About: Quaternary and tertiary structure of haemerythrin

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scientific article published on 01 October 1975

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в жовтні 1975 (uk) im Oktober 1975 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'ochobre de 1975 (ast) scientific article published on 01 October 1975 (en)
publication date	wds:Q67328983-24BE83FA-A3B8-41FE-A1AC-237ADD2518A9
publication date	1975-10-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q67328983-3E077549-BF0C-41EA-BC91-1C12B4492C07
language of work or name	English
exact match	wds:Q67328983-B33654E0-C6A0-43CF-825A-9C8307B59DC2
exact match	https://scigraph.springernature.com/pub.10.1038/257818a0
cites work	wds:Q67328983-3E2D94CF-A64E-4EAC-886E-75BD5EB1DA2E wds:Q67328983-40770A4B-A132-471B-9873-B4984FDAE897 wds:Q67328983-761F4084-F851-4686-A27D-90060C5DA017 wds:Q67328983-7CAA5032-8DC8-460A-BEBC-D891C3711E98 wds:Q67328983-7DB01719-5D0F-4B28-9047-8F8020265806 wds:Q67328983-7E2A48C5-04D0-47F9-BA89-BBA2846AC601 wds:Q67328983-8BE68E0D-3AE0-4587-BC44-2FD241D13BED wds:Q67328983-9BA98322-2F9B-4CEF-B8F1-7E4A211AAEA3 wds:Q67328983-A15E2795-EDEC-47F3-9847-5D81D6203597 wds:Q67328983-A32045D0-9706-4D02-ADEF-F7E02BD5025B wds:Q67328983-A3F2B793-886A-4436-9617-AB41D21FC8FE wds:Q67328983-B034EC92-5DD7-44B3-B268-163A712FF0C1 wds:Q67328983-DFBE769E-93AD-4B36-83D0-CCB19C05E359
cites work	Solvent content of protein crystals Tertiary structure of myohemerythrin at low resolution Structure and Symmetry of Oligomeric Enzymes Molecular variants of Golfingia gouldii hemerythrin. Primary structure of the variants arising from five amino acid interchanges Tyrosine ligands to iron in hemerythrin. II. Specification of residues involved Complete chemical modification of the carboxyl groups in hemerythrin: effect on the active center and subunit interactions Implication of histidine at the active site of hemerythrin The role of tyrosine in the hemerythrin active site. An X-ray crystallographic study of hemerythrin Crystallography of hemerythrin. Crystals of myohemerythrin Structural studies on dendrostomum pyroides hemerythrin MERCAPTAN INVOLVEMENT IN DISSOCIATION AND RECONSTITUTION OF HEMERYTHRIN
author name string	wds:Q67328983-900B70AB-7FDB-443B-9A59-C4D899637190 wds:Q67328983-CEF3F450-F5CC-4C5F-B490-4F9449F74A8F
author name string	W A Hendrickson G L Klippenstein
rdfs:label	Quaternary and tertiary structure of haemerythrin (en) Quaternary and tertiary structure of haemerythrin (nl)
skos:prefLabel	Quaternary and tertiary structure of haemerythrin (en) Quaternary and tertiary structure of haemerythrin (nl)
name	Quaternary and tertiary structure of haemerythrin (en) Quaternary and tertiary structure of haemerythrin (nl)
author	wds:Q67328983-DC96B97C-A83E-405E-A07C-CA74BEC81362
author	Keith Ward
title	wds:Q67328983-06A8288D-95F1-4A87-B067-E550231FEFDB
title	Quaternary and tertiary structure of haemerythrin (en)
page(s)	wds:Q67328983-0CD156FF-6FB6-4654-85C6-C764C1E31E7A
page(s)	818-821
instance of	wds:Q67328983-071F924D-3128-42E9-9A82-C528F0A66D52
instance of	scholarly article
PubMed ID	wds:Q67328983-9CA516DD-79F9-412A-A23B-FE22C56E6D45
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/1186872
PubMed ID	1186872
published in	wds:Q67328983-BEAB4755-4564-455F-8278-422DE09FAA07
published in	Nature
issue	wds:Q67328983-8FEC6C59-0648-4CAB-942E-485104154C2E
volume	wds:Q67328983-D2192CED-3B6D-47DA-827F-9D9441C9FF85
issue	5529
volume	257
DOI	wds:Q67328983-2B598876-F28D-4808-B7CC-89BD50BC1BD7
DOI	http://dx.doi.org/10.1038/257818A0
DOI	10.1038/257818A0
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q67328983
is cites work of	Structural Aspects of Metal Liganding to Functional Groups in Proteins The anatomy and taxonomy of protein structure Structural and functional diversity in 4-α-helical proteins Structure of cytochrome c': a dimeric, high-spin haem protein Anomalous diffraction in crystallographic phase evaluation Helix packing and subunit conformation in horse spleen apoferritin Structure of the lamprey yolk lipid-protein complex lipovitellin-phosvitin at 2.8 Å resolution Iron superoxide dismutase from Escherichia coli at 3.1-A resolution: a structure unlike that of copper/zinc protein at both monomer and dimer levels Cloning and expression analysis of a cDNA that encodes a leech hemerythrin. Influence of solvent accessibility and intermolecular contacts on atomic mobilities in hemerythrins Hemerythrin: Alternative Oxygen Carrier Histidine placement in de novo-designed heme proteins Crystal structure of galactan-binding mouse immunoglobulin J539 Fab at 4.5-A resolution Motifs involved in protein-protein interactions Discovery and evolution of novel hemerythrin genes in annelid worms Molecular Evolution and Phylogeny of Sipunculan Hemerythrins Structure of trimeric haemerythrin A leucine residue "Gates" solvent but not O2 access to the binding pocket of phascolopsis gouldii hemerythrin Sequence and structural relationships in the cytokine family Viscosity dependence of O2 escape from respiratory proteins as a function of cosolvent molecular weight X-ray absorption spectroscopy of the dimeric iron site in azidomethemerythrin from Phascolopsis gouldii Recent Insights into the Diversity and Evolution of Invertebrate Hemerythrins and Extracellular Globins Sequence structure relationships in metalloproteins-I. A predictive model of hemerythrin
is cites work of	wds:Q36318786-A57BC8B3-A888-43BD-BFE6-1DBBCAED28D1 wds:Q37678139-74C1A966-BCBB-44B0-AA89-FAC524693CF7 wds:Q38313626-49E3B8B5-B402-4266-BCED-8B3175D95E2D wds:Q27729170-224FB67F-6C51-407D-9A1F-362D5EF8403F wds:Q34128483-905034E7-01D3-4755-ADF8-5CB127EAF0E4 wds:Q68453336-DC8360DA-C295-47F4-AC6F-B128902EEE11 wds:Q34025733-F69937E0-531C-4943-97CF-E4E5BE8AD874 wds:Q30664431-1C402DE4-3C95-4321-8427-FE79BC4DB4B6

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