about
Computing phenomenologic Adair-Klotz constants from microscopic MWC parametersHigh and low oxygen affinity conformations of T state hemoglobinLigand depletion in vivo modulates the dynamic range and cooperativity of signal transduction.Amino acid recognition and gene regulation by riboswitches.Oxygen-organophosphate linkage in hemoglobin A. The double hump effect.Mechanism of tertiary structural change in hemoglobin.Ligand-promoted weakening of intersubunit bonding domains in aspartate transcarbamolylasePositive cooperativity without domains or subunits in a monomeric membrane channel.Sickle cell hemoglobin fiber structure altered by alpha-chain mutationLinkage between ligand binding and the dimer-tetramer equilibrium in the Monod-Wyman-Changeux model of hemoglobin.Spectroscopic studies of oxy- and carbonmonoxyhemoglobin after pulsed optical excitationAllosteric effectors do not alter the oxygen affinity of hemoglobin crystals.Circular dichroism spectroscopy of tertiary and quaternary conformations of human hemoglobin entrapped in wet silica gels.Tangential flow filtration of hemoglobinCoupling between oxidation state and hydrogen bond conformation in heme proteins.Allosteric interpretation of the measurement of cooperative free energy in cyanomethemoglobin.Application of linear free energy relations to protein conformational changes: the quaternary structural change of hemoglobin.Distinctions between the two-state and sequential models for cooperative ligand binding.The multiple phenotypes of allosteric receptor mutants.Experimental evolution in bacteria.A unified view of cystic fibrosis transmembrane conductance regulator (CFTR) gating: combining the allosterism of a ligand-gated channel with the enzymatic activity of an ATP-binding cassette (ABC) transporterHow do disordered regions achieve comparable functions to structured domains?Using the MWC model to describe heterotropic interactions in hemoglobin.Integrated analysis of RNA-binding protein complexes using in vitro selection and high-throughput sequencing and sequence specificity landscapes (SEQRS).The Allostery Model of TCR Regulation.Kinetics of carboxymyoglobin and oxymyoglobin studied by picosecond spectroscopy.A role of heme side-chains of human hemoglobin in its function revealed by circular dichroism and resonance Raman spectroscopy.On the different sources of cooperativity in pH titrating sites of a membrane protein channel
P2860
Q21202789-B2735C78-B423-46C0-9295-97FBD3D39A63Q28361931-77C60119-07A9-47EE-AC93-324DB150D305Q33522206-CB0CA204-CEB8-434B-93F6-26A38F29AB48Q34018578-F3841BE5-0834-44ED-AA76-48FCB2F27943Q34259546-B7FF0213-E986-4796-A51B-140A6EF19244Q35007132-865FC61F-8E13-40A4-AD86-DD35AD505890Q35049726-A6053A4D-ADA0-4CCE-8F28-1F1710280EE8Q35168874-83F25ABC-7C6C-4D3C-89C9-7DE8942FAAE5Q35319484-5FC0CD7C-0F4F-45FD-A935-4AFA7EDE6DEFQ35608107-9B372E35-7BE2-40A9-B920-EA5BC7DC77E3Q36272325-0828B0A9-149C-43B6-8C40-370F2E2125F0Q36280298-9547BF08-5BB5-4C88-8FF4-0094AD7A2364Q36458558-542FDABF-076C-4653-AAE0-502A8A62AF95Q37109197-1E61F825-069E-4C52-9F12-93AA89A0AEECQ37318986-0EE277DB-E9E3-46DB-97A8-EF579A34DE19Q37397111-05E6A818-6F65-46E5-94F5-B16FFDE64F08Q37516292-FB565A0E-6015-4F22-BE56-2C14D7DA1BAEQ37598347-93ADD286-A390-4EEB-A1EC-EC7479EC0AD6Q37703420-503A7856-74C1-4C13-872D-B448934D6023Q37827733-07F7C877-FC85-41B8-AE39-BAC18D39F45CQ37836188-CB00369A-527A-436D-B67C-5C4F8C2EDD85Q38370771-1F97F0FB-04CF-4FF7-9F06-C67C1DEBD5EEQ38632051-0B918371-CAAC-41BB-A13D-6D6472429AD6Q38978225-B38EB7CC-D92F-4435-9F3D-A7CB17BE71F0Q39043852-43F9FA6C-E1E0-4EA7-8A69-DA20553E8F1FQ40462250-810260B4-0200-40BB-9FFF-7EED319BA723Q48089238-D50D19D0-0AD7-4FCB-9A60-367EC8F80222Q58056180-4D950C8B-4080-4D7C-B0F4-6AF4B2272CD2
P2860
description
1975 nî lūn-bûn
@nan
1975 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1975 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1975年の論文
@ja
1975年論文
@yue
1975年論文
@zh-hant
1975年論文
@zh-hk
1975年論文
@zh-mo
1975年論文
@zh-tw
1975年论文
@wuu
name
Cooperative interactions of hemoglobin.
@ast
Cooperative interactions of hemoglobin.
@en
Cooperative interactions of hemoglobin.
@nl
type
label
Cooperative interactions of hemoglobin.
@ast
Cooperative interactions of hemoglobin.
@en
Cooperative interactions of hemoglobin.
@nl
prefLabel
Cooperative interactions of hemoglobin.
@ast
Cooperative interactions of hemoglobin.
@en
Cooperative interactions of hemoglobin.
@nl
P1476
Cooperative interactions of hemoglobin.
@en
P2093
Edelstein SJ
P304
P356
10.1146/ANNUREV.BI.44.070175.001233
P577
1975-01-01T00:00:00Z