Human MSH2 (hMSH2) protein controls ATP processing by hMSH2-hMSH6 - Wikidata - wikimedia - TriplyDB

Human MSH2 (hMSH2) protein controls ATP processing by hMSH2-hMSH6

Human MSH2 (hMSH2) protein controls ATP processing by hMSH2-hMSH6

http://www.wikidata.org/entity/Q35562811

about

Single-molecule views of MutS on mismatched DNA.Defining the nature of human γδ T cells: a biographical sketch of the highly empathetic Postreplicative mismatch repair.Large conformational changes in MutS during DNA scanning, mismatch recognition and repair signalling.Mismatch repair protein hMSH2-hMSH6 recognizes mismatches and forms sliding clamps within a D-loop recombination intermediate Evolutionary Covariance Combined with Molecular Dynamics Predicts a Framework for Allostery in the MutS DNA Mismatch Repair Protein.The mechanism of mismatch repair and the functional analysis of mismatch repair defects in Lynch syndrome.Mismatch repair during homologous and homeologous recombination Mutations in the nucleotide binding and hydrolysis domains of Helicobacter pylori MutS2 lead to altered biochemical activities and inactivation of its in vivo function.Mismatch repair Engineered disulfide-forming amino acid substitutions interfere with a conformational change in the mismatch recognition complex Msh2-Msh6 required for mismatch repair.Dynamic control of strand excision during human DNA mismatch repair ATP alters the diffusion mechanics of MutS on mismatched DNA.Mismatch binding, ADP-ATP exchange and intramolecular signaling during mismatch repair.Distinct requirements within the Msh3 nucleotide binding pocket for mismatch and double-strand break repair.MSH2:MSH6 exchanges ADP for ATP Cascading MutS and MutL sliding clamps control DNA diffusion to activate mismatch repair.Coordinated protein and DNA conformational changes govern mismatch repair initiation by MutS

P2860

Q26999680-2FBE53BD-4E63-4414-841D-74E135F29DBB Q27026152-980244E5-6C0D-43F1-A4CB-E30D4032FB30 Q27690911-23BCC55E-7120-4DA9-8ADE-FBC107AF8A5D Q28264548-5C9F77AA-16BB-4BAA-8113-C7158F0D8CAA Q30569509-779C45B0-9FA3-4054-BFA8-EF701E53DFB4 Q30841579-5E611EAB-88A9-41C7-A5F0-0D14A32FAEBD Q34533276-93080CF2-91D2-468B-9908-5DE8446F30E0 Q35164333-35F43B36-7CF3-4838-AE06-6069E035CCE8 Q35914165-FE529651-1F92-42BB-82B4-7490EEF2B29C Q36283640-9D297E05-27C0-48B1-9EEB-9AB8B2E26B13 Q36436073-72AE7DD2-D7C9-4D83-AAC5-6BE632B122E9 Q36742733-ACFB1CA2-C44E-4745-A567-C3A75A5A2919 Q37683114-5D7831CD-DF4D-4857-B816-2B9FAF7CDBFA Q38254881-843B2824-ADA3-40DF-8FE7-09AE61FC5356 Q40823475-1CF8B807-BC29-4DA6-9E49-31380F85DDB7 Q50287452-6AB93278-3B94-4207-9731-4178B672E508 Q51324871-66132230-6CD1-4714-A754-F50BEF212FFC Q57060631-72EE63BD-0EFE-4339-9F51-1BD3D58CCA18

P2860

Human MSH2 (hMSH2) protein controls ATP processing by hMSH2-hMSH6

http://www.wikidata.org/entity/Q35562811

description

2011 nî lūn-bûn

@nan

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

2011年论文

@zh

2011年论文

@zh-cn

name

Human MSH2 (hMSH2) protein controls ATP processing by hMSH2-hMSH6

@ast

Human MSH2 (hMSH2) protein controls ATP processing by hMSH2-hMSH6

@en

type

label

Human MSH2 (hMSH2) protein controls ATP processing by hMSH2-hMSH6

@ast

Human MSH2 (hMSH2) protein controls ATP processing by hMSH2-hMSH6

@en

prefLabel

Human MSH2 (hMSH2) protein controls ATP processing by hMSH2-hMSH6

@ast

Human MSH2 (hMSH2) protein controls ATP processing by hMSH2-hMSH6

@en

P1433

Q35562811-50E1052C-F799-4280-B64B-A89B97A07681

P1476

Q35562811-70C48CA5-7522-4130-B066-7C123D3D194D

P2093

Q35562811-0D0F0280-A3B9-471D-829F-EC8B85AABC1D

Q35562811-0FFDAA7C-004F-4C63-AB44-4667ECB973A7

Q35562811-4F76BF7C-B7A2-4B5A-B70D-5EDD894589E4

Q35562811-5DE86DDB-30BF-4A00-B0F1-319025EEF57A

Q35562811-73FAE2A9-7182-4DD2-A7D9-2806ED10CE50

Q35562811-7F219F17-124A-45AC-B6FA-57DAF5FCD560

Q35562811-890008DD-41D9-46E0-A441-F9CD5BC658BD

Q35562811-941AD84A-572F-4123-A6B3-7230F7C2B01D

Q35562811-C0E585E4-EA89-4232-91CA-24E597439FF8

P2860

Q35562811-043C231D-9548-4604-B55A-2E355426B133

Q35562811-084CA4FF-084E-4186-831F-4EAE16B7DDCD

Q35562811-0DD9FEF8-9D37-4549-AF3F-C74F1761E049

Q35562811-0E79FF32-EF11-478E-A66B-A45B46DAA9C7

Q35562811-14231BD6-F8B7-4050-BD03-7BDB41EE3C4A

Q35562811-18856DCA-6336-43FC-A493-FE22D9C4E20C

Q35562811-1F95D97D-BB6F-4FB7-A14B-6A2493F2A61D

Q35562811-23C34850-CCE9-44EB-98D8-E27818D40E10

Q35562811-2BA6999B-E8DA-46D6-A9ED-1E6B3AE141F4

Q35562811-3408F449-C301-4925-AD22-336921D58B62

P304

Q35562811-6BD7828C-BD75-4EE8-B5A5-64DA7DC31885

P31

Q35562811-C1DC8B7C-09FC-49F7-AADC-D5182AC2EC0B

P356

Q35562811-3C60F2F6-42C8-4898-9B02-C7EF069E4782

P407

Q35562811-7A545077-5B16-4E37-81A8-7888AAE16651

P433

Q35562811-A3C43772-7256-4D83-A66E-326858974DE7

P478

Q35562811-ECAA2BD6-1244-4EF2-A3C4-060669A585ED

P577

Q35562811-4135F84F-89EC-4981-8332-E94BE32293DA

P698

Q35562811-6C1D7892-756E-4D8C-9E25-EB0F82C56FC4

P932

Q35562811-937D5399-BE2F-4BA4-BD75-BC22E227525C

P356

JBC.M111.297523

P1433

Journal of Biological Chemistry

P1476

Human MSH2 (hMSH2) protein controls ATP processing by hMSH2-hMSH6

@en

P2093

Christopher Cook

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

Christopher D Heinen

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

Jennifer L Cyr

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

Juana Martin Lopez

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

Manju M Hingorani

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

Miho Sakato

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

Nidhi Punja

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

Richard Fishel

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

Robert A Forties

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

P2860

hMSH2 forms specific mispair-binding complexes with hMSH3 and hMSH6

Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA

The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch

Structure of the human MutSalpha DNA lesion recognition complex

Structural model for strain-dependent microtubule activation of Mg-ADP release from kinesin

Magnesium Coordination Controls the Molecular Switch Function of DNA Mismatch Repair Protein MutS

Genetic and biochemical analysis of Msh2p-Msh6p: role of ATP hydrolysis and Msh2p-Msh6p subunit interactions in mismatch base pair recognition.

Eukaryotic DNA mismatch repair.

hMSH2-hMSH6 forms a hydrolysis-independent sliding clamp on mismatched DNA

The human mismatch recognition complex hMSH2-hMSH6 functions as a novel molecular switch

P304

40287-40295

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

P31

scholarly article

P356

10.1074/JBC.M111.297523

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

P407

P433

46

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

P478

286

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

P577

2011-09-19T00:00:00Z

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

P698

21937421

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

P932

3220577

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