About: Madeline Shea

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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	Forscher (de) ricercatore (it) investigador (es) chercheur (fr) wetenschapper (nl) дослідниця (uk) 研究者 (zh) American biochemist (en)
rdfs:label	M A Shea (ast) Madeline Shea (cy) Madeline Shea (de) Madeline Shea (en) Madeline Shea (es) Madeline Shea (fr) Madeline Shea (it) Madeline Shea (nl) Madeline Shea (pt) Madeline Shea (sq) Madeline Shea (sv) Madeline Shea (en-gb) Madeline Shea (pt-br)
skos:prefLabel	M A Shea (ast) Madeline Shea (cy) Madeline Shea (de) Madeline Shea (en) Madeline Shea (es) Madeline Shea (fr) Madeline Shea (it) Madeline Shea (nl) Madeline Shea (pt) Madeline Shea (sq) Madeline Shea (sv) Madeline Shea (en-gb) Madeline Shea (pt-br)
name	M A Shea (ast) Madeline Shea (cy) Madeline Shea (de) Madeline Shea (en) Madeline Shea (es) Madeline Shea (fr) Madeline Shea (it) Madeline Shea (nl) Madeline Shea (pt) Madeline Shea (sq) Madeline Shea (sv) Madeline Shea (en-gb) Madeline Shea (pt-br)
Scopus author ID	wds:Q67280365-06CBDBB0-C05B-4A91-8181-487EA20D0AA7
Scopus author ID	7202221513
given name	wds:Q67280365-5B7F7B1A-CC3F-4EBA-A0DA-BD6D89F23333
given name	Madeline
instance of	wds:Q67280365-43FFDAEB-A516-4280-A686-9F4FB91F102C
instance of	Homo sapiens
award received	wds:Q67280365-1ce648fc-4dc4-12e2-c557-973f8d080ac0 wds:Q67280365-2d9f73ac-4354-584a-8459-9ddf13a49c3f
award received	Fellow of the American Association for the Advancement of Science Emily M. Gray Award
Academic Tree ID	wds:Q67280365-91AD0F21-4271-4179-90BA-CAD77252A406
Academic Tree ID	393660
skos:altLabel	M. A. Shea (en) Madeline A. Shea (en)
occupation	wds:Q67280365-95548307-BBB9-43D5-90D7-BFB8E705BC77
employer	wds:Q67280365-8C7AFA0B-6572-4C2A-ACD2-CE3369EFDDD4 wds:Q67280365-bf4db3c1-4fd5-0ca8-7fb0-fc45d36121bd
sex or gender	wds:Q67280365-5555f306-4375-cd77-b3ef-246064911e5e
VIAF ID	wds:Q67280365-710bcc29-48a0-ab4e-1307-667692b295f4
Library of Congress authority ID	wds:Q67280365-237fa2a7-4998-a79c-4ec5-bf33c9baca5c
educated at	wds:Q67280365-D1A9D21C-D268-480D-9929-4950D58FC831 wds:Q67280365-E5261284-68E1-41E3-8F02-CC880557E64C
family name	wds:Q67280365-d7ded4f1-4835-1402-8ac7-b6416605d9bd
VIAF ID	http://viaf.org/viaf/6448032
Library of Congress authority ID	http://id.loc.gov/authorities/names/n87148724
occupation	biochemist
employer	Roy J. and Lucille A. Carver College of Medicine University of Iowa
sex or gender	female organism
VIAF ID	6448032
Library of Congress authority ID	n87148724
educated at	Johns Hopkins University California Institute of Technology
family name	Shea
ORCID iD	wds:Q67280365-96C08726-7D24-48BA-AA8A-5D1B77363FF8
ORCID iD	https://orcid.org/0000-0003-0814-7069
ORCID iD	0000-0003-0814-7069
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q67280365
is author of	Quantitative model for gene regulation by lambda phage repressor The NMDA Receptor NR1 C1 Region Bound to Calmodulin: Structural Insights into Functional Differences between Homologous Domains The OR control system of bacteriophage lambda. A physical-chemical model for gene regulation The neuronal voltage-dependent sodium channel type II IQ motif lowers the calcium affinity of the C-domain of calmodulin. Calcium binding to calmodulin mutants monitored by domain-specific intrinsic phenylalanine and tyrosine fluorescence. Quantitative DNase footprint titration: a method for studying protein-DNA interactions Regulation of calcium/calmodulin-dependent protein kinase II docking to N-methyl-D-aspartate receptors by calcium/calmodulin and alpha-actinin. Displacement of alpha-actinin from the NMDA receptor NR1 C0 domain By Ca2+/calmodulin promotes CaMKII binding HEXIM1 is a promiscuous double-stranded RNA-binding protein and interacts with RNAs in addition to 7SK in cultured cells. Calcium-induced conformational switching of Paramecium calmodulin provides evidence for domain coupling Subunit hybridization studies of partially ligated cyanomethemoglobins using a cryogenic method. Evidence for three allosteric states. Recognition of β-calcineurin by the domains of calmodulin: thermodynamic and structural evidence for distinct roles Structural and Energetic Determinants of Apo Calmodulin Binding to the IQ Motif of the NaV1.2 Voltage-Dependent Sodium Channel Calcium-induced interactions of calmodulin domains revealed by quantitative thrombin footprinting of Arg37 and Arg106.

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