최소 단어 이상 선택하여야 합니다.
최대 10 단어까지만 선택 가능합니다.
다음과 같은 기능을 한번의 로그인으로 사용 할 수 있습니다.
NTIS 바로가기Cell, v.177 no.5, 2019년, pp.1232 - 1242.e11
Du, Yang (Molecular and Cellular Physiology, School of Medicine, Stanford University) , Duc, Nguyen Minh (School of Pharmacy, Sungkyunkwan University) , Rasmussen, Søren G.F. (Department of Neuroscience, University of Copenhagen) , Hilger, Daniel (Molecular and Cellular Physiology, School of Medicine, Stanford University) , Kubiak, Xavier (Department of Neuroscience, University of Copenhagen) , Wang, Liwen (Department of Nutrition, Center for Proteomics and Bioinformatics, School of Medicine, Case Western Reserve University) , Bohon, Jennifer (Department of Nutrition, Center for Proteomics and Bioinformatics, School of Medicine, Case Western Reserve University) , Kim, Hee Ryung (School of Pharmacy, Sungkyunkwan University) , Wegrecki, Marcin (Department of Neuroscience, University of Copenhagen) , Asuru, Awuri (Department of Nutrition, Center for Proteomics and Bioinformatics, School of Medicine, Case Western) , Jeong, Kyung Min , Lee, Jeongmi , Chance, Mark R. , Lodowski, David T. , Kobilka, Brian K. , Chung, Ka Young
Summary The activation of G proteins by G protein-coupled receptors (GPCRs) underlies the majority of transmembrane signaling by hormones and neurotransmitters. Recent structures of GPCR-G protein complexes obtained by crystallography and cryoelectron microscopy (cryo-EM) reveal similar interaction...
Nat. Struct. Mol. Biol. Alexander 21 56 2014 10.1038/nsmb.2705 Energetic analysis of the rhodopsin-G-protein complex links the α5 helix to GDP release
Proc. Natl. Acad. Sci. USA Angel 106 14367 2009 10.1073/pnas.0901074106 Structural waters define a functional channel mediating activation of the GPCR, rhodopsin
J Synch Rad. Asuru 26 2019 The XFP (17-BM) beamline for X-ray footprinting at NSLS-II
Biochem. Soc. Trans. Bavro 43 983 2015 10.1042/BST20150130 Oxidative footprinting in the study of structure and function of membrane proteins: current state and perspectives
Methods Calabrese 147 187 2018 10.1016/j.ymeth.2018.02.020 Mass spectrometry-enabled structural biology of membrane proteins
Nature Carpenter 536 104 2016 10.1038/nature18966 Structure of the adenosine A(2A) receptor bound to an engineered G protein
Nature Chung 477 611 2011 10.1038/nature10488 Conformational changes in the G protein Gs induced by the β2 adrenergic receptor
Mol. Endocrinol. DeMars 25 1416 2011 10.1210/me.2011-0009 The extreme C-terminal region of Gαs differentially couples to the luteinizing hormone and beta2-adrenergic receptors
J. Am. Chem. Soc. Denisov 126 3477 2004 10.1021/ja0393574 Directed self-assembly of monodisperse phospholipid bilayer Nanodiscs with controlled size
Nature Draper-Joyce 558 559 2018 10.1038/s41586-018-0236-6 Structure of the adenosine-bound human adenosine A1 receptor-Gi complex
Science Dror 348 1361 2015 10.1126/science.aaa5264 SIGNAL TRANSDUCTION. Structural basis for nucleotide exchange in heterotrimeric G proteins
J. Am. Soc. Mass Spectrom. Duc 26 808 2015 10.1007/s13361-015-1083-4 Effective application of bicelles for conformational analysis of G protein-coupled receptors by hydrogen/deuterium exchange mass spectrometry
Nature Garcia-Nafria 558 620 2018 10.1038/s41586-018-0241-9 Cryo-EM structure of the serotonin 5-HT1B receptor coupled to heterotrimeric Go
Nature Gregorio 547 68 2017 10.1038/nature22354 Single-molecule analysis of ligand efficacy in β2AR-G-protein activation
J. Synchrotron Radiat. Gupta 14 233 2007 10.1107/S0909049507013118 The Beamline X28C of the Center for Synchrotron Biosciences: a national resource for biomolecular structure and dynamics experiments using synchrotron footprinting
Nature Gupta 512 101 2014 10.1038/nature13382 Visualizing the kinetic power stroke that drives proton-coupled zinc(II) transport
Curr. Opin. Struct. Biol. Harrison 41 187 2016 10.1016/j.sbi.2016.08.003 Conformational insight into multi-protein signaling assemblies by hydrogen-deuterium exchange mass spectrometry
Nature Kang 523 561 2015 10.1038/nature14656 Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser
Nature Kang 558 553 2018 10.1038/s41586-018-0215-y Cryo-EM structure of human rhodopsin bound to an inhibitory G protein
J. Biol. Chem. Kaya 289 24475 2014 10.1074/jbc.M114.572875 A conserved phenylalanine as a relay between the α5 helix and the GDP binding region of heterotrimeric Gi protein α subunit
J. Struct. Biol. Kim 190 250 2015 10.1016/j.jsb.2015.04.006 Different conformational dynamics of various active states of β-arrestin1 analyzed by hydrogen/deuterium exchange mass spectrometry
Annu. Rev. Biophys. Kiselar 47 1 2018 10.1146/annurev-biophys-070317-033123 High-Resolution Hydroxyl Radical Protein Footprinting: Biophysics Tool for Drug Discovery
Nature Koehl 558 547 2018 10.1038/s41586-018-0219-7 Structure of the μ-opioid receptor-Gi protein complex
Mass Spectrom. Rev. Konermann 22 1 2003 10.1002/mas.10044 Protein-folding kinetics and mechanisms studied by pulse-labeling and mass spectrometry
J. Mass Spectrom. Konermann 43 1021 2008 10.1002/jms.1435 Protein structure and dynamics studied by mass spectrometry: H/D exchange, hydroxyl radical labeling, and related approaches
Acta Physiol. (Oxf.) Lefkowitz 190 9 2007 10.1111/j.1365-201X.2007.01693.x Seven transmembrane receptors: something old, something new
Nature Liang 546 118 2017 10.1038/nature22327 Phase-plate cryo-EM structure of a class B GPCR-G-protein complex
Cell Liu 177 1243 2019 10.1016/j.cell.2019.04.021 Structural insights into the process of GPCR-G protein complex formation
Science Markby 262 1895 1993 10.1126/science.8266082 Separate GTP binding and GTPase activating domains of a G alpha subunit
J. Biol. Chem. Moro 268 22273 1993 10.1016/S0021-9258(18)41524-4 Hydrophobic amino acid in the i2 loop plays a key role in receptor-G protein coupling
Mol. Pharmacol. Nanoff 69 397 2006 10.1124/mol.105.016725 The carboxyl terminus of the Galpha-subunit is the latch for triggered activation of heterotrimeric G proteins
Nat. Struct. Mol. Biol. Oldham 13 772 2006 10.1038/nsmb1129 Mechanism of the receptor-catalyzed activation of heterotrimeric G proteins
Proc. Natl. Acad. Sci. USA Oldham 104 7927 2007 10.1073/pnas.0702623104 Mapping allosteric connections from the receptor to the nucleotide-binding pocket of heterotrimeric G proteins
Structure Orban 20 826 2012 10.1016/j.str.2012.03.017 Conformational dynamics of activation for the pentameric complex of dimeric G protein-coupled receptor and heterotrimeric G protein
J. Mol. Biol. Preininger 425 2288 2013 10.1016/j.jmb.2013.04.011 Conformational flexibility and structural dynamics in GPCR-mediated G protein activation: a perspective
Annu. Rev. Physiol. Pryor 48 657 1986 10.1146/annurev.ph.48.030186.003301 Oxy-radicals and related species: their formation, lifetimes, and reactions
Methods Rajabi 89 13 2015 10.1016/j.ymeth.2015.03.004 Mass spectrometric methods to analyze the structural organization of macromolecular complexes
Nature Rasmussen 477 549 2011 10.1038/nature10361 Crystal structure of the β2 adrenergic receptor-Gs protein complex
Science Rosenbaum 318 1266 2007 10.1126/science.1150609 GPCR engineering yields high-resolution structural insights into beta2-adrenergic receptor function
Proc. Natl. Acad. Sci. USA Scheerer 106 10660 2009 10.1073/pnas.0900072106 Structural and kinetic modeling of an activating helix switch in the rhodopsin-transducin interface
Mol. Pharmacol. Swaminath 61 65 2002 10.1124/mol.61.1.65 Allosteric modulation of beta2-adrenergic receptor by Zn(2+)
Mol. Cell. Biochem. Traut 140 1 1994 10.1007/BF00928361 Physiological concentrations of purines and pyrimidines
Proc. Natl. Acad. Sci. USA Van Eps 108 9420 2011 10.1073/pnas.1105810108 Interaction of a G protein with an activated receptor opens the interdomain interface in the alpha subunit
Mol. Cell. Proteomics Wang 16 706 2017 10.1074/mcp.O116.064386 Protein Footprinting Comes of Age: Mass Spectrometry for Biophysical Structure Assessment
Proc. Natl. Acad. Sci. USA Westfield 108 16086 2011 10.1073/pnas.1113645108 Structural flexibility of the G alpha s alpha-helical domain in the beta2-adrenoceptor Gs complex
Proc. Natl. Acad. Sci. USA Whorton 104 7682 2007 10.1073/pnas.0611448104 A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein
BMC Bioinformatics Xu 8 133 2007 10.1186/1471-2105-8-133 A mass accuracy sensitive probability based scoring algorithm for database searching of tandem mass spectrometry data
Anal. Chem. Xu 77 3029 2005 10.1021/ac048282z Secondary reactions and strategies to improve quantitative protein footprinting
J. Proteome Res. Xu 7 138 2008 10.1021/pr070363z Identification and characterization of disulfide bonds in proteins and peptides from tandem MS data by use of the MassMatrix MS/MS search engine
Science Xu 332 322 2011 10.1126/science.1202793 Structure of an agonist-bound human A2A adenosine receptor
Biochim Biophys Acta Mol Cell Biol Lipids Yano 1862 615 2017 10.1016/j.bbalip.2017.03.006 An aromatic amino acid within intracellular loop 2 of the prostaglandin EP2 receptor is a prerequisite for selective association and activation of Gαs
Proc. Natl. Acad. Sci. USA Yao 106 9501 2009 10.1073/pnas.0811437106 The effect of ligand efficacy on the formation and stability of a GPCR-G protein complex
Nature Zhang 546 248 2017 10.1038/nature22394 Cryo-EM structure of the activated GLP-1 receptor in complex with a G protein
Structure Zheng 16 38 2008 10.1016/j.str.2007.10.019 Complementary structural mass spectrometry techniques reveal local dynamics in functionally important regions of a metastable serpin
Biochem. Biophys. Res. Commun. Zhou 264 171 1999 10.1006/bbrc.1999.1508 Phenylalanine 138 in the second intracellular loop of human thromboxane receptor is critical for receptor-G-protein coupling
*원문 PDF 파일 및 링크정보가 존재하지 않을 경우 KISTI DDS 시스템에서 제공하는 원문복사서비스를 사용할 수 있습니다.
출판사/학술단체 등이 한시적으로 특별한 프로모션 또는 일정기간 경과 후 접근을 허용하여, 출판사/학술단체 등의 사이트에서 이용 가능한 논문
※ AI-Helper는 부적절한 답변을 할 수 있습니다.