Interfacial and distal-heme pocket mutations exhibit additive effects on the structure and function of hemoglobin. - Wikidata - awgldk - TriplyDB

Interfacial and distal-heme pocket mutations exhibit additive effects on the structure and function of hemoglobin.

Interfacial and distal-heme pocket mutations exhibit additive effects on the structure and function of hemoglobin.

http://www.wikidata.org/entity/Q37217030

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Development of recombinant hemoglobin-based oxygen carriers A biochemical--biophysical study of hemoglobins from woolly mammoth, Asian elephant, and humans WAXS studies of the structural diversity of hemoglobin in solution.Distal histidine stabilizes bound O2 and acts as a gate for ligand entry in both subunits of adult human hemoglobin.An investigation of the distal histidyl hydrogen bonds in oxyhemoglobin: effects of temperature, pH, and inositol hexaphosphate.Recombinant hemoglobin II from Lucina pectinata: a large-scale method for hemeprotein expression in E. coli Repeated elevational transitions in hemoglobin function during the evolution of Andean hummingbirds.New look at hemoglobin allostery.Modulating distal cavities in the α and β subunits of human HbA reveals the primary ligand migration pathway.2017 Military Supplement: Current Challenges in the Development of Acellular Hemoglobin Oxygen Carriers by Protein Engineering.Hemoglobin Reactivity and Regulation

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P2860

Interfacial and distal-heme pocket mutations exhibit additive effects on the structure and function of hemoglobin.

http://www.wikidata.org/entity/Q37217030

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

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scientific article published on 13 September 2008

@en

vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

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vědecký článek

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name

Interfacial and distal-heme po ...... re and function of hemoglobin.

@en

Interfacial and distal-heme po ...... re and function of hemoglobin.

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type

label

Interfacial and distal-heme po ...... re and function of hemoglobin.

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Interfacial and distal-heme po ...... re and function of hemoglobin.

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prefLabel

Interfacial and distal-heme po ...... re and function of hemoglobin.

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Interfacial and distal-heme po ...... re and function of hemoglobin.

@nl

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Interfacial and distal-heme po ...... re and function of hemoglobin.

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David H Maillett

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Nancy T Ho

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

Tong-Jian Shen

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Virgil Simplaceanu

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P2860

A human recombinant haemoglobin designed for use as a blood substitute

A third quaternary structure of human hemoglobin A at 1.7-A resolution

Insights into the solution structure of human deoxyhemoglobin in the absence and presence of an allosteric effector

Mechanism of NO-induced oxidation of myoglobin and hemoglobin

Structures of a hemoglobin-based blood substitute: insights into the function of allosteric proteins

Novel water-mediated hydrogen bonds as the structural basis for the low oxygen affinity of the blood substitute candidate rHb(alpha 96Val-->Trp)

ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

High and low oxygen affinity conformations of T state hemoglobin

A novel site-directed mutant of myoglobin with an unusually high O2 affinity and low autooxidation rate.

A test of the role of the proximal histidines in the Perutz model for cooperativity in haemoglobin.

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10551-10563

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scholarly article

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10.1021/BI800816V

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40

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47

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2008-09-13T00:00:00Z

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23254331

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18788751

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2692483

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