About: Nature of Haem–Haem Interaction

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scientific article published in Nature

Attributes	Values
rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) article publié dans la revue scientifique Nature (fr) scientific article published in Nature (en) im Juni 1972 veröffentlichter wissenschaftlicher Artikel (de) наукова стаття, опублікована в Nature в червні 1972 (uk)
publication date	wds:Q59071453-80730597-45FB-4617-A161-C679C1541325
publication date	1972-06-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q59071453-8E9E814E-FD52-4AD7-8A72-557CFDF1A894
language of work or name	English
exact match	wds:Q59071453-7D98F5AB-A2FF-45B1-B1AC-CE454418C0F1
exact match	https://scigraph.springernature.com/pub.10.1038/237495a0
cites work	wds:Q59071453-2B07971E-AD76-41FE-B932-FB186E01B191 wds:Q59071453-2CE05AD8-62F6-46B4-B63F-5E53D4C61F35 wds:Q59071453-393AE334-0CEC-45DF-911C-0B08B398DE67 wds:Q59071453-49D8ACF8-3918-4255-B784-03612E5219D8 wds:Q59071453-7A41B21D-EBD7-402B-81A3-72FA18C7F6F0 wds:Q59071453-9C29B63D-8AE8-48B1-82E9-85A2A04BCD79 wds:Q59071453-A0998A07-B9CE-4C52-83F3-BCF413CDCDE2 wds:Q59071453-CE1B5ABE-0ED3-43E3-B5B4-175C4C3DF3DA wds:Q59071453-D8E6B5EC-6C3A-4BD9-8356-D2FA8011E614 wds:Q59071453-E2F34187-AFF8-43C3-8FE1-22933CB20C55 wds:Q59071453-FD5341A1-ADFE-4C1F-AB06-AE94EFDDDC98
cites work	ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery The absence of "heme-heme" interactions in hemoglobin Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits* Nuclear Magnetic Resonance Studies of Haemoglobin M Milwaukee Structure and subunit interaction of haemoglobin M Milwaukee. Stereochemistry of Cooperative Effects in Hemoglobin Effects of phosphate upon co binding kinetics and NMR spectra of hemoglobin valency hybrids Observation of allosteric transition in hemoglobin The Effect of Removal of C-terminal Residues on Cooperative Interactions in Hemoglobin Nuclear magnetic resonance studies of hemoglobins
author name string	wds:Q59071453-FC65F5B1-6274-434E-84E3-8CAF8DCBCF4C
author name string	M F Perutz
rdfs:label	Nature of Haem–Haem Interaction (en) Nature of Haem–Haem Interaction (nl)
skos:prefLabel	Nature of Haem–Haem Interaction (en) Nature of Haem–Haem Interaction (nl)
name	Nature of Haem–Haem Interaction (en) Nature of Haem–Haem Interaction (nl)
title	wds:Q59071453-24A70FD5-B06F-43B4-94A4-C82803200FE4
title	Nature of haem-haem interaction (en)
page(s)	wds:Q59071453-1B685801-2D62-4CF6-9AE3-28A7C0FE1CA7
page(s)	495-499
instance of	wds:Q59071453-2CD20B71-6FC3-4B3C-9FE8-0E8418A7D792
instance of	scholarly article
PubMed ID	wds:Q59071453-62D3FAAB-A98E-48B9-B6C1-9AD145D93DC5
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/12635193
PubMed ID	12635193
published in	wds:Q59071453-ADDA7451-5BDD-45ED-B5F9-6D24DB694944
published in	Nature
issue	wds:Q59071453-ACEB19F2-1000-40B3-9E89-83BB481FC4DC
volume	wds:Q59071453-627337A7-51D1-454D-ADAE-F3C079A23D9A
issue	5357
volume	237
DOI	wds:Q59071453-10618FFC-B1B8-4FE3-8C8D-0065702E712C
DOI	http://dx.doi.org/10.1038/237495A0
DOI	10.1038/237495A0
Dimensions Publication ID	wds:Q59071453-05512462-8034-4294-A853-345FBA011E3B
Dimensions Publication ID	1039868773
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q59071453
is cites work of	Mechanisms of hemoglobin adaptation to high altitude hypoxia Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism Resonance raman spectroscopic studies of heme proteins Proton nuclear magnetic resonance studies on hemoglobin: cooperative interactions and partially ligated intermediates Structure of erythrocruorin in different ligand states refined at 1·4 Å resolution Motions in Proteins Structure of fully liganded Hb ζ2β2s trapped in a tense conformation Structure of liganded T-state haemoglobin from cat (Felis silvestris catus), a low oxygen-affinity species, in two different crystal forms Proximal ligand control of heme iron coordination structure and reactivity with hydrogen peroxide: investigations of the myoglobin cavity mutant H93G with unnatural oxygen donor proximal ligands Coupling between oxidation state and hydrogen bond conformation in heme proteins Stereochemical Trigger for Initiating Cooperative Interaction of the Subunits During the Oxygenation of Cobaltohemoglobin Electronic configuration of high-spin imidazole-ligated iron(II) octaethylporphyrinates. Electronic configuration assignment and the importance of low-lying excited states in high-spin imidazole-ligated iron(II) porphyrinates Resonance Raman Spectra of Cobalt-Substituted Hemoglobin: Cooperativity and Displacement of the Cobalt Atom upon Oxygenation Binding Energy, Specificity, and Enzymic Catalysis: The Circe Effect Quaternary conformational changes in human hemoglobin studied by laser photolysis of carboxyhemoglobin Structure of the human antibody molecule kol (immunoglobulin G1): An electron density map at 5 Å resolution Analysis of the interaction of organic phosphates with hemoglobin Conformation and spin state in methemoglobin Hemoglobins and hemocyanins: Comparative aspects of structure and function Structural features and the reaction mechanism of cytochrome oxidase: iron and copper X-ray absorption fine structure Energy-structure correlation in metalloporphyrins and the control of oxygen binding by hemoglobin Doming modes and dynamics of model heme compounds Epistasis constrains mutational pathways of hemoglobin adaptation in high-altitude pikas Clinical implications of the loss of vasoactive nitric oxide during red blood cell storage Nuclear magnetic resonance studies of ferric porphyrins Molecular aspects of embryonic hemoglobin function Differences in Fe(II)-N epsilon(His-F8) stretching frequencies between deoxyhemoglobins in the two alternative quaternary structures Electron nuclear double resonance (ENDOR) investigation on myoglobin and hemoglobin. Allosteric interpretation of haemoglobin properties Structure and function of haemoglobin High-resolution proton NMR studies of low affinity hemoglobins. Structure and subunit interaction of haemoglobin M Milwaukee. Novel mechanisms of pH sensitivity in tuna hemoglobin: a structural explanation of the root effect The physico-chemical and functional properties of extracellular respiratory haemoglobins and chlorocruorins The Solution Structures of Tuna and Horse Cytochromes c

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