Asymmetric cooperativity in a symmetric tetramer: human hemoglobin. - Wikidata - awgldk - TriplyDB

Asymmetric cooperativity in a symmetric tetramer: human hemoglobin.

Asymmetric cooperativity in a symmetric tetramer: human hemoglobin.

http://www.wikidata.org/entity/Q34486165

about

Dynamic dissociating homo-oligomers and the control of protein function Tertiary and Quaternary Allostery in Tetrameric Hemoglobin from Scapharca inaequivalvis The mechanism of allosteric coupling in choline kinase α1 revealed by the action of a rationally designed inhibitor Energy transfer in molecular devices.Structural basis for cooperative oxygen binding and bracelet-assisted assembly of Lumbricus terrestris hemoglobin.Experiments on Hemoglobin in Single Crystals and Silica Gels Distinguish among Allosteric Models.Receptor Activation of HIV-1 Env Leads to Asymmetric Exposure of the gp41 Trimer.Allostery: an illustrated definition for the 'second secret of life'.An Origin of Cooperative Oxygen Binding of Human Adult Hemoglobin: Different Roles of the α and β Subunits in the α2β2 Tetramer Symmetry distortion in the human hemoglobin tetramer induced by asymmetric ligation.Hemoglobin Reactivity and Regulation Dissimilar flexibility of α and β subunits of human adult hemoglobin influences the protein dynamics and its alteration induced by allosteric effectors.

P2860

Q24619847-E4799A9E-93DE-450F-A1CA-E46AB9BEF9A5 Q27676689-010860BA-7EEB-48CE-B2CE-A56C57D305EB Q27684087-140C54C4-C834-4640-8658-2EF8FB8E980A Q30371023-ECA6C562-8EA8-4C4B-82B5-F8AE176CA4D4 Q30844404-EDDD5866-D731-4D22-8598-69D11EFF3525 Q36076141-7AF917F8-9278-40BC-B019-24908B269203 Q36228646-2BF7BA6C-F622-4742-8B16-0A16FD64266C Q37244995-A8708CDB-41F5-48A6-A980-809EB05541D1 Q42420729-52A1A0AD-EBC1-4456-8BE2-4A1CCAC075D8 Q43814672-43FED33F-71D4-4B88-BE13-6E98B8966851 Q53408119-3C97437C-21E7-4C2D-9AC4-2743336F10F6 Q55049796-D180BB8E-275A-4456-B35E-4CEDDF2ABF3F

P2860

Asymmetric cooperativity in a symmetric tetramer: human hemoglobin.

http://www.wikidata.org/entity/Q34486165

description

2006 nî lūn-bûn

@nan

2006 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2006年の論文

@ja

2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

name

Asymmetric cooperativity in a symmetric tetramer: human hemoglobin.

@ast

Asymmetric cooperativity in a symmetric tetramer: human hemoglobin.

@en

Asymmetric cooperativity in a symmetric tetramer: human hemoglobin.

@nl

type

label

Asymmetric cooperativity in a symmetric tetramer: human hemoglobin.

@ast

Asymmetric cooperativity in a symmetric tetramer: human hemoglobin.

@en

Asymmetric cooperativity in a symmetric tetramer: human hemoglobin.

@nl

prefLabel

Asymmetric cooperativity in a symmetric tetramer: human hemoglobin.

@ast

Asymmetric cooperativity in a symmetric tetramer: human hemoglobin.

@en

Asymmetric cooperativity in a symmetric tetramer: human hemoglobin.

@nl

P1433

Q34486165-961E08A8-7378-44B9-BE23-9D18C704821D

P1476

Q34486165-BCA242B0-55FD-4633-AE76-6A530881E56F

P2093

Q34486165-8DCD8E02-447B-45F1-A5C9-04F484FC4763

Q34486165-E2AA06AB-4E56-485C-A4E8-6FEA2D50BF30

P2860

Q34486165-22D06A72-8855-4D3B-944F-2B5B0AF0ED90

Q34486165-328226AA-194B-4711-B188-2C48202453E9

Q34486165-3C35BBBD-777B-4644-8D26-39F501C27212

Q34486165-3E9A4B24-797A-40AC-BCA0-35443F56D781

Q34486165-41C4337B-26D3-430A-B1C9-607E0CF56A75

Q34486165-4F30EE27-E49F-4FF6-B196-41A77C43A158

Q34486165-517D0C1C-249A-443B-87C6-AA20CEBF050D

Q34486165-5FCBDB64-36B2-4F87-93DD-020017B5FF66

Q34486165-690B778C-5152-46BC-8B74-DFFCAD596B1E

Q34486165-6B638693-A733-4780-84BF-2BD040B06C85

P304

Q34486165-6F231A98-DA2D-4FFE-9AC8-1D1DA1E2D44A

P31

Q34486165-D91E85A8-A810-4990-A136-BB30910CCD1A

P356

Q34486165-643457E6-4215-4D71-9870-823DD80C1A51

P407

Q34486165-BD914F7C-C000-4D26-8DC1-80295CB95ABE

P433

Q34486165-BCF1E585-4CE7-4F33-BFCF-713BBDC03C6D

P478

Q34486165-195522ED-2BDB-46E0-8E3A-92687F98A3CA

P577

Q34486165-90CCF11E-6EC4-4B1C-81D0-E38C60ED00E4

P698

Q34486165-B7C63A2C-8498-421B-9CBC-65A2F7066536

P356

P1433

Journal of Biological Chemistry

P1476

Asymmetric cooperativity in a symmetric tetramer: human hemoglobin.

@en

P2093

Gary K Ackers

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

Jo M Holt

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

P2860

Crystallographic evidence for a new ensemble of ligand-induced allosteric transitions in hemoglobin: the T-to-T(high) quaternary transitions

Comparison of experimental binding data and theoretical models in proteins containing subunits

The linkage between oxygenation and subunit dissociation in human hemoglobin

A signature of the T ---> R transition in human hemoglobin.

Single residue modification of only one dimer within the hemoglobin tetramer reveals autonomous dimer function

Molecular dynamics of human methemoglobin: the transmission of conformational information between subunits in an alpha beta dimer.

High-resolution X-ray study of deoxyhemoglobin Rothschild 37 beta Trp----Arg: a mutation that creates an intersubunit chloride-binding site.

The structure--function relationship of hemoglobin in solution at atomic resolution.

Haemoglobin: the structural changes related to ligand binding and its allosteric mechanism.

Effects of amino acid substitutions at beta 131 on the structure and properties of hemoglobin: evidence for communication between alpha 1 beta 1- and alpha 1 beta 2-subunit interfaces.

P304

11441-11443

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

P31

scholarly article

P356

10.1074/JBC.R500019200

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

P407

P433

17

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

P478

281

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

P577

2006-01-19T00:00:00Z

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

P698

16423822

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