About: Bernard L. Trumpower

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

Attributes	Values
rdf:type	Item
field of work	wds:Q112495091-8247D99A-B827-4F9E-9FCB-CC7E02280519 wds:Q112495091-9634C5EA-F8B5-437A-BDEA-601BB43F5586
field of work	biology biochemistry
description	باحت (ary) americký profesor biochemie a biologie, též specialista na výzkum enzymů, podílel se na vývoji antimalarik (cs)
rdfs:label	Bernard L. Trumpower (cs) Bernard L. Trumpower (en) Bernard L. Trumpower (sk) Bernard L. Trumpower (sq)
skos:prefLabel	Bernard L. Trumpower (cs) Bernard L. Trumpower (en) Bernard L. Trumpower (sk) Bernard L. Trumpower (sq)
name	Bernard L. Trumpower (cs) Bernard L. Trumpower (en) Bernard L. Trumpower (sk) Bernard L. Trumpower (sq)
given name	wds:Q112495091-FDDC78D5-8266-4C6A-86CB-9D4B8F8ABB53
given name	Bernard
instance of	wds:Q112495091-4EB42068-2813-49A2-8040-B63DED918310
NL CR AUT ID	wds:Q112495091-66D3DC66-43B7-4C17-9CDD-A7CA51295F51
instance of	Homo sapiens
NL CR AUT ID	mub2015891521
occupation	wds:Q112495091-60E5FF82-9455-40F8-80AE-CC7E4EA9290B
languages spoken, written or signed	wds:Q112495091-FFFC395E-D615-4645-ACD8-C3FA595D6C2A
sex or gender	wds:Q112495091-E1DC4C8B-E003-4231-8E09-8CF689198318
VIAF ID	wds:Q112495091-CB2AC23B-B0A2-429C-9125-A3193653E91C
date of birth	wds:Q112495091-3AD210CF-1F7B-43B7-9D24-143C41A50C80
date of death	wds:Q112495091-4CB3B8C8-CB2E-44C8-B838-CEA26F6C3CCB
family name	wds:Q112495091-A01BB086-61AC-47A2-9CB1-6D21C08EEB00
VIAF ID	http://viaf.org/viaf/816144928096854341320
occupation	professor
languages spoken, written or signed	English
sex or gender	male
VIAF ID	816144928096854341320
date of birth	1943-01-01 00:00:00Z (xsd:dateTime)
date of death	2014-01-01 00:00:00Z (xsd:dateTime)
family name	Trumpower
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q112495091
is author of	Biogenesis of the yeast cytochrome bc1 complex. Direct demonstration of half-of-the-sites reactivity in the dimeric cytochrome bc1 complex: enzyme with one inactive monomer is fully active but unable to activate the second ubiquinol oxidation site in response to ligand binding at the ubiquinone r Regulatory interactions in the dimeric cytochrome bc(1) complex: the advantages of being a twin Inhibitory analogs of ubiquinol act anti-cooperatively on the Yeast cytochrome bc1 complex. Evidence for an alternating, half-of-the-sites mechanism of ubiquinol oxidation. Molecular basis for atovaquone binding to the cytochrome bc1 complex Modeling the molecular basis of atovaquone resistance in parasites and pathogenic fungi RPL29 codes for a non-essential protein of the 60S ribosomal subunit in Saccharomyces cerevisiae and exhibits synthetic lethality with mutations in genes for proteins required for subunit coupling Structure of the yeast cytochrome bc1 complex with a hydroxyquinone anion Qo site inhibitor bound A comparison of stigmatellin conformations, free and bound to the photosynthetic reaction center and the cytochrome bc1 complex The rate-limiting step in the cytochrome bc1 complex (Ubiquinol-Cytochrome c Oxidoreductase) is not changed by inhibition of cytochrome b-dependent deprotonation: implications for the mechanism of ubiquinol oxidation at center P of the bc1 complex Mutational Analysis of Cytochrome b at the Ubiquinol Oxidation Site of Yeast Complex III Elimination of the Disulfide Bridge in the Rieske Iron−Sulfur Protein Allows Assembly of the [2Fe-2S] Cluster into the Rieske Protein but Damages the Ubiquinol Oxidation Site in the Cytochrome bc1 Complex Membrane potential greatly enhances superoxide generation by the cytochrome bc1 complex reconstituted into phospholipid vesicles Protonmotive pathways and mechanisms in the cytochrome bc1 complex A concerted, alternating sites mechanism of ubiquinol oxidation by the dimeric cytochrome bc(1) complex The dimeric structure of the cytochrome bc(1) complex prevents center P inhibition by reverse reactions at center N. Anti-cooperative oxidation of ubiquinol by the yeast cytochrome bc1 complex. Rapid electron transfer between monomers when the cytochrome bc1 complex dimer is reduced through center N. Regulatory interactions between ubiquinol oxidation and ubiquinone reduction sites in the dimeric cytochrome bc1 complex Asymmetric and redox-specific binding of quinone and quinol at center N of the dimeric yeast cytochrome bc1 complex. Consequences for semiquinone stabilization Design of a ruthenium-labeled cytochrome c derivative to study electron transfer with the cytochrome bc1 complex Parameters determining the relative efficacy of hydroxy-naphthoquinone inhibitors of the cytochrome bc1 complex Molecular basis for atovaquone resistance in Pneumocystis jirovecii modeled in the cytochrome bc(1) complex of Saccharomyces cerevisiae Inhibition of the yeast cytochrome bc1 complex by ilicicolin H, a novel inhibitor that acts at the Qn site of the bc1 complex. Further insights into the assembly of the yeast cytochrome bc1 complex based on analysis of single and double deletion mutants lacking supernumerary subunits and cytochrome b. Recapitulation in Saccharomyces cerevisiae of cytochrome b mutations conferring resistance to atovaquone in Pneumocystis jiroveci Identification and characterization of cytochrome bc1 subcomplexes in mitochondria from yeast with single and double deletions of genes encoding cytochrome bc1 subunits Mutations in cytochrome b that affect kinetics of the electron transfer reactions at center N in the yeast cytochrome bc1 complex DB75, a novel trypanocidal agent, disrupts mitochondrial function in Saccharomyces cerevisiae Similar transition states mediate the Q-cycle and superoxide production by the cytochrome bc1 complex Cytochrome b mutations that modify the ubiquinol-binding pocket of the cytochrome bc1 complex and confer anti-malarial drug resistance in Saccharomyces cerevisiae Superoxide anion generation by the cytochrome bc1 complex Introduction of cytochrome b mutations in Saccharomyces cerevisiae by a method that allows selection for both functional and non-functional cytochrome b proteins Investigating the Qn site of the cytochrome bc1 complex in Saccharomyces cerevisiae with mutants resistant to ilicicolin H, a novel Qn site inhibitor. Design of anti-parasitic and anti-fungal hydroxy-naphthoquinones that are less susceptible to drug resistance Differential efficacy of inhibition of mitochondrial and bacterial cytochrome bc1 complexes by center N inhibitors antimycin, ilicicolin H and funiculosin Chapter 27 An improved method for introducing point mutations into the mitochondrial cytochrome B gene to facilitate studying the role of cytochrome B in the formation of reactive oxygen species. Asymmetric binding of stigmatellin to the dimeric Paracoccus denitrificans bc1 complex: evidence for anti-cooperative ubiquinol oxidation and communication between center P ubiquinol oxidation sites Disulfide bond formation involves a quinhydrone-type charge–transfer complex Evidence that the assembly of the yeast cytochrome bc1 complex involves the formation of a large core structure in the inner mitochondrial membrane Failure to insert the iron-sulfur cluster into the Rieske iron-sulfur protein impairs both center N and center P of the cytochrome bc1 complex. Bcs1p can rescue a large and productive cytochrome bc1 complex assembly intermediate in the inner membrane of yeast mitochondria Combining Inhibitor Resistance-conferring Mutations in Cytochrome b Creates Conditional Synthetic Lethality in Saccharomyces cerevisiae Ilicicolin Inhibition and Binding at Center N of the Dimeric Cytochrome bc1 Complex Reveal Electron Transfer and Regulatory Interactions between Monomers Probing binding determinants in center P of the cytochrome bc(1) complex using novel hydroxy-naphthoquinones Molecular basis of Toxoplasma gondii atovaquone resistance modeled in Saccharomyces cerevisiae Multiple cytochrome B mutations may cause atovaquone resistance
is author of	wds:Q34534276-33BE7B77-4343-42BA-9542-4BF31764F596 wds:Q35685361-5DC348A2-4A56-479F-AE4E-48A470FED476 wds:Q37012903-4F0240DA-D123-41AF-9C85-08052BB3E058 wds:Q41982283-9A16E79A-9A9F-499F-B728-85145261FB00 wds:Q46712458-9B859BFB-BDAA-4C99-A726-2D15B395AD0C wds:Q60319645-B01FA555-C9F2-4580-9601-91F636AA4C41 wds:Q57828203-377A120F-030A-4F7D-86D7-731394EEADD9 wds:Q80462663-ACC3CAA2-C5CD-49AA-8802-AE065FB8C5E8 wds:Q36934557-E51433DC-EBE8-432E-B368-AD796E3E1244 wds:Q43158594-FBE068F9-8046-4DEF-8454-612526197762 wds:Q44657957-19E366AA-BA39-4CEE-951D-7E873C0BF1BB wds:Q60319632-94CC88D7-926A-47A8-AEC7-29B333AB24AE

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