.024711_bib29) 2007; 19
Ronquist (10.1074/jbc.M109.024711_bib64) 2003; 19
Davidson (10.1074/jbc.M109.024711_bib52) 2007; 18
Sinnarajah (10.1074/jbc.M109.024711_bib37) 2001; 409
Wieland (10.1074/jbc.M109.024711_bib40) 2000; 275
Willard (10.1074/jbc.M109.024711_bib10) 2009
Slep (10.1074/jbc.M109.024711_bib45) 2008; 105
Gu (10.1074/jbc.M109.024711_bib14) 2008; 73
Huelsenbeck (10.1074/jbc.M109.024711_bib63) 2001; 17
Tesmer (10.1074/jbc.M109.024711_bib42) 1997; 89
Hepler (10.1074/jbc.M109.024711_bib47) 1997; 94
Hains (10.1074/jbc.M109.024711_bib59) 2004; 389
Pierce (10.1074/jbc.M109.024711_bib1) 2002; 3
Oliveira-Dos-Santos (10.1074/jbc.M109.024711_bib16) 2000; 97
Notredame (10.1074/jbc.M109.024711_bib61) 2000; 302
Painter (10.1074/jbc.M109.024711_bib36) 2006; 62
Heximer (10.1074/jbc.M109.024711_bib60) 2007; 2007
Emsley (10.1074/jbc.M109.024711_bib35) 2004; 60
Fukuhara (10.1074/jbc.M109.024711_bib5) 2001; 20
Storoni (10.1074/jbc.M109.024711_bib33) 2004; 60
Sierra (10.1074/jbc.M109.024711_bib50) 2002; 79
Leslie (10.1074/jbc.M109.024711_bib31) 1999; 55
Evans (10.1074/jbc.M109.024711_bib32) 1993
Willard (10.1074/jbc.M109.024711_bib38) 2005; 340
Rhee (10.1074/jbc.M109.024711_bib6) 2001; 70
Cui (10.1074/jbc.M109.024711_bib18) 2008; 33
Offermanns (10.1074/jbc.M109.024711_bib2) 2003; 83
Ingi (10.1074/jbc.M109.024711_bib57) 1998; 18
McKenzie (10.1074/jbc.M109.024711_bib54) 2007
Suga (10.1074/jbc.M109.024711_bib49) 1999; 48
Hollinger (10.1074/jbc.M109.024711_bib9) 2002; 54
Tang (10.1074/jbc.M109.024711_bib13) 2003; 9
Druey (10.1074/jbc.M109.024711_bib43) 1997; 94
Popov (10.1074/jbc.M109.024711_bib39) 1997; 94
Tesmer (10.1074/jbc.M109.024711_bib8) 2005; 310
Pancer (10.1074/jbc.M109.024711_bib53) 2004; 101
Galtier (10.1074/jbc.M109.024711_bib62) 1996; 12
Sunahara (10.1074/jbc.M109.024711_bib4) 2002; 2
Akhter (10.1074/jbc.M109.024711_bib24) 1998; 280
References_xml – volume: 97
  start-page: 12272
  year: 2000
  end-page: 12277
  ident: bib16
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  contributor:
    fullname: Penninger
– volume: 36
  start-page: 1197
  year: 2004
  end-page: 1202
  ident: bib17
  publication-title: Nat. Genet.
  contributor:
    fullname: Mott
– volume: 1401
  start-page: 93
  year: 1998
  end-page: 103
  ident: bib48
  publication-title: Biochim. Biophys. Acta
  contributor:
    fullname: Müller
– volume: 105
  start-page: 6243
  year: 2008
  end-page: 6248
  ident: bib45
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  contributor:
    fullname: Sigler
– volume: 62
  start-page: 439
  year: 2006
  end-page: 450
  ident: bib36
  publication-title: Acta Crystallogr. D Biol. Crystallogr.
  contributor:
    fullname: Merritt
– year: 2006
  ident: bib56
  publication-title: The Physiology of Fishes
  contributor:
    fullname: Claiborne
– volume: 94
  start-page: 7216
  year: 1997
  end-page: 7220
  ident: bib39
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  contributor:
    fullname: Wilkie
– volume: 24
  start-page: 1115
  year: 2006
  end-page: 1124
  ident: bib15
  publication-title: J. Hypertens.
  contributor:
    fullname: Pessina
– volume: 318
  start-page: 1923
  year: 2007
  end-page: 1927
  ident: bib7
  publication-title: Science
  contributor:
    fullname: Tesmer
– start-page: 114
  year: 1993
  end-page: 122
  ident: bib32
  publication-title: Proceedings of the CCP4 Study Weekend on Data Collection and Processing
  contributor:
    fullname: Evans
– volume: 273
  start-page: 1529
  year: 1998
  end-page: 1533
  ident: bib44
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Blumer
– volume: 274
  start-page: 34253
  year: 1999
  end-page: 34259
  ident: bib21
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Blumer
– volume: 40
  start-page: 660
  year: 2002
  end-page: 666
  ident: bib22
  publication-title: Hypertension
  contributor:
    fullname: Eckhart
– year: 2007
  ident: bib54
  publication-title: Primitive Fishes
  contributor:
    fullname: Brauner
– volume: 65
  start-page: 298
  year: 2008
  end-page: 308
  ident: bib19
  publication-title: Arch. Gen. Psychiatry
  contributor:
    fullname: Stein
– volume: 280
  start-page: 574
  year: 1998
  end-page: 577
  ident: bib24
  publication-title: Science
  contributor:
    fullname: Koch
– volume: 2
  start-page: 168
  year: 2002
  end-page: 184
  ident: bib4
  publication-title: Mol. Interv.
  contributor:
    fullname: Taussig
– volume: 119
  start-page: 408
  year: 2009
  end-page: 420
  ident: bib23
  publication-title: J. Clin. Invest.
  contributor:
    fullname: Kass
– volume: 19
  start-page: 1572
  year: 2003
  end-page: 1574
  ident: bib64
  publication-title: Bioinformatics
  contributor:
    fullname: Huelsenbeck
– volume: 12
  start-page: 543
  year: 1996
  end-page: 548
  ident: bib62
  publication-title: Comput. Appl. Biosci.
  contributor:
    fullname: Gautier
– volume: 19
  start-page: 428
  year: 2007
  end-page: 438
  ident: bib29
  publication-title: Cell. Signal.
  contributor:
    fullname: Siderovski
– volume: 62
  start-page: 551
  year: 2005
  end-page: 577
  ident: bib3
  publication-title: Cell Mol. Life Sci.
  contributor:
    fullname: Willard
– volume: 389
  start-page: 71
  year: 2004
  end-page: 88
  ident: bib59
  publication-title: Methods Enzymol.
  contributor:
    fullname: Harden
– volume: 302
  start-page: 205
  year: 2000
  end-page: 217
  ident: bib61
  publication-title: J. Mol. Biol.
  contributor:
    fullname: Heringa
– volume: 33
  start-page: 1537
  year: 2008
  end-page: 1544
  ident: bib18
  publication-title: Neuropsychopharmacology
  contributor:
    fullname: Shirakawa
– volume: 54
  start-page: 527
  year: 2002
  end-page: 559
  ident: bib9
  publication-title: Pharmacol. Rev.
  contributor:
    fullname: Hepler
– volume: 275
  start-page: 28500
  year: 2000
  end-page: 28506
  ident: bib40
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Simon
– volume: 3
  start-page: 639
  year: 2002
  end-page: 650
  ident: bib1
  publication-title: Nat. Rev. Mol. Cell Biol.
  contributor:
    fullname: Lefkowitz
– volume: 389
  start-page: 56
  year: 2004
  end-page: 71
  ident: bib28
  publication-title: Methods Enzymol.
  contributor:
    fullname: Siderovski
– volume: 60
  start-page: 2126
  year: 2004
  end-page: 2132
  ident: bib35
  publication-title: Acta Crystallogr. D Biol. Crystallogr.
  contributor:
    fullname: Cowtan
– volume: 21
  start-page: 285
  year: 2004
  end-page: 298
  ident: bib51
  publication-title: Zool. Sci.
  contributor:
    fullname: Satoh
– volume: 70
  start-page: 281
  year: 2001
  end-page: 312
  ident: bib6
  publication-title: Annu. Rev. Biochem.
  contributor:
    fullname: Rhee
– volume: 6
  start-page: 211
  year: 1996
  end-page: 212
  ident: bib11
  publication-title: Curr. Biol.
  contributor:
    fullname: Tyers
– volume: 1774
  start-page: 1213
  year: 2007
  end-page: 1220
  ident: bib26
  publication-title: Biochim. Biophys. Acta
  contributor:
    fullname: Siderovski
– volume: 274
  start-page: 8770
  year: 1999
  end-page: 8778
  ident: bib46
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Hamm
– volume: 353
  start-page: 147
  year: 2006
  end-page: 149
  ident: bib30
  publication-title: Anal. Biochem.
  contributor:
    fullname: Siderovski
– volume: 105
  start-page: 6457
  year: 2008
  end-page: 6462
  ident: bib20
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  contributor:
    fullname: Siderovski
– volume: 409
  start-page: 1051
  year: 2001
  end-page: 1055
  ident: bib37
  publication-title: Nature
  contributor:
    fullname: Kehrl
– volume: 18
  start-page: 7178
  year: 1998
  end-page: 7188
  ident: bib57
  publication-title: J. Neurosci.
  contributor:
    fullname: Worley
– volume: 83
  start-page: 101
  year: 2003
  end-page: 130
  ident: bib2
  publication-title: Prog. Biophys. Mol. Biol.
  contributor:
    fullname: Offermanns
– volume: 55
  start-page: 1696
  year: 1999
  end-page: 1702
  ident: bib31
  publication-title: Acta Crystallogr. D Biol. Crystallogr.
  contributor:
    fullname: Leslie
– volume: 2007
  start-page: pe2
  year: 2007
  ident: bib60
  publication-title: Sci. STKE
  contributor:
    fullname: Blumer
– volume: 53
  start-page: 396
  year: 2007
  end-page: 403
  ident: bib27
  publication-title: Protein Expr. Purif.
  contributor:
    fullname: Donnelly
– volume: 73
  start-page: 1037
  year: 2008
  end-page: 1043
  ident: bib14
  publication-title: Mol. Pharmacol.
  contributor:
    fullname: Heximer
– volume: 94
  start-page: 12851
  year: 1997
  end-page: 12856
  ident: bib43
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  contributor:
    fullname: Kehrl
– volume: 89
  start-page: 251
  year: 1997
  end-page: 261
  ident: bib42
  publication-title: Cell
  contributor:
    fullname: Sprang
– volume: 48
  start-page: 646
  year: 1999
  end-page: 653
  ident: bib49
  publication-title: J. Mol. Evol.
  contributor:
    fullname: Miyata
– volume: 18
  start-page: 16
  year: 2007
  end-page: 26
  ident: bib52
  publication-title: Semin. Cell Dev. Biol.
  contributor:
    fullname: Davidson
– volume: 94
  start-page: 428
  year: 1997
  end-page: 432
  ident: bib47
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  contributor:
    fullname: Kozasa
– volume: 198
  start-page: 2185
  year: 1995
  end-page: 2196
  ident: bib55
  publication-title: J. Exp. Biol.
  contributor:
    fullname: DeMont
– volume: 17
  start-page: 754
  year: 2001
  end-page: 755
  ident: bib63
  publication-title: Bioinformatics
  contributor:
    fullname: Ronquist
– volume: 9
  start-page: 1506
  year: 2003
  end-page: 1512
  ident: bib13
  publication-title: Nat. Med.
  contributor:
    fullname: Wang
– volume: 7
  start-page: 1236
  year: 2001
  end-page: 1240
  ident: bib25
  publication-title: Nat. Med.
  contributor:
    fullname: Offermanns
– volume: 340
  start-page: 341
  year: 2005
  end-page: 351
  ident: bib38
  publication-title: Anal. Biochem.
  contributor:
    fullname: Siderovski
– volume: 53
  start-page: 240
  year: 1997
  end-page: 255
  ident: bib34
  publication-title: Acta Crystallogr. D Biol. Crystallogr.
  contributor:
    fullname: Dodson
– volume: 273
  start-page: 12794
  year: 1998
  end-page: 12797
  ident: bib41
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Neubig
– volume: 101
  start-page: 13273
  year: 2004
  end-page: 13278
  ident: bib53
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  contributor:
    fullname: Cooper
– volume: 79
  start-page: 177
  year: 2002
  end-page: 185
  ident: bib50
  publication-title: Genomics
  contributor:
    fullname: Wilkie
– volume: 20
  start-page: 1661
  year: 2001
  end-page: 1668
  ident: bib5
  publication-title: Oncogene
  contributor:
    fullname: Gutkind
– volume: 310
  start-page: 1686
  year: 2005
  end-page: 1690
  ident: bib8
  publication-title: Science
  contributor:
    fullname: Tesmer
– volume: 111
  start-page: 445
  year: 2003
  end-page: 452
  ident: bib12
  publication-title: J. Clin. Invest.
  contributor:
    fullname: Blumer
– volume: 78
  start-page: 364
  year: 1996
  end-page: 369
  ident: bib65
  publication-title: Biochimie
  contributor:
    fullname: Gouy
– year: 2009
  ident: bib10
  publication-title: Handbook of Cell Signaling
  contributor:
    fullname: Siderovski
– volume: 60
  start-page: 432
  year: 2004
  end-page: 438
  ident: bib33
  publication-title: Acta Crystallogr. D Biol. Crystallogr.
  contributor:
    fullname: Read
– volume: 3
  start-page: 639
  year: 2002
  ident: 10.1074/jbc.M109.024711_bib1
  publication-title: Nat. Rev. Mol. Cell Biol.
  doi: 10.1038/nrm908
  contributor:
    fullname: Pierce
– volume: 24
  start-page: 1115
  year: 2006
  ident: 10.1074/jbc.M109.024711_bib15
  publication-title: J. Hypertens.
  doi: 10.1097/01.hjh.0000226202.80689.8f
  contributor:
    fullname: Semplicini
– volume: 9
  start-page: 1506
  year: 2003
  ident: 10.1074/jbc.M109.024711_bib13
  publication-title: Nat. Med.
  doi: 10.1038/nm958
  contributor:
    fullname: Tang
– volume: 310
  start-page: 1686
  year: 2005
  ident: 10.1074/jbc.M109.024711_bib8
  publication-title: Science
  doi: 10.1126/science.1118890
  contributor:
    fullname: Tesmer
– volume: 1774
  start-page: 1213
  year: 2007
  ident: 10.1074/jbc.M109.024711_bib26
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/j.bbapap.2007.06.002
  contributor:
    fullname: Kimple
– year: 2006
  ident: 10.1074/jbc.M109.024711_bib56
  contributor:
    fullname: Evans
– volume: 105
  start-page: 6457
  year: 2008
  ident: 10.1074/jbc.M109.024711_bib20
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  doi: 10.1073/pnas.0801508105
  contributor:
    fullname: Soundararajan
– volume: 119
  start-page: 408
  year: 2009
  ident: 10.1074/jbc.M109.024711_bib23
  publication-title: J. Clin. Invest.
  contributor:
    fullname: Takimoto
– volume: 94
  start-page: 12851
  year: 1997
  ident: 10.1074/jbc.M109.024711_bib43
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  doi: 10.1073/pnas.94.24.12851
  contributor:
    fullname: Druey
– year: 2009
  ident: 10.1074/jbc.M109.024711_bib10
  contributor:
    fullname: Willard
– volume: 105
  start-page: 6243
  year: 2008
  ident: 10.1074/jbc.M109.024711_bib45
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  doi: 10.1073/pnas.0801569105
  contributor:
    fullname: Slep
– volume: 274
  start-page: 8770
  year: 1999
  ident: 10.1074/jbc.M109.024711_bib46
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.274.13.8770
  contributor:
    fullname: Skiba
– volume: 19
  start-page: 1572
  year: 2003
  ident: 10.1074/jbc.M109.024711_bib64
  publication-title: Bioinformatics
  doi: 10.1093/bioinformatics/btg180
  contributor:
    fullname: Ronquist
– volume: 18
  start-page: 16
  year: 2007
  ident: 10.1074/jbc.M109.024711_bib52
  publication-title: Semin. Cell Dev. Biol.
  doi: 10.1016/j.semcdb.2006.12.007
  contributor:
    fullname: Davidson
– volume: 353
  start-page: 147
  year: 2006
  ident: 10.1074/jbc.M109.024711_bib30
  publication-title: Anal. Biochem.
  doi: 10.1016/j.ab.2006.02.004
  contributor:
    fullname: Willard
– volume: 20
  start-page: 1661
  year: 2001
  ident: 10.1074/jbc.M109.024711_bib5
  publication-title: Oncogene
  doi: 10.1038/sj.onc.1204182
  contributor:
    fullname: Fukuhara
– volume: 273
  start-page: 1529
  year: 1998
  ident: 10.1074/jbc.M109.024711_bib44
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.273.3.1529
  contributor:
    fullname: Srinivasa
– volume: 53
  start-page: 396
  year: 2007
  ident: 10.1074/jbc.M109.024711_bib27
  publication-title: Protein Expr. Purif.
  doi: 10.1016/j.pep.2007.01.013
  contributor:
    fullname: Stols
– volume: 94
  start-page: 428
  year: 1997
  ident: 10.1074/jbc.M109.024711_bib47
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  doi: 10.1073/pnas.94.2.428
  contributor:
    fullname: Hepler
– volume: 275
  start-page: 28500
  year: 2000
  ident: 10.1074/jbc.M109.024711_bib40
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M004187200
  contributor:
    fullname: Wieland
– volume: 70
  start-page: 281
  year: 2001
  ident: 10.1074/jbc.M109.024711_bib6
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev.biochem.70.1.281
  contributor:
    fullname: Rhee
– volume: 60
  start-page: 2126
  year: 2004
  ident: 10.1074/jbc.M109.024711_bib35
  publication-title: Acta Crystallogr. D Biol. Crystallogr.
  doi: 10.1107/S0907444904019158
  contributor:
    fullname: Emsley
– volume: 97
  start-page: 12272
  year: 2000
  ident: 10.1074/jbc.M109.024711_bib16
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  doi: 10.1073/pnas.220414397
  contributor:
    fullname: Oliveira-Dos-Santos
– volume: 340
  start-page: 341
  year: 2005
  ident: 10.1074/jbc.M109.024711_bib38
  publication-title: Anal. Biochem.
  doi: 10.1016/j.ab.2005.02.015
  contributor:
    fullname: Willard
– volume: 273
  start-page: 12794
  year: 1998
  ident: 10.1074/jbc.M109.024711_bib41
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.273.21.12794
  contributor:
    fullname: Lan
– volume: 6
  start-page: 211
  year: 1996
  ident: 10.1074/jbc.M109.024711_bib11
  publication-title: Curr. Biol.
  doi: 10.1016/S0960-9822(02)00454-2
  contributor:
    fullname: Siderovski
– volume: 274
  start-page: 34253
  year: 1999
  ident: 10.1074/jbc.M109.024711_bib21
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.274.48.34253
  contributor:
    fullname: Heximer
– volume: 60
  start-page: 432
  year: 2004
  ident: 10.1074/jbc.M109.024711_bib33
  publication-title: Acta Crystallogr. D Biol. Crystallogr.
  doi: 10.1107/S0907444903028956
  contributor:
    fullname: Storoni
– volume: 65
  start-page: 298
  year: 2008
  ident: 10.1074/jbc.M109.024711_bib19
  publication-title: Arch. Gen. Psychiatry
  doi: 10.1001/archgenpsychiatry.2007.48
  contributor:
    fullname: Smoller
– volume: 111
  start-page: 445
  year: 2003
  ident: 10.1074/jbc.M109.024711_bib12
  publication-title: J. Clin. Invest.
  doi: 10.1172/JCI15598
  contributor:
    fullname: Heximer
– volume: 40
  start-page: 660
  year: 2002
  ident: 10.1074/jbc.M109.024711_bib22
  publication-title: Hypertension
  doi: 10.1161/01.HYP.0000035397.73223.CE
  contributor:
    fullname: Keys
– volume: 62
  start-page: 439
  year: 2006
  ident: 10.1074/jbc.M109.024711_bib36
  publication-title: Acta Crystallogr. D Biol. Crystallogr.
  doi: 10.1107/S0907444906005270
  contributor:
    fullname: Painter
– volume: 79
  start-page: 177
  year: 2002
  ident: 10.1074/jbc.M109.024711_bib50
  publication-title: Genomics
  doi: 10.1006/geno.2002.6693
  contributor:
    fullname: Sierra
– volume: 101
  start-page: 13273
  year: 2004
  ident: 10.1074/jbc.M109.024711_bib53
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  doi: 10.1073/pnas.0405529101
  contributor:
    fullname: Pancer
– volume: 33
  start-page: 1537
  year: 2008
  ident: 10.1074/jbc.M109.024711_bib18
  publication-title: Neuropsychopharmacology
  doi: 10.1038/sj.npp.1301557
  contributor:
    fullname: Cui
– volume: 94
  start-page: 7216
  year: 1997
  ident: 10.1074/jbc.M109.024711_bib39
  publication-title: Proc. Natl. Acad. Sci. U.S.A.
  doi: 10.1073/pnas.94.14.7216
  contributor:
    fullname: Popov
– volume: 89
  start-page: 251
  year: 1997
  ident: 10.1074/jbc.M109.024711_bib42
  publication-title: Cell
  doi: 10.1016/S0092-8674(00)80204-4
  contributor:
    fullname: Tesmer
– volume: 19
  start-page: 428
  year: 2007
  ident: 10.1074/jbc.M109.024711_bib29
  publication-title: Cell. Signal.
  doi: 10.1016/j.cellsig.2006.07.013
  contributor:
    fullname: Willard
– volume: 62
  start-page: 551
  year: 2005
  ident: 10.1074/jbc.M109.024711_bib3
  publication-title: Cell Mol. Life Sci.
  doi: 10.1007/s00018-004-4462-3
  contributor:
    fullname: McCudden
– volume: 55
  start-page: 1696
  year: 1999
  ident: 10.1074/jbc.M109.024711_bib31
  publication-title: Acta Crystallogr. D Biol. Crystallogr.
  doi: 10.1107/S090744499900846X
  contributor:
    fullname: Leslie
– volume: 83
  start-page: 101
  year: 2003
  ident: 10.1074/jbc.M109.024711_bib2
  publication-title: Prog. Biophys. Mol. Biol.
  doi: 10.1016/S0079-6107(03)00052-X
  contributor:
    fullname: Offermanns
– volume: 21
  start-page: 285
  year: 2004
  ident: 10.1074/jbc.M109.024711_bib51
  publication-title: Zool. Sci.
  doi: 10.2108/zsj.21.285
  contributor:
    fullname: Chiba
– volume: 409
  start-page: 1051
  year: 2001
  ident: 10.1074/jbc.M109.024711_bib37
  publication-title: Nature
  doi: 10.1038/35059104
  contributor:
    fullname: Sinnarajah
– volume: 280
  start-page: 574
  year: 1998
  ident: 10.1074/jbc.M109.024711_bib24
  publication-title: Science
  doi: 10.1126/science.280.5363.574
  contributor:
    fullname: Akhter
– volume: 48
  start-page: 646
  year: 1999
  ident: 10.1074/jbc.M109.024711_bib49
  publication-title: J. Mol. Evol.
  doi: 10.1007/PL00006508
  contributor:
    fullname: Suga
– volume: 1401
  start-page: 93
  year: 1998
  ident: 10.1074/jbc.M109.024711_bib48
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/S0167-4889(97)00121-3
  contributor:
    fullname: Seack
– volume: 73
  start-page: 1037
  year: 2008
  ident: 10.1074/jbc.M109.024711_bib14
  publication-title: Mol. Pharmacol.
  doi: 10.1124/mol.107.044214
  contributor:
    fullname: Gu
– year: 2007
  ident: 10.1074/jbc.M109.024711_bib54
  contributor:
    fullname: McKenzie
– volume: 389
  start-page: 71
  year: 2004
  ident: 10.1074/jbc.M109.024711_bib59
  publication-title: Methods Enzymol.
  doi: 10.1016/S0076-6879(04)89005-0
  contributor:
    fullname: Hains
– volume: 17
  start-page: 754
  year: 2001
  ident: 10.1074/jbc.M109.024711_bib63
  publication-title: Bioinformatics
  doi: 10.1093/bioinformatics/17.8.754
  contributor:
    fullname: Huelsenbeck
– volume: 2
  start-page: 168
  year: 2002
  ident: 10.1074/jbc.M109.024711_bib4
  publication-title: Mol. Interv.
  doi: 10.1124/mi.2.3.168
  contributor:
    fullname: Sunahara
– volume: 7
  start-page: 1236
  year: 2001
  ident: 10.1074/jbc.M109.024711_bib25
  publication-title: Nat. Med.
  doi: 10.1038/nm1101-1236
  contributor:
    fullname: Wettschureck
– volume: 12
  start-page: 543
  year: 1996
  ident: 10.1074/jbc.M109.024711_bib62
  publication-title: Comput. Appl. Biosci.
  contributor:
    fullname: Galtier
– volume: 62
  start-page: 654
  year: 2002
  ident: 10.1074/jbc.M109.024711_bib58
  publication-title: Mol. Pharmacol.
  doi: 10.1124/mol.62.3.654
  contributor:
    fullname: Cladman
– volume: 198
  start-page: 2185
  year: 1995
  ident: 10.1074/jbc.M109.024711_bib55
  publication-title: J. Exp. Biol.
  doi: 10.1242/jeb.198.10.2185
  contributor:
    fullname: Davison
– volume: 54
  start-page: 527
  year: 2002
  ident: 10.1074/jbc.M109.024711_bib9
  publication-title: Pharmacol. Rev.
  doi: 10.1124/pr.54.3.527
  contributor:
    fullname: Hollinger
– volume: 36
  start-page: 1197
  year: 2004
  ident: 10.1074/jbc.M109.024711_bib17
  publication-title: Nat. Genet.
  doi: 10.1038/ng1450
  contributor:
    fullname: Yalcin
– start-page: 114
  year: 1993
  ident: 10.1074/jbc.M109.024711_bib32
  contributor:
    fullname: Evans
– volume: 389
  start-page: 56
  year: 2004
  ident: 10.1074/jbc.M109.024711_bib28
  publication-title: Methods Enzymol.
  doi: 10.1016/S0076-6879(04)89004-9
  contributor:
    fullname: Willard
– volume: 2007
  start-page: pe2
  year: 2007
  ident: 10.1074/jbc.M109.024711_bib60
  publication-title: Sci. STKE
  doi: 10.1126/stke.3702007pe2
  contributor:
    fullname: Heximer
– volume: 78
  start-page: 364
  year: 1996
  ident: 10.1074/jbc.M109.024711_bib65
  publication-title: Biochimie
  doi: 10.1016/0300-9084(96)84768-7
  contributor:
    fullname: Perrière
– volume: 302
  start-page: 205
  year: 2000
  ident: 10.1074/jbc.M109.024711_bib61
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.2000.4042
  contributor:
    fullname: Notredame
– volume: 53
  start-page: 240
  year: 1997
  ident: 10.1074/jbc.M109.024711_bib34
  publication-title: Acta Crystallogr. D Biol. Crystallogr.
  doi: 10.1107/S0907444996012255
  contributor:
    fullname: Murshudov
– volume: 18
  start-page: 7178
  year: 1998
  ident: 10.1074/jbc.M109.024711_bib57
  publication-title: J. Neurosci.
  doi: 10.1523/JNEUROSCI.18-18-07178.1998
  contributor:
    fullname: Ingi
– volume: 318
  start-page: 1923
  year: 2007
  ident: 10.1074/jbc.M109.024711_bib7
  publication-title: Science
  doi: 10.1126/science.1147554
  contributor:
    fullname: Lutz
SSID ssj0000491
Score 2.263739
Snippet “Regulator of G-protein signaling” (RGS) proteins facilitate the termination of G protein-coupled receptor (GPCR) signaling via their ability to increase the...
"Regulator of G-protein signaling" (RGS) proteins facilitate the termination of G protein-coupled receptor (GPCR) signaling via their ability to increase the...
SourceID pubmedcentral
proquest
crossref
pubmed
fao
elsevier
SourceType Open Access Repository
Aggregation Database
Index Database
Publisher
StartPage 19402
SubjectTerms Binding Sites - genetics
Cell Line
Evolution, Molecular
Fluorescence Resonance Energy Transfer
GTP-Binding Protein alpha Subunits - genetics
GTP-Binding Protein alpha Subunits - metabolism
Guanosine Triphosphate - metabolism
Humans
Hydrolysis
Luminescent Proteins - genetics
Luminescent Proteins - metabolism
Mechanisms of Signal Transduction
Models, Molecular
Point Mutation
Protein Binding
Protein Interaction Domains and Motifs
Protein Structure, Tertiary
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
RGS Proteins - chemistry
RGS Proteins - genetics
RGS Proteins - metabolism
Surface Plasmon Resonance
Transfection
Title Structural Determinants of G-protein α Subunit Selectivity by Regulator of G-protein Signaling 2 (RGS2)
URI https://dx.doi.org/10.1074/jbc.M109.024711
https://www.ncbi.nlm.nih.gov/pubmed/19478087
https://search.proquest.com/docview/67476460
https://pubmed.ncbi.nlm.nih.gov/PMC2740565
Volume 284
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Nb9QwEB11e4ELghZo-Cg-IFQO2c16bcd7rBbaCrQIGlbqzXLseLuIdSpoD_1Z_BF-E2Mnhi4qFy45JHEUecYzb-KXNwAvg8jZxGidWydEzgK_seY6yOOVrNGaNzr2Iph_ECcL9u6Mn20BT__CRNK-qVdD_3U99KvzyK28WJtR4omNPs5n-BzM23w0gAGm31Sip_DL-jZ5gXtAuUx6PiUbfanNcD4OCpUUY3JsEjNlpSwCn-72rDRwur0Ne_5NobyRk47uw70eTJLD7qUfwFbjd2D30GMhvb4mr0ikd8bv5jtwZ5Zau-3CeRVVY4PiBnlzgw9DWkeO8yjdsPLk5w-CYeUK1zypYrec2GeC1NfktGtg337bHFCtlgHW-yWh5OD0uKKvH8Li6O3n2Unet1zIDRP8MmfO6nFpnZ1QGUqLEk9wao2UWMvSqTOM1cZMHZ9YLoOUmaXGCASJBnGc1XbyCLZ965s9IIV0tNA1E1pPEfUZicGkKdhYy8ZpBFoZHKQpVxedsoaKO-IlU2goFQylOkNlQJNJVA8MuoSvMO7_e9AeGk_pJQZLtaho2KIdC44HmsGLZFGFMx-2SLRv2qvvSmB1JZgoMnjc2ffPq_WekkG5YfnfNwSd7s0r6L5Rr7t31yf_PfIp3O02sYKe5zPYRh9pniMWuqz3YfD-k9yPK-AX76IHfA
link.rule.ids 230,314,727,780,784,885,27924,27925,53791,53793
linkProvider National Library of Medicine
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1NT9wwEB0BPdBL1UJb0i98qCp6yG7i2E5yREth27KoIqzEzXKceNmq6yA-Dvws_gi_qWMnoWxFL73kkMRR5BmP32Re3gB8dCJniVYqrIwQIXP8xpIrJ4-XslopXivfi2ByJMZT9u2Un64A7_-F8aR9Xc4H9tdiYOdnnlt5vtDDnic2_DEZ4XNw3-bDVXjCkzSP-yS9D8Csa5Tn2AeUZ72iT8qGP0s9mMROo5JiVPZtYnKWZpFj1D2-L60a1TyGPv8mUT7Ylfafw7MOTpLd9rVfwEptN2Bz12Iqvbghn4gnePov5xuwPuqbu23CWeF1Y53mBtl7wIghjSEHoRdvmFtyd0swsFzjqieF75fjO02Q8oYcty3sm4vlAcV85oC9nRFKdo4PCvr5JUz3v5yMxmHXdCHUTPCrkJlKxWllqoRmLrlI8QSnlc4yzGZpbjRjpda54UnFMydmVlGtBcJEjUiuUlXyCtZsY-stIFFmaKRKJpTKEffpDMNJHbFYZbVRCLUC2OmnXJ632hrS18RTJtFQ0hlKtoYKgPYmkR00aLd8iZH_34O20HhSzTBcymlBXZE2FhwPNIDt3qISZ94VSZStm-tLKTC_EkxEAbxu7fvn1TpPCSBdsvz9DU6pe_kKOrBX7O4c9s1_j9yG9fHJ5FAefj36_haetiUtp-75DtbQX-r3iIyuyg9-HfwGupIJ3A
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Nb9QwEB3RIgEXVFpoUyj1AaFyyCbr2E72WG3Zlo-tqoaVerMcO94u6iarfhz6s_gj_CbGTgK7qFy45JDEUeSZjN_ET-8BvHMiZ4lWKjRWiJA5fmPBlZPHS1mpFC-V9yIYn4qTCft8wS-WrL48aV8Xs151Ne9Vs0vPrVzMddTxxKKz8RCfg-s2jxbGRmvwmCeYZF2j3hVh1prlOQYC5Vmn6pOy6Huhe-O-06mkWJm9VcyApVnsWHUPr01rVtUPIdC_iZRLK9NoA563kJIcNq_-Ah6V1SZsHVbYTs_vyXviSZ7-7_kmPB12Bm9bcJl77Vinu0GOllgxpLbkOPQCDrOK_PxBsLjc4ZdPcu-Z490mSHFPzhsb-_p6dUA-mzpwX00JJQfnxzn98BImo4_fhidha7wQaib4bcisUf3UWJPQzDUYKZ7g1Ogsw46WDqxmrNB6YHlieOYEzQzVWiBU1IjmjDLJK1iv6qrcARJnlsaqYEKpAWI_nWFJKWPWV1lpFcKtAA66KZeLRl9D-n3xlEkMlHSBkk2gAqBdSGQLD5plX2L1__egHQyeVFMsmXKSU7dR2xccDzSA_S6iEmfebZSoqqzvbqTAHkswEQew3cT3z6u1mRJAuhL53zc4te7VK5jEXrW7Tdrd_x65D0_Ojkby66fTL6_hWbOr5QQ-38A6pku5h-DotnjrP4NflfcK7w
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=Structural+Determinants+of+G-protein+%CE%B1+Subunit+Selectivity+by+Regulator+of+G-protein+Signaling+2+%28RGS2%29&rft.jtitle=The+Journal+of+biological+chemistry&rft.au=Kimple%2C+Adam+J.&rft.au=Soundararajan%2C+Meera&rft.au=Hutsell%2C+Stephanie+Q.&rft.au=Roos%2C+Annette+K.&rft.date=2009-07-17&rft.pub=American+Society+for+Biochemistry+and+Molecular+Biology&rft.issn=0021-9258&rft.eissn=1083-351X&rft.volume=284&rft.issue=29&rft.spage=19402&rft.epage=19411&rft_id=info:doi/10.1074%2Fjbc.M109.024711&rft_id=info%3Apmid%2F19478087&rft.externalDBID=PMC2740565
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0021-9258&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0021-9258&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0021-9258&client=summon