About: Miles D. Houslay

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

biochemist

Attributes	Values
rdf:type	Item
description	biochemist (en) biochemicus (nl)
exact match	wds:Q37378801-B8D9E39E-91BB-45DB-869E-39BE1EBD8421
exact match	https://scigraph.springernature.com/person.01306405173.45
rdfs:label	Miles D Houslay (es) Miles D Houslay (nl) Miles D. Houslay (en) Miles D. Houslay (it) Miles D. Houslay (sq) Miles D. Houslay (tr)
skos:prefLabel	Miles D Houslay (es) Miles D Houslay (nl) Miles D. Houslay (en) Miles D. Houslay (it) Miles D. Houslay (sq) Miles D. Houslay (tr)
name	Miles D Houslay (es) Miles D Houslay (nl) Miles D. Houslay (en) Miles D. Houslay (it) Miles D. Houslay (sq) Miles D. Houslay (tr)
given name	wds:Q37378801-3161A828-B92E-4CD9-B19F-4BA9B793B059
given name	Miles
instance of	wds:Q37378801-88470519-62E5-47AE-AEB8-F2820E6A7F74
instance of	Homo sapiens
award received	wds:Q37378801-4b43bcd1-4c77-ad1a-afd4-3caeb6fa7f57
award received	Colworth Medal
skos:altLabel	Miles Houslay (en)
Nationale Thesaurus voor Auteursnamen ID	wds:Q37378801-86eb826a-ff11-4a9f-9c51-25a1426b3e6c
occupation	wds:Q37378801-1BB9B0C1-B350-4747-B1C6-984F6821FACE
employer	wds:Q37378801-4901328B-05AA-4D16-930E-D647585AC704 wds:Q37378801-4F5D9A3C-1868-4AC3-BA49-93D23D36E5AD wds:Q37378801-7B79DE29-F294-4CF3-BB2D-3D6DA994E3AC wds:Q37378801-B8EB0806-3925-4D7D-A443-D1E37EDB5243
KBR person ID	wds:Q37378801-ED5EAF47-0A23-4D3D-B6E0-5095E022CB60
NUKAT ID	wds:Q37378801-926AFC29-830B-4AD9-B3D8-E00BA0A8FA44
sex or gender	wds:Q37378801-B0661A19-7DE2-4033-8988-C884E0070760
ISNI	wds:Q37378801-5BFBB0C7-7EEC-4FCA-8872-D39B1C6BF353
VIAF ID	wds:Q37378801-4F6D4E42-87BC-436C-B50A-FB3547810C7F
Library of Congress authority ID	wds:Q37378801-29BCBDDF-7392-411B-968B-A2704EAC59F1
Bibliothèque nationale de France ID	wds:Q37378801-BAEE31F5-8766-4264-B8FC-30160F3B9BD3
IdRef ID	wds:Q37378801-4D771773-74AE-4856-86A4-90EADC94E86C
SHARE Catalogue author ID	wds:Q37378801-8CA319EC-DB59-4380-BD2C-265A9C85F242
date of birth	wds:Q37378801-41D523F3-16DD-46EE-ACC8-1E111E964F83
educated at	wds:Q37378801-418C03D6-456C-4E10-BF22-C1B23F8F3A4B
WorldCat Identities ID (superseded)	wds:Q37378801-A5693124-C1CE-430D-B55C-0C96DB7795F9
National Library of Israel J9U ID	wds:Q37378801-33EF5AFC-7C8B-4D07-8DA4-504A38DB8D25
Nationale Thesaurus voor Auteursnamen ID	http://data.bibliotheken.nl/id/thes/p06991897X
VIAF ID	http://viaf.org/viaf/51759249
Library of Congress authority ID	http://id.loc.gov/authorities/names/n81097074
Bibliothèque nationale de France ID	http://data.bnf.fr/ark:/12148/cb123248089#about
IdRef ID	http://www.idref.fr/032164068/id
Nationale Thesaurus voor Auteursnamen ID	06991897X
occupation	biochemist
employer	University of Manchester University of Glasgow University of Strathclyde King's College London
KBR person ID	13997329
NUKAT ID	n2005115907
sex or gender	male
ISNI	0000000109006597
VIAF ID	51759249
Library of Congress authority ID	n81097074
Bibliothèque nationale de France ID	123248089
IdRef ID	032164068
SHARE Catalogue author ID	92478
date of birth	2000-01-01 00:00:00Z (xsd:dateTime)
educated at	John Ffowcs Williams
WorldCat Identities ID (superseded)	lccn-n81097074
National Library of Israel J9U ID	987007279012405171
ORCID iD	wds:Q37378801-82F9BE9B-AEA2-4E60-8D50-DD37B8EB2594
Dimensions author ID	wds:Q37378801-184A826C-D0F2-4706-BC4A-77FD7F6F9364
ORCID iD	https://orcid.org/0000-0002-3826-8091
ORCID iD	0000-0002-3826-8091
Dimensions author ID	01306405173.45
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q37378801
is author of	Targeting of cyclic AMP degradation to beta 2-adrenergic receptors by beta-arrestins UCR1 and UCR2 domains unique to the cAMP-specific phosphodiesterase family form a discrete module via electrostatic interactions. Upregulation of cAMP-specific PDE-4 activity following ligation of the TCR complex on thymocytes is blocked by selective inhibitors of protein kinase C and tyrosyl kinases β-Arrestin 1 inhibits the GTPase-activating protein function of ARHGAP21, promoting activation of RhoA following angiotensin II type 1A receptor stimulation. Rat liver mitochondrial monoamine oxidase. A change in the reaction mechanism on solubilization A phosphodiesterase 3B-based signaling complex integrates exchange protein activated by cAMP 1 and phosphatidylinositol 3-kinase signals in human arterial endothelial cells Thrombin, unlike vasopressin, appears to stimulate two distinct guanine nucleotide regulatory proteins in human platelets Determination of the structure of the N-terminal splice region of the cyclic AMP-specific phosphodiesterase RD1 (RNPDE4A1) by 1H NMR and identification of the membrane association domain using chimeric constructs Molecular cloning and expression, in both COS-1 cells and S. cerevisiae, of a human cytosolic type-IVA, cyclic AMP specific phosphodiesterase (hPDE-IVA-h6.1) The insulin receptor tyrosyl kinase phosphorylates holomeric forms of the guanine nucleotide regulatory proteins Gi and Go. Diabetes induces selective alterations in the expression of protein kinase C isoforms in hepatocytes G-protein linked receptors: a family probed by molecular cloning and mutagenesis procedures Altered Expression of PDE1 and PDE4 Cyclic Nucleotide Phosphodiesterase Isoforms in 7-oxo-prostacyclin-preconditioned Rat Heart Tyrosine 302 in RACK1 is essential for insulin-like growth factor-I-mediated competitive binding of PP2A and beta1 integrin and for tumor cell proliferation and migration Disrupted-in-Schizophrenia 1 (DISC1) regulates spines of the glutamate synapse via Rac1 Investigation of extracellular signal-regulated kinase 2 mitogen-activated protein kinase phosphorylation and regulation of activity of PDE4 cyclic adenosine monophosphate-specific phosphodiesterases Adaptation in cyclic AMP signalling processes: A central role for cyclic AMP phosphodiesterases Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases Cyclic AMP-dependent transcriptional up-regulation of phosphodiesterase 4D5 in human airway smooth muscle cells. Identification and characterization of a novel PDE4D5 promoter Mdm2 directs the ubiquitination of beta-arrestin-sequestered cAMP phosphodiesterase-4D5 Keynote review: phosphodiesterase-4 as a therapeutic target

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