About: Sanford Bernstein

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

researcher

Attributes	Values
rdf:type	Item
field of work	wds:Q42880156-bb849037-136d-4647-a4d8-3b8ef636715f
field of work	biology
description	researcher (en) 연구원 (ko) গবেষক (bn) 研究者 (ja) ഗവേഷകൻ (ml) wetenschapper (nl) дослідник (uk) باحت (ary) 研究者 (zh) հետազոտող (hy) hulumtues (sq)
rdfs:label	Sanford Bernstein (en) Sanford Bernstein (es) Sanford Bernstein (nl) Sanford Bernstein (sl) Sanford Bernstein (ast)
skos:prefLabel	Sanford Bernstein (en) Sanford Bernstein (es) Sanford Bernstein (nl) Sanford Bernstein (sl) Sanford Bernstein (ast)
name	Sanford Bernstein (en) Sanford Bernstein (es) Sanford Bernstein (nl) Sanford Bernstein (sl) Sanford Bernstein (ast)
affiliation	wds:Q42880156-57d356ef-9156-434e-9a69-02c197362e23 wds:Q42880156-640c36ef-c30c-49df-ba8f-6f06f60ef7be
affiliation	San Diego State University College of Sciences San Diego State University Department of Biology
Scopus author ID	wds:Q42880156-9AFD86C5-B885-41E2-95F2-9A7D70C9ECA2
Scopus author ID	7201589050
given name	wds:Q42880156-3589DE32-F813-4312-B2EE-5A9D178515AA
given name	Sanford
instance of	wds:Q42880156-D275FF2C-22C1-4971-94E0-71C27D15A305
instance of	Homo sapiens
occupation	wds:Q42880156-73e0293f-7ab0-4ac6-af87-64fac5fb8161
NUKAT ID	wds:Q42880156-3DDA3E35-1E62-46A1-A114-DCBB7617413F
sex or gender	wds:Q42880156-53B03427-B069-4C8D-8AC9-8C83C1380D5C
ISNI	wds:Q42880156-F753D643-375E-4DC5-BB8F-B3587465FA4F
VIAF ID	wds:Q42880156-89FE4797-C4FE-4DCB-980D-5FC555772671
Library of Congress authority ID	wds:Q42880156-4b7d3f1f-ed24-43b0-ac84-1dfe88de9c9b
IdRef ID	wds:Q42880156-f7bf799a-89f7-4402-818b-71a95e861ca1
position held	wds:Q42880156-1AECBC00-8F21-47E6-8B3E-3C9F904C7127
SHARE Catalogue author ID	wds:Q42880156-DB9EF30E-9E4A-4231-A064-37F1503E9E6D
educated at	wds:Q42880156-fc163420-8c89-4903-aede-8137c08151b0
family name	wds:Q42880156-819BA6CC-AC78-4223-A460-7FD7D1A30037
National Library of Israel J9U ID	wds:Q42880156-CB1933CF-13B1-4884-BDEE-350374B629E0
VIAF ID	http://viaf.org/viaf/45851792
Library of Congress authority ID	http://id.loc.gov/authorities/names/n88106017
IdRef ID	http://www.idref.fr/123604362/id
occupation	university teacher
NUKAT ID	n96107895
sex or gender	male
ISNI	0000000031303996
VIAF ID	45851792
Library of Congress authority ID	n88106017
IdRef ID	123604362
position held	professor emeritus
SHARE Catalogue author ID	92213
educated at	Center for Advanced Studies
family name	Bernstein
National Library of Israel J9U ID	987007429964105171
ORCID iD	wds:Q42880156-A9A5F0E4-7F42-412B-880D-0FCBD827D2CC
ORCID iD	https://orcid.org/0000-0001-7094-5390
ORCID iD	0000-0001-7094-5390
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q42880156
is author of	Paramyosin phosphorylation site disruption affects indirect flight muscle stiffness and power generation in Drosophila melanogaster Defects in the Drosophila myosin rod permit sarcomere assembly but cause flight muscle degeneration. Similarities and differences between frozen-hydrated, rigor acto-S1 complexes of insect flight and chicken skeletal muscles A mighty small heart: the cardiac proteome of adult Drosophila melanogaster Kinetic analysis of Drosophila muscle myosin isoforms suggests a novel mode of mechanochemical coupling Semi-automated Optical Heartbeat Analysis of small hearts. UCS proteins: managing the myosin motor alphaB-crystallin maintains skeletal muscle myosin enzymatic activity and prevents its aggregation under heat-shock stress Fine tuning a molecular motor: the location of alternative domains in the Drosophila myosin head. Genetic approaches to understanding muscle development. Alternative S2 hinge regions of the myosin rod affect myofibrillar structure and myosin kinetics. Alternative N-terminal regions of Drosophila myosin heavy chain tune muscle kinetics for optimal power output. An alternative domain near the ATP binding pocket of Drosophila myosin affects muscle fiber kinetics The myosin converter domain modulates muscle performance An alternative domain near the nucleotide-binding site of Drosophila muscle myosin affects ATPase kinetics Myosin transducer mutations differentially affect motor function, myofibril structure, and the performance of skeletal and cardiac muscles Expression of the inclusion body myopathy 3 mutation in Drosophila depresses myosin function and stability and recapitulates muscle inclusions and weakness Alternative relay domains of Drosophila melanogaster myosin differentially affect ATPase activity, in vitro motility, myofibril structure and muscle function Myosin storage myopathy mutations yield defective myosin filament assembly in vitro and disrupted myofibrillar structure and function in vivo. Alternative exon-encoded regions of Drosophila myosin heavy chain modulate ATPase rates and actin sliding velocity. Spatially and temporally regulated expression of myosin heavy chain alternative exons during Drosophila embryogenesis. Mapping interactions between myosin relay and converter domains that power muscle function Mutating the converter-relay interface of Drosophila myosin perturbs ATPase activity, actin motility, myofibril stability and flight ability Alternative exon 9-encoded relay domains affect more than one communication pathway in the Drosophila myosin head Two Drosophila myosin transducer mutants with distinct cardiomyopathies have divergent ADP and actin affinities Alternative versions of the myosin relay domain differentially respond to load to influence Drosophila muscle kinetics Transgenic expression and purification of myosin isoforms using the Drosophila melanogaster indirect flight muscle system Alternative S2 hinge regions of the myosin rod differentially affect muscle function, myofibril dimensions and myosin tail length. Huntington's disease induced cardiac amyloidosis is reversed by modulating protein folding and oxidative stress pathways in the Drosophila heart Transformation of Drosophila melanogaster with the wild-type myosin heavy-chain gene: rescue of mutant phenotypes and analysis of defects caused by overexpression

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