-
1
-
-
84855799592
-
Diversity and modularity of G protein-coupled receptor structures
-
Elsevier Ltd
-
Katritch V, Cherezov V, Stevens RC. Diversity and modularity of G protein-coupled receptor structures. Trends Pharmacol Sci. Elsevier Ltd; 2012; 33: 17-27. doi: 10.1016/j.tips.2011.09.003
-
(2012)
Trends Pharmacol Sci.
, vol.33
, pp. 17-27
-
-
Katritch, V.1
Cherezov, V.2
Stevens, R.C.3
-
2
-
-
37549016836
-
Heterotrimeric G protein activation by G-protein-coupled receptors
-
PMID: 18043707
-
Oldham WM, Hamm HE. Heterotrimeric G protein activation by G-protein-coupled receptors. Nat Rev Mol Cell Biol. 2008; 9: 60-71. doi: 10.1038/nrm2299 PMID: 18043707
-
(2008)
Nat Rev Mol Cell Biol.
, vol.9
, pp. 60-71
-
-
Oldham, W.M.1
Hamm, H.E.2
-
3
-
-
80051658642
-
Crystal structure of the ?2 adrenergic receptor-Gs protein complex
-
2011/07/21 ed. PMID: 21772288
-
Rasmussen SGF, DeVree BT, Zou Y, Kruse AC, Chung KY, Kobilka TS, et al. Crystal structure of the ?2 adrenergic receptor-Gs protein complex. Nature. 2011/07/21 ed. 2011; 477: 549-55. doi: 10.1038/nature10361 PMID: 21772288
-
(2011)
Nature.
, vol.477
, pp. 549-555
-
-
Rasmussen, S.G.F.1
DeVree, B.T.2
Zou, Y.3
Kruse, A.C.4
Chung, K.Y.5
Kobilka, T.S.6
-
4
-
-
0029907599
-
Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
-
Department of Biology Massachusetts Institute of Technology Cambridge MA 02139 USA. Available
-
Farrens DL, Altenbach C, Yang K, Hubbell WL, Khorana HG. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science (80-). Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.; 1996; 274: 768-770. Available: Http://www.ncbi.nlm.nih.gov/pubmed/8864113
-
(1996)
Science (80-)
, vol.274
, pp. 768-770
-
-
Farrens, D.L.1
Altenbach, C.2
Yang, K.3
Hubbell, W.L.4
Khorana, H.G.5
-
5
-
-
52949102889
-
Crystal structure of opsin in its G-protein-interacting conformation
-
Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany.: Nature Publishing Group Available
-
Scheerer P, Park JH, Hildebrand PW, Kim YJ, Krauss N, Choe H-W, et al. Crystal structure of opsin in its G-protein-interacting conformation. Nature. Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany.: Nature Publishing Group; 2008; 455: 497-502. Available: Http://www.nature.com/nature/journal/v455/n7212/abs/nature07330.html
-
(2008)
Nature
, vol.455
, pp. 497-502
-
-
Scheerer, P.1
Park, J.H.2
Hildebrand, P.W.3
Kim, Y.J.4
Krauss, N.5
Choe, H.-W.6
-
6
-
-
84889564886
-
Activation and allosteric modulation of a muscarinic acetylcholine receptor
-
Nature Publishing Group
-
Kruse AC, Ring AM, Manglik A, Hu J, Hu K, Eitel K, et al. Activation and allosteric modulation of a muscarinic acetylcholine receptor. Nature. Nature Publishing Group; 2013; 504: 101-6. doi: 10.1038/nature12735
-
(2013)
Nature
, vol.504
, pp. 101-106
-
-
Kruse, A.C.1
Ring, A.M.2
Manglik, A.3
Hu, J.4
Hu, K.5
Eitel, K.6
-
7
-
-
0029593456
-
The structure of the G protein heterotrimer Gi?1?1?2
-
Wall MA, Coleman DE, Lee E, Iñiguez-Lluhi JA, Posner BA, Gilman AG, et al. The structure of the G protein heterotrimer Gi?1?1?2. Cell. 1995; 83: 1047-1058.
-
(1995)
Cell.
, vol.83
, pp. 1047-1058
-
-
Wall, M.A.1
Coleman, D.E.2
Lee, E.3
Iñiguez-Lluhi, J.A.4
Posner, B.A.5
Gilman, A.G.6
-
8
-
-
70350362562
-
A G protein-coupled receptor at work: The rhodopsin model
-
Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany. klaus-peter. hofmann@charite.de
-
Hofmann KP, Scheerer P, Hildebrand PW, Choe H-W, Park JH, Heck M, et al. A G protein-coupled receptor at work: The rhodopsin model. Trends Biochem Sci. Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany. klaus-peter. hofmann@charite.de; 2009; 34: 540-52. doi: 10.1016/j.tibs.2009.07.005
-
(2009)
Trends Biochem Sci
, vol.34
, pp. 540-552
-
-
Hofmann, K.P.1
Scheerer, P.2
Hildebrand, P.W.3
Choe, H.-W.4
Park, J.H.5
Heck, M.6
-
9
-
-
36248970132
-
Crystal structure of the ?(2) adrenergic receptor-Gs protein complex
-
1] Department of Molecular and Cellular Physiology Stanford University School of Medicine, Stanford, California 94305, USA [2] , 2200 Copenhagen N, Denmark [3].: Nature Publishing Group Available
-
Rasmussen SGF, Devree BT, Zou Y, Kruse AC, Chung KY, Kobilka TS, et al. Crystal structure of the ? (2) adrenergic receptor-Gs protein complex. Nature. 1] Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, California 94305, USA [2] , 2200 Copenhagen N, Denmark [3].: Nature Publishing Group; 2011; 450: 383-387. Available: Http://eutils.ncbi.nlm.nih. gov/entrez/eutils/elink.fcgi?dbfrom = pubmed&id=21772288&retmode = ref&cmd = prlinks
-
(2011)
Nature
, vol.450
, pp. 383-387
-
-
Rasmussen, S.G.F.1
Devree, B.T.2
Zou, Y.3
Kruse, A.C.4
Chung, K.Y.5
Kobilka, T.S.6
-
10
-
-
84932647495
-
Structural basis for nucleotide exchange in heterotrimeric G proteins
-
Dror RO, Mildorf TJ, Hilger D, Manglik A, Borhani DW, Arlow DH, et al. Structural basis for nucleotide exchange in heterotrimeric G proteins. Science (80-). 2015; 348: 1361-1365. doi: 10.1126/science. aaa5264
-
(2015)
Science (80-).
, vol.348
, pp. 1361-1365
-
-
Dror, R.O.1
Mildorf, T.J.2
Hilger, D.3
Manglik, A.4
Borhani, D.W.5
Arlow, D.H.6
-
11
-
-
84887443683
-
Molecular basis of cannabinoid CB1 receptor coupling to the G protein heterotrimer G?i: Identification of key CB1 contacts with the C-terminal helix ?5 of G?i
-
PMID: 24092756
-
Shim J-Y, Ahn KH, Kendall D a. Molecular basis of cannabinoid CB1 receptor coupling to the G protein heterotrimer G?i: Identification of key CB1 contacts with the C-terminal helix ?5 of G?i. J Biol Chem. 2013; 288: 32449-65. doi: 10.1074/jbc.M113.489153 PMID: 24092756
-
(2013)
J Biol Chem.
, vol.288
, pp. 32449-32465
-
-
Shim, J.-Y.1
Ahn, K.H.2
Kendall, D.A.3
-
12
-
-
84904488770
-
Structural basis of g protein-coupled receptor-gi protein interaction: Formation of the cannabinoid cb2 receptor/gi protein complex
-
Mnpotra JS, Qiao Z, Cai J, Lynch DL, Grossfield A, Leioatts N, et al. Structural Basis of G Protein-Coupled Receptor-Gi Protein Interaction: Formation of the Cannabinoid CB2 Receptor/Gi Protein Complex. J Biol Chem. 2014; 0-31. doi: 10.1074/jbc.M113.539916
-
(2014)
J Biol Chem.
, pp. 0-31
-
-
Mnpotra, J.S.1
Qiao, Z.2
Cai, J.3
Lynch, D.L.4
Grossfield, A.5
Leioatts, N.6
-
13
-
-
0035971240
-
Maximal rate and nucleotide dependence of rhodopsin-catalyzed transducin activation: Initial rate analysis based on a double displacement mechanism
-
PMID: 11116153
-
Heck M, Hofmann KP. Maximal rate and nucleotide dependence of rhodopsin-catalyzed transducin activation: Initial rate analysis based on a double displacement mechanism. J Biol Chem. 2001; 276: 10000-9. doi: 10.1074/jbc.M009475200 PMID: 11116153
-
(2001)
J Biol Chem.
, vol.276
, pp. 10000-10009
-
-
Heck, M.1
Hofmann, K.P.2
-
14
-
-
67649743779
-
Structural and kinetic modeling of an activating helix switch in the rhodopsin-transducin interface
-
Institut für Medizinische Physik und Biophysik (CC2) and. Available
-
Scheerer P, Heck M, Goede A, Park J, Choe H, Ernst OP, et al. Structural and kinetic modeling of an activating helix switch in the rhodopsin-transducin interface. Proc Natl Acad Sci U S A. Institut für Medizinische Physik und Biophysik (CC2) and.; 2009; 106: 10660-10665. Available: Http://www.pnas.org/content/106/26/10660.abstract
-
(2009)
Proc Natl Acad Sci U S A
, vol.106
, pp. 10660-10665
-
-
Scheerer, P.1
Heck, M.2
Goede, A.3
Park, J.4
Choe, H.5
Ernst, O.P.6
-
15
-
-
80053357815
-
Conformational changes in the G protein Gs induced by the ?2 adrenergic receptor
-
Nature Publishing Group Available
-
Chung KY, Rasmussen SGF, Liu T, Li S, Devree BT, Chae PS, et al. Conformational changes in the G protein Gs induced by the ?2 adrenergic receptor. Nature. Nature Publishing Group; 2011; 477: 611-615. Available: Http://www.nature.com/doifinder/10.1038/nature10488
-
(2011)
Nature
, vol.477
, pp. 611-615
-
-
Chung, K.Y.1
Rasmussen, S.G.F.2
Liu, T.3
Li, S.4
Devree, B.T.5
Chae, P.S.6
-
16
-
-
84922309763
-
Ghrelin receptor conformational dynamics regulate the transition from a preassembled to an active receptor:Gq complex
-
PMID: 25605885
-
Damian M, Mary S, Maingot M, M'Kadmi C, Gagne D, Leyris J-P, et al. Ghrelin receptor conformational dynamics regulate the transition from a preassembled to an active receptor:Gq complex. Proc Natl Acad Sci. 2015; 112: 1601-1606. doi: 10.1073/pnas.1414618112 PMID: 25605885
-
(2015)
Proc Natl Acad Sci.
, vol.112
, pp. 1601-1606
-
-
Damian, M.1
Mary, S.2
Maingot, M.3
M'Kadmi, C.4
Gagne, D.5
Leyris, J.-P.6
-
17
-
-
77956635542
-
Differential association modes of the thrombin receptor PAR1 with Galphai1 Galpha12 and beta-arrestin 1
-
PMID 20410441
-
Ayoub MA, Trinquet E, Pfleger KDG, Pin J-P. Differential association modes of the thrombin receptor PAR1 with Galphai1, Galpha12, and beta-arrestin 1. FASEB J. 2010; 24: 3522-3535. doi: 10.1096/fj. 10-154997 PMID: 20410441
-
(2010)
FASEB J.
, vol.24
, pp. 3522-3535
-
-
Ayoub, M.A.1
Trinquet, E.2
Pfleger, K.D.G.3
Pin, J.-P.4
-
18
-
-
0032516098
-
Light-activated rhodopsin induces structural binding motif in G protein alpha subunit
-
Institute for Biomedical Computing, Washington University Medical School, St. Louis, MO 63110, USA. Available
-
Kisselev OG, Kao J, Ponder JW, Fann YC, Gautam N, Marshall GR. Light-activated rhodopsin induces structural binding motif in G protein alpha subunit. Proc Natl Acad Sci U S A. Institute for Biomedical Computing, Washington University Medical School, St. Louis, MO 63110, USA.; 1998; 95: 4270-4275. Available: Http://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom = pubmed&id= 9539726&retmode = ref&cmd = prlinks
-
(1998)
Proc Natl Acad Sci U S A
, vol.95
, pp. 4270-4275
-
-
Kisselev, O.G.1
Kao, J.2
Ponder, J.W.3
Fann, Y.C.4
Gautam, N.5
Marshall, G.R.6
-
19
-
-
0036385914
-
Structure and orientation of a G protein fragment in the receptor bound state from residual dipolar couplings
-
2002/09/10 ed. S0022283602007453 [pii] PMID: 12217702
-
Koenig BW, Kontaxis G, Mitchell DC, Louis JM, Litman BJ, Bax A. Structure and orientation of a G protein fragment in the receptor bound state from residual dipolar couplings. J Mol Biol. 2002/09/10 ed. 2002; 322: 441-461. S0022283602007453 [pii] PMID: 12217702
-
(2002)
J Mol Biol.
, vol.322
, pp. 441-461
-
-
Koenig, B.W.1
Kontaxis, G.2
Mitchell, D.C.3
Louis, J.M.4
Litman, B.J.5
Bax, A.6
-
20
-
-
79953234218
-
Crystal structure of metarhodopsin II
-
Nature Publishing Group a division of Macmillan Publishers Limited. All Rights Reserved.
-
Choe H-W, Kim YJ, Park JH, Morizumi T, Pai EF, Krauss N, et al. Crystal structure of metarhodopsin II. Nature. Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.; 2011; 471: 651-5.
-
(2011)
Nature
, vol.471
, pp. 651-655
-
-
Choe, H.-W.1
Kim, Y.J.2
Park, J.H.3
Morizumi, T.4
Pai, E.F.5
Krauss, N.6
-
21
-
-
84855990615
-
Stabilized G protein binding site in the structure of constitutively active metarhodopsin-II
-
Paul Scherrer Institut Villigen PSI 5232, Switzerland. Available
-
Deupi X, Edwards P, Singhal A, Nickle B, Oprian D, Schertler G, et al. Stabilized G protein binding site in the structure of constitutively active metarhodopsin-II. Proc Natl Acad Sci U S A. Paul Scherrer Institut, Villigen PSI, 5232, Switzerland.; 2012; 109: 119-24. Available: Http://www.pnas.org/cgi/content/abstract/109/1/119
-
(2012)
Proc Natl Acad Sci U S A
, vol.109
, pp. 119-124
-
-
Deupi, X.1
Edwards, P.2
Singhal, A.3
Nickle, B.4
Oprian, D.5
Schertler, G.6
-
22
-
-
79953242234
-
The structural basis of agonist-induced activation in constitutively active rhodopsin
-
Standfuss J, Edwards PC, D'Antona A, Fransen M, Xie G, Oprian DD, et al. The structural basis of agonist-induced activation in constitutively active rhodopsin. Nature. 2011; 471: 656-60.
-
(2011)
Nature.
, vol.471
, pp. 656-660
-
-
Standfuss, J.1
Edwards, P.C.2
D'Antona, A.3
Fransen, M.4
Xie, G.5
Oprian, D.D.6
-
23
-
-
84879548723
-
The Role of Ligands on the Equilibria between Functional States of a
-
American Chemical Society
-
Kim TH, Chung KY, Manglik A, Hansen AL, Dror RO, Mildorf TJ, et al. The Role of Ligands on the Equilibria Between Functional States of a. J Am Chem Soc. American Chemical Society; 2013; 135: 9465-74. doi: 10.1021/ja404305k
-
(2013)
J Am Chem Soc.
, vol.135
, pp. 9465-9474
-
-
Kim, T.H.1
Chung, K.Y.2
Manglik, A.3
Hansen, A.L.4
Dror, R.O.5
Mildorf, T.J.6
-
24
-
-
84883072253
-
Precision vs flexibility in GPCR signaling
-
PMID: 23883288
-
Elgeti M, Rose AS, Bartl FJ, Hildebrand PW, Hofmann K-P, Heck M. Precision vs flexibility in GPCR signaling. J Am Chem Soc. 2013; 135: 12305-12. doi: 10.1021/ja405133k PMID: 23883288
-
(2013)
J Am Chem Soc.
, vol.135
, pp. 12305-12312
-
-
Elgeti, M.1
Rose, A.S.2
Bartl, F.J.3
Hildebrand, P.W.4
Hofmann, K.-P.5
Heck, M.6
-
25
-
-
84906088654
-
Position of transmembrane helix 6 determines receptor g protein coupling specificity
-
PMID: 25046433
-
Rose AS, Elgeti M, Zachariae U, Grubmüller H, Hofmann KP, Scheerer P, et al. Position of transmembrane helix 6 determines receptor g protein coupling specificity. J Am Chem Soc. 2014; 136: 11244-7. doi: 10.1021/ja5055109 PMID: 25046433
-
(2014)
J Am Chem Soc.
, vol.136
, pp. 11244-11247
-
-
Rose, A.S.1
Elgeti, M.2
Zachariae, U.3
Grubmüller, H.4
Hofmann, K.P.5
Scheerer, P.6
-
26
-
-
84893790121
-
Energetic analysis of the rhodopsin-G-protein complex links the ?5 helix to GDP release
-
PMID: 24292645
-
Alexander NS, Preininger AM, Kaya AI, Stein RA, Hamm HE, Meiler J. Energetic analysis of the rhodopsin-G-protein complex links the ?5 helix to GDP release. Nat Struct Mol Biol. 2014; 21: 56-63. doi: 10.1038/nsmb.2705 PMID: 24292645
-
(2014)
Nat Struct Mol Biol.
, vol.21
, pp. 56-63
-
-
Alexander, N.S.1
Preininger, A.M.2
Kaya, A.I.3
Stein, R.A.4
Hamm, H.E.5
Meiler, J.6
-
27
-
-
0036468995
-
Kinetic studies of protein-protein interactions
-
Available PMID: 11839488
-
Schreiber G. Kinetic studies of protein-protein interactions. Curr Opin Struct Biol. 2002; 12: 41-7. Available: Http://www.ncbi.nlm.nih.gov/pubmed/11839488 PMID: 11839488
-
(2002)
Curr Opin Struct Biol.
, vol.12
, pp. 41-47
-
-
Schreiber, G.1
-
28
-
-
0025036350
-
Rhodopsin mutants that bind but fail to activate transducin
-
Department of Biology Massachusetts Institute of Technology Cambridge 02139.
-
Franke R, Konig B, Sakmar T, Khorana H, Hofmann K. Rhodopsin mutants that bind but fail to activate transducin. Science (80-). Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.; 1990; 250: 123-125. doi: 10.1126/science.2218504
-
(1990)
Science (80-)
, vol.250
, pp. 123-125
-
-
Franke, R.1
Konig, B.2
Sakmar, T.3
Khorana, H.4
Hofmann, K.5
-
29
-
-
0028946950
-
Characterization of rhodopsin mutants that bind transducin but fail to induce GTP nucleotide uptake. Classification of mutant pigments by fluorescence, nucleotide release, and flash-induced light-scattering assays
-
Howard Hughes Medical Institute, Laboratory of Molecular Biology and Biochemistry, Rockefeller University, New York, New York 10021, USA. Available
-
Ernst OP, Hofmann KP, Sakmar TP. Characterization of rhodopsin mutants that bind transducin but fail to induce GTP nucleotide uptake. Classification of mutant pigments by fluorescence, nucleotide release, and flash-induced light-scattering assays. J Biol Chem. Howard Hughes Medical Institute, Laboratory of Molecular Biology and Biochemistry, Rockefeller University, New York, New York 10021, USA.; 1995; 270: 10580-10586. Available: Http://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi? dbfrom = pubmed&id=7737995&retmode = ref&cmd = prlinks
-
(1995)
J Biol Chem
, vol.270
, pp. 10580-10586
-
-
Ernst, O.P.1
Hofmann, K.P.2
Sakmar, T.P.3
-
30
-
-
0026320866
-
The energy landscapes and motions of proteins
-
Frauenfelder H, Sligar S, Wolynes P. The energy landscapes and motions of proteins. Science (80-). 1991; 254: 1598-1603. doi: 10.1126/science.1749933
-
(1991)
Science (80-).
, vol.254
, pp. 1598-1603
-
-
Frauenfelder, H.1
Sligar, S.2
Wolynes, P.3
-
31
-
-
47049130668
-
Crystal structure of the ligand-free G-proteincoupled receptor opsin
-
Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany.: Nature Publishing Group Available
-
Park JH, Scheerer P, Hofmann KP, Choe H-W, Ernst OP. Crystal structure of the ligand-free G-proteincoupled receptor opsin. Nature. Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany.: Nature Publishing Group; 2008; 454: 183-187. Available: Http://www.nature.com/nature/journal/v454/n7201/abs/nature07063.html
-
(2008)
Nature
, vol.454
, pp. 183-187
-
-
Park, J.H.1
Scheerer, P.2
Hofmann, K.P.3
Choe, H.-W.4
Ernst, O.P.5
-
32
-
-
0034723294
-
Rhodopsin recognition by mutant gs containing c-terminal residues of transducin
-
PMID 10644728
-
Natochin M, Muradov KG, McEntaffer RL, Artemyev NO. Rhodopsin Recognition by Mutant Gs Containing C-terminal Residues of Transducin. J Biol Chem. 2000; 275: 2669-2675. doi: 10.1074/jbc.275. 4.2669 PMID: 10644728
-
(2000)
J Biol Chem.
, vol.275
, pp. 2669-2675
-
-
Natochin, M.1
Muradov, K.G.2
McEntaffer, R.L.3
Artemyev, N.O.4
-
33
-
-
0023518498
-
The hydrophobic tryptic core of the beta-adrenergic receptor retains Gs regulatory activity in response to agonists and thiols
-
Available PMID: 2890639
-
Rubenstein RC, Wong SK, Ross EM. The hydrophobic tryptic core of the beta-adrenergic receptor retains Gs regulatory activity in response to agonists and thiols. J Biol Chem. 1987; 262: 16655-16662. Available: Http://www.jbc.org/cgi/content/abstract/262/34/16655 PMID: 2890639
-
(1987)
J Biol Chem.
, vol.262
, pp. 16655-16662
-
-
Rubenstein, R.C.1
Wong, S.K.2
Ross, E.M.3
-
34
-
-
67649755549
-
SuperLooper-a prediction server for the modeling of loops in globular and membrane proteins
-
Institute of Medical Physics and Biophysics Charité, University of Medicine, Berlin, Germany. peter.hildebrand@-charite.de: Oxford University Press
-
Hildebrand PW, Goede A, Bauer RA, Gruening B, Ismer J, Michalsky E, et al. SuperLooper-a prediction server for the modeling of loops in globular and membrane proteins. Nucleic Acids Res. Institute of Medical Physics and Biophysics, Charité, University of Medicine, Berlin, Germany. peter.hildebrand@-charite.de: Oxford University Press; 2009; 37: W571-4. doi: 10.1093/nar/gkp338
-
(2009)
Nucleic Acids Res
, vol.37
, pp. 571-574
-
-
Hildebrand, P.W.1
Goede, A.2
Bauer, R.A.3
Gruening, B.4
Ismer, J.5
Michalsky, E.6
-
35
-
-
0041919542
-
Improved protein-ligand docking using GOLD
-
Available PMID: 12910460
-
Verdonk ML, Cole JC, Hartshorn MJ, Murray CW, Taylor RD. Improved protein-ligand docking using GOLD. Proteins. 2003; 52: 609-23. Available: Http://www.ncbi.nlm.nih.gov/pubmed/12910460 PMID: 12910460
-
(2003)
Proteins.
, vol.52
, pp. 609-623
-
-
Verdonk, M.L.1
Cole, J.C.2
Hartshorn, M.J.3
Murray, C.W.4
Taylor, R.D.5
-
36
-
-
46249092554
-
Gromacs 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
-
American Chemical Society
-
Hess B, Kutzner C, Van Der Spoel D, Lindahl E. GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation. J Chem Theory Comput. American Chemical Society; 2008; 4: 435-447.
-
(2008)
J Chem Theory Comput.
, vol.4
, pp. 435-447
-
-
Hess, B.1
Kutzner, C.2
Van Der Spoel, D.3
Lindahl, E.4
-
37
-
-
77954256616
-
G-membed: Efficient insertion of a membrane protein into an equilibrated lipid bilayer with minimal perturbation
-
PMID: 20336801
-
Wolf MG, Hoefling M, Aponte-Santamaría C, Grubmüller H, Groenhof G. g-membed: Efficient insertion of a membrane protein into an equilibrated lipid bilayer with minimal perturbation. J Comput Chem. 2010; 31: 2169-74. doi: 10.1002/jcc.21507 PMID: 20336801
-
(2010)
J Comput Chem.
, vol.31
, pp. 2169-2174
-
-
Wolf, M.G.1
Hoefling, M.2
Aponte-Santamaría, C.3
Grubmüller, H.4
Groenhof, G.5
-
38
-
-
0030999097
-
Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature
-
Available PMID: 9129804
-
Berger O, Edholm O. Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature. Biophys J. 1997; 72: 2002-2013. Available: Http://www.sciencedirect.com/science/article/pii/S0006349597788453 PMID: 9129804
-
(1997)
Biophys J.
, vol.72
, pp. 2002-2013
-
-
Berger, O.1
Edholm, O.2
-
39
-
-
1242346370
-
The missing term in effective pair potentials
-
Inst Fis Liquidos & Sistemas Biol,Ra-1900 La Plata Argentina Available
-
Berendsen HJC, Grigera JR, Straatsma TP. The Missing Term in Effective Pair Potentials. J Phys Chem. Inst Fis Liquidos & Sistemas Biol,Ra-1900 La Plata,Argentina; 1987; 91: 6269-6271. Available: Http://links.isiglobalnet2.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth = mekentosj&SrcApp= Papers&DestLinkType=FullRecord&DestApp=WOS&KeyUT=A1987K994100038
-
(1987)
J Phys Chem
, vol.91
, pp. 6269-6271
-
-
Berendsen, H.J.C.1
Grigera, J.R.2
Straatsma, T.P.3
-
40
-
-
77953513118
-
Improved side-chain torsion potentials for the Amber ff99SB protein force field
-
Shaw Research, New York, New York 10036, USA. Available
-
Lindorff-Larsen K, Piana S, Palmo K, Maragakis P, Klepeis JL, Dror RO, et al. Improved side-chain torsion potentials for the Amber ff99SB protein force field. Proteins. D. E. Shaw Research, New York, New York 10036, USA.; 2010; 78: 1950-1958. Available: Http://sfx.mpg.de/sfx-local?id = doi:10.1002/prot. 22711
-
(2010)
Proteins. D. E.
, vol.78
, pp. 1950-1958
-
-
Lindorff-Larsen, K.1
Piana, S.2
Palmo, K.3
Maragakis, P.4
Klepeis, J.L.5
Dror, R.O.6
-
41
-
-
7544226311
-
PRODRG: A tool for high-throughput crystallography of proteinligand complexes
-
Division of Biological Chemistry and Molecular Microbiology, Wellcome Trust Biocentre, School of Life Sciences, University of Dundee, Dow Street, DD1 5EH, Scotland.
-
Schüttelkopf AW, Van Aalten DMF. PRODRG: A ToOl fOr hIgH-ThRoUgHpUt cRyStAlLoGrApHy oF Proteinligand complexes. Acta Crystallogr D Biol Crystallogr. Division of Biological Chemistry and Molecular Microbiology, Wellcome Trust Biocentre, School of Life Sciences, University of Dundee, Dow Street, DD1 5EH, Scotland.; 2004; 60: 1355-63. doi: 10.1107/S0907444904011679
-
(2004)
Acta Crystallogr D Biol Crystallogr
, vol.60
, pp. 1355-1363
-
-
Schüttelkopf, A.W.1
Van Aalten, D.M.F.2
|