About: John S. Olson

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An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

American biochemist

Attributes	Values
rdf:type	Item
description	ikertzailea (eu) 연구원 (ko) 研究者 (ja) araştırmacı (tr) wetenschapper (nl) дослідник (uk) эрдэмтэн (mn) वैज्ञानिक (hi) изилдөөчү (ky) 研究者 (zh) American biochemist (en) հետազոտող (hy) amerykański biochemik (pl)
rdfs:label	John Olson (pl) John S Olson (nl) John S Olson (sl) John S. Olson (en) John S. Olson (es)
skos:prefLabel	John Olson (pl) John S Olson (nl) John S Olson (sl) John S. Olson (en) John S. Olson (es)
name	John Olson (pl) John S Olson (nl) John S Olson (sl) John S. Olson (en) John S. Olson (es)
LinkedIn personal profile ID	wds:Q55835345-2d8ae54c-430a-c4aa-f079-8bf510b269c2
LinkedIn personal profile ID	john-olson-7bba1a63
Scopus author ID	wds:Q55835345-28100A92-4432-48E8-A462-7CF3773F556B
Scopus author ID	7402882490
given name	wds:Q55835345-D663BB73-FB09-426B-952C-D214F7B71662
given name	John
instance of	wds:Q55835345-F16428B2-DD51-4716-AFE5-67EFF76D206E
instance of	Homo sapiens
award received	wds:Q55835345-3ad1e858-4e11-2181-5acd-df4c6d9d22be
award received	Emily M. Gray Award
Academic Tree ID	wds:Q55835345-91439938-4715-02b6-6835-786d1f487409
Academic Tree ID	66668
Google Scholar author ID	wds:Q55835345-8ac04221-4bb0-e46d-fdb2-2d08ab28d39e
Google Scholar author ID	vUDs6oEAAAAJ
skos:altLabel	John Olson (en) John Steve Olson (en)
occupation	wds:Q55835345-3d08c3e7-425c-b56d-0909-88418a2260e3 wds:Q55835345-D29C9A52-9F8A-41B9-9521-C190C0F6EB58
employer	wds:Q55835345-0C481D76-2A32-48C8-9E54-9D4E452F1CF0 wds:Q55835345-815F9FD2-D6D7-441A-AD13-490C80F7D4AF
sex or gender	wds:Q55835345-1a1054d1-455a-990e-6f2e-5f1cc88b1556
country of citizenship	wds:Q55835345-216878ec-43d4-95ec-0c86-0a649e9c80e6
educated at	wds:Q55835345-0dbfe18a-409c-2c7b-1d5e-3487631f6c8d wds:Q55835345-a828bc14-455a-c218-149a-5ec569613061
family name	wds:Q55835345-99C49CEF-E56F-43B4-89C3-5468B05F225B
occupation	researcher biochemist
employer	University of Michigan Rice University
sex or gender	male
country of citizenship	United States of America
educated at	Cornell University University of Illinois at Urbana–Champaign
family name	Olson
ORCID iD	wds:Q55835345-E2AFCF35-9AA4-4799-82B2-8D265387E0D2
ORCID iD	https://orcid.org/0000-0002-0760-5403
ORCID iD	0000-0002-0760-5403
Arnet Miner author ID	wds:Q55835345-9adcf6cf-4481-ed09-9289-232b5959fdad
Arnet Miner author ID	54096c10dabfae450f482f0d
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q55835345
is author of	Water and ligand entry in myoglobin: assessing the speed and extent of heme pocket hydration after CO photodissociation Crystal structure of a nonsymbiotic plant hemoglobin High resolution crystal structures of the deoxy, oxy, and aquomet forms of cobalt myoglobin Mechanism of hydrogen cyanide binding to myoglobin. How do heme-protein sensors exclude oxygen? Lessons learned from cytochrome c', Nostoc puntiforme heme nitric oxide/oxygen-binding domain, and soluble guanylyl cyclase The Oxygen and Carbon Monoxide Reactions of Heme Oxygenase Dynamics of carbon monoxide binding to CooA. Real-time tracking of CO migration and binding in the α and β subunits of human hemoglobin via 150-ps time-resolved Laue crystallography Ligand pathways in myoglobin: a review of Trp cavity mutations Blocking the Gate to Ligand Entry in Human Hemoglobin Mechanism of NO-induced oxidation of myoglobin and hemoglobin Myoglobin as a model system for designing heme protein based blood substitutes Distal histidine stabilizes bound O2 and acts as a gate for ligand entry in both subunits of adult human hemoglobin Kinetic spectroscopy of heme hydration and ligand binding in myoglobin and isolated hemoglobin chains: an optical window into heme pocket water dynamics No scavenging and the hypertensive effect of hemoglobin-based blood substitutes Enhancement of recombinant hemoglobin production in Escherichia coli BL21(DE3) containing the Plesiomonas shigelloides heme transport system Enhancing stability and expression of recombinant human hemoglobin in E. coli: Progress in the development of a recombinant HBOC source Interfacial and distal-heme pocket mutations exhibit additive effects on the structure and function of hemoglobin Modulating distal cavities in the α and β subunits of human HbA reveals the primary ligand migration pathway Mapping the pathways for O2 entry into and exit from myoglobin. Bis-methionyl Coordination in the Crystal Structure of the Heme-binding Domain of the Streptococcal Cell Surface Protein Shp Biochemical Fates of α Hemoglobin Bound to α Hemoglobin-stabilizing Protein AHSP Determination of ligand pathways in globins: apolar tunnels versus polar gates Differential Function of Lip Residues in the Mechanism and Biology of an Anthrax Hemophore Picosecond time-resolved X-ray crystallography: probing protein function in real time Heme transfer to the bacterial cell envelope occurs via a secreted hemophore in the Gram-positive pathogen Bacillus anthracis A Bacillus anthracis S-layer homology protein that binds heme and mediates heme delivery to IsdC The five near-iron transporter (NEAT) domain anthrax hemophore, IsdX2, scavenges heme from hemoglobin and transfers heme to the surface protein IsdC. Pathway for heme uptake from human methemoglobin by the iron-regulated surface determinants system of Staphylococcus aureus Steady-state and Transient Kinetics ofEscherichia coliNitric-oxide Dioxygenase (Flavohemoglobin) Kinetics of α-globin binding to α-hemoglobin stabilizing protein (AHSP) indicate preferential stabilization of hemichrome folding intermediate

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