Monitoring the GAP catalyzed H-Ras GTPase reaction at atomic resolution in real time. - Wikidata - awgldk - TriplyDB

Monitoring the GAP catalyzed H-Ras GTPase reaction at atomic resolution in real time.

Monitoring the GAP catalyzed H-Ras GTPase reaction at atomic resolution in real time.

http://www.wikidata.org/entity/Q36521874

about

Biochemical characterization of the Ran-RanBP1-RanGAP system: are RanBP proteins and the acidic tail of RanGAP required for the Ran-RanGAP GTPase reaction?High resolution crystal structures of human Rab5a and five mutants with substitutions in the catalytically important phosphate-binding loop Structural basis of mechanochemical coupling in a hexameric molecular motor Catalytic mechanism of a mammalian Rab{middle dot}RabGAP complex in atomic detail The small terminase, gp16, of bacteriophage T4 is a regulator of the DNA packaging motor Effects of protonation on the hydrolysis of triphosphate in vacuum and the implications for catalysis by nucleotide hydrolyzing enzymes Regioselective long-range proton transfer in new rifamycin antibiotics: a process in which crown ethers act as stronger Brønsted bases than amines.Mdr1 gene expression and mutations in Ras proto-oncogenes in acute myeloid leukemia.A phosphoryl transfer intermediate in the GTPase reaction of Ras in complex with its GTPase-activating protein Phosphate vibrations probe local electric fields and hydration in biomolecules Common hydrogen bond interactions in diverse phosphoryl transfer active sites.Relevance of the kinetic equilibrium of forces to the control of the cell cycle by Ras proteins.Intragenic suppressor mutations restore GTPase and translation functions of a eukaryotic initiation factor 5B switch II mutant.Structural flexibility of small GTPases. Can it explain their functional versatility?Proteins in action monitored by time-resolved FTIR spectroscopy.Overview of simulation studies on the enzymatic activity and conformational dynamics of the GTPase Ras.The GAP arginine finger movement into the catalytic site of Ras increases the activation entropy Role of hybrid tRNA-binding states in ribosomal translocation.Lessons from computer simulations of Ras proteins in solution and in membrane The hydrolysis activity of adenosine triphosphate in myosin: a theoretical analysis of anomeric effects and the nature of the transition state Why nature really chose phosphate.Ras activation revisited: role of GEF and GAP systems.The small GTPases K-Ras, N-Ras, and H-Ras have distinct biochemical properties determined by allosteric effects.Invited review: Small GTPases and their GAPs.Invited review: Activation of G proteins by GTP and the mechanism of Gα-catalyzed GTP hydrolysis.Unravelling the mechanism of dual-specificity GAPs.Theoretical IR spectroscopy based on QM/MM calculations provides changes in charge distribution, bond lengths, and bond angles of the GTP ligand induced by the Ras-protein.Formation and decay of the arrestin·rhodopsin complex in native disc membranes.Kinetic timing: a novel mechanism that improves the accuracy of GTPase timers in endosome fusion and other biological processes.The role of magnesium for geometry and charge in GTP hydrolysis, revealed by quantum mechanics/molecular mechanics simulations.Reversible immobilization of peptides: surface modification and in situ detection by attenuated total reflection FTIR spectroscopy.Fourier transform infrared spectroscopy on the Rap.RapGAP reaction, GTPase activation without an arginine finger.Role of the arginine finger in Ras.RasGAP revealed by QM/MM calculations.New insights into RAS biology reinvigorate interest in mathematical modeling of RAS signaling.A FTIR microspectroscopy study of the structural and biochemical perturbations induced by natively folded and aggregated transthyretin in HL-1 cardiomyocytes

P2860

Q24649967-5CF71DF4-2FDE-4995-A3A3-818FD4523EE5 Q27639966-8D346AF2-9513-45AE-A69D-2C787001C56B Q27649210-E3F8AEE3-8B2C-4230-9020-73FC3584E07D Q27675470-8EEA4359-1844-49F6-B133-C89942B7A865 Q28749848-E94F9F4B-7992-4518-BEEA-FC9B4F532213 Q28817399-0AE6C041-F5F4-47BD-8860-9F468E90F5B9 Q30886914-847C9884-7324-4F98-A668-43016B821D68 Q34155343-27CCDAB1-7444-4BC6-A015-A191EBEBFBFD Q35080333-44BB14CF-B5CD-444E-A5F2-0C8E8F08F051 Q35179482-05344C8C-BEDB-4751-B301-CA08B85833B3 Q35264740-F40FEBC5-E71A-474E-9A25-72EF6F14F838 Q35672329-AE16CABF-DD3D-4ADF-B423-B7DCE4E0B4A1 Q35676181-FD800A01-A087-4AA5-BAA9-ED496027D692 Q36011162-BB44AE00-C919-4743-AA37-E1755A10DE7C Q36122187-D8E46974-F51A-4938-BE24-3404CA449B9B Q36176891-E6F700F3-4A35-4327-AFBF-999E5B014A8C Q36609155-E9302493-43AA-4D92-AC7A-2D30C18C65C3 Q36756856-50DF9CBE-BA1B-457C-B9FA-A9BBAFF12E05 Q37301995-85DCAB5D-79A5-4CD9-8F27-203210DF2B9B Q37438825-C466060A-1088-42DD-AD8C-EB68ED2A246F Q38073986-09F7D268-AE55-433E-8A23-B72E9FB5AA02 Q38381506-53C3517D-6A2D-46EF-9693-D32BD3B61353 Q38718478-1694EF94-8AF8-479C-8F00-6728883152B7 Q38772657-C1206423-7203-41FE-8BB1-523B708FFC95 Q38782431-DFAF0984-E324-4867-A3B0-F777EABA24F2 Q40117233-2F813518-618F-4928-9D0B-4CB4C72D0D2C Q40334259-C2CE5126-D98E-475B-B808-038CD1F48E0D Q40680953-E21AB88A-0EA6-45D9-BC22-FDF46BB119E4 Q40740814-19C1D845-F101-4F4B-8273-1BF95804E58D Q42243109-3DE91194-7B76-4F53-9912-0D346A78BA20 Q44389732-6F2355E2-88B5-40F1-B3A7-E5A5D701D0B3 Q45005958-3E236523-3BB9-4207-927E-65E58A721019 Q46893990-B34975A8-73B0-4949-9A2D-8C460DC3ECF8 Q52666594-00110F3E-8670-4272-BC24-56EA64C78394 Q58731093-58AB3DAE-C124-4850-A741-A2CBE7F60AA7

P2860

Monitoring the GAP catalyzed H-Ras GTPase reaction at atomic resolution in real time.

http://www.wikidata.org/entity/Q36521874

description

2001 nî lūn-bûn

@nan

2001年の論文

@ja

2001年論文

@yue

2001年論文

@zh-hant

2001年論文

@zh-hk

2001年論文

@zh-mo

2001年論文

@zh-tw

2001年论文

@wuu

2001年论文

@zh

2001年论文

@zh-cn

name

Monitoring the GAP catalyzed H-Ras GTPase reaction at atomic resolution in real time.

@ast

Monitoring the GAP catalyzed H-Ras GTPase reaction at atomic resolution in real time.

@en

type

label

Monitoring the GAP catalyzed H-Ras GTPase reaction at atomic resolution in real time.

@ast

Monitoring the GAP catalyzed H-Ras GTPase reaction at atomic resolution in real time.

@en

prefLabel

Monitoring the GAP catalyzed H-Ras GTPase reaction at atomic resolution in real time.

@ast

Monitoring the GAP catalyzed H-Ras GTPase reaction at atomic resolution in real time.

@en

P1433

Q36521874-5BAA5A50-DF7B-4534-AD34-09403FB0FE7B

P1476

Q36521874-82E43B89-FB13-4FA8-8A3C-4917A05B6118

P2093

Q36521874-4D743F85-0316-453C-B307-74ABB75B91F1

Q36521874-8326BED8-A289-4EC9-91B6-8F5D1D594C4D

Q36521874-B3434440-F6A8-4181-AAEA-A3509BEBD9E8

Q36521874-E02CBF93-4419-46A3-9086-49C6D1DEDE3F

P2860

Q36521874-07BE985B-0B79-4A5C-9D76-DC0DF3E8E63A

Q36521874-119F7115-021F-4A48-8C94-C9FA3351B267

Q36521874-14D21106-392E-4518-A0C9-082C54A740E3

Q36521874-22717E0E-D515-4E2A-8AB4-E1610E5386BA

Q36521874-24CFDA8B-FE4F-4F71-8F72-1DD3A6E31CBA

Q36521874-49A3D9CF-FD46-4B95-B5C1-68507D33FBEA

Q36521874-4AC5E434-D7B8-4BF8-81A1-0F454DEFAC39

Q36521874-4E910EC4-617F-4450-98BF-29B01E2630E8

Q36521874-511E9281-6A7B-40BA-9784-D595FBCFF262

Q36521874-54C312A6-1EB2-44E1-AAA5-368A203CD5D6

P304

Q36521874-17C16F93-44E4-4D1F-B00A-B68159D5AD39

P31

Q36521874-92A3C21C-4479-4440-91CC-476912E8A138

P356

Q36521874-CB0D874A-B0D6-4B3F-BC97-F8C350DDE297

P407

Q36521874-B3EF41D2-4D8C-421C-B1BD-C66E4EE08930

P433

Q36521874-CE4BC161-61B5-4435-8803-613D717BD572

P478

Q36521874-A0885DDB-0FF9-471B-9DDE-BA057B6098B3

P577

Q36521874-39384A31-0E27-46D8-8947-149DA8F9FF34

P5875

Q36521874-FA1BDDAE-F501-4AD0-B72F-7EE80AC106CC

P698

Q36521874-282EB69F-E535-4209-A7A5-15AC73A7F875

P932

Q36521874-133B84C3-952F-47F0-9FC9-F2CD3A123004

P356

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Monitoring the GAP catalyzed H-Ras GTPase reaction at atomic resolution in real time.

@en

P2093

Ahmadian MR

http://www.w3.org/2001/XMLSchema#string

Allin C

http://www.w3.org/2001/XMLSchema#string

Gerwert K

http://www.w3.org/2001/XMLSchema#string

Wittinghofer A

http://www.w3.org/2001/XMLSchema#string

P2860

Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP

The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants

Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue

Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP

Ras-catalyzed hydrolysis of GTP: a new perspective from model studies

The pre-hydrolysis state of p21(ras) in complex with GTP: new insights into the role of water molecules in the GTP hydrolysis reaction of ras-like proteins

Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis

GAP into the breach

Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras

P304

7754-7759

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1073/PNAS.131549798

http://www.w3.org/2001/XMLSchema#string

P407

P433

14

http://www.w3.org/2001/XMLSchema#string

P478

98

http://www.w3.org/2001/XMLSchema#string

P577

2001-07-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

11901923

http://www.w3.org/2001/XMLSchema#string

P698

11438727

http://www.w3.org/2001/XMLSchema#string

P932

35414

http://www.w3.org/2001/XMLSchema#string