About: John Tesmer

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: John Tesmer Goto Sponge NotDistinct Permalink

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

American biophysicist and pharmacologist

Attributes	Values
rdf:type	Item
description	Forscher (de) forskare (sv) ikertzailea (eu) 연구원 (ko) ricercatore (it) investigador (es) araştırmacı (tr) chercheur (fr) wetenschapper (nl) дослідник (uk) эрдэмтэн (mn) वैज्ञानिक (hi) 研究者 (zh) American biophysicist and pharmacologist (en)
rdfs:label	J J Tesmer (es) J J Tesmer (nl) J J Tesmer (ast) John Tesmer (en)
skos:prefLabel	J J Tesmer (es) J J Tesmer (nl) J J Tesmer (ast) John Tesmer (en)
name	J J Tesmer (es) J J Tesmer (nl) J J Tesmer (ast) John Tesmer (en)
Scopus author ID	wds:Q68034798-FF30E5A3-957B-4B00-8E7C-13A919FE90DA
Scopus author ID	7005472035
given name	wds:Q68034798-BEDF4B41-AB6A-43E8-9A09-6813D8519BE7
given name	John
instance of	wds:Q68034798-D91045F1-F49F-4BE7-B10C-B8DA0673747F
instance of	Homo sapiens
award received	wds:Q68034798-8e307804-4ad5-4592-e3a5-e45f1e36e6d9 wds:Q68034798-fcb84fb2-4801-22fe-762d-0d2c82ba02bb
award received	Fellow of the American Association for the Advancement of Science John J. Abel Award
skos:altLabel	John J. G. Tesmer (en)
occupation	wds:Q68034798-1de8a199-4788-ffa9-4669-8d44374145a2 wds:Q68034798-3d4e9c2e-4b2f-c69f-edd4-0cc37524a21a wds:Q68034798-BBFAB1CF-1776-4D11-89D6-947B70200FA6
employer	wds:Q68034798-2DCC64F5-F97F-45FD-9A76-008E5E4FBB87
sex or gender	wds:Q68034798-9FFC4D0A-9E94-4889-88FB-E2BEA559A747
VIAF ID	wds:Q68034798-37dca044-6621-4e54-a798-974ef4f9a78d
IdRef ID	wds:Q68034798-1BAFBFD2-5AB6-47CC-AC59-53096B87DE34
country of citizenship	wds:Q68034798-5e52f400-415e-0dfb-d861-b406c5a7642a
educated at	wds:Q68034798-295C46EE-C10D-4252-A7C7-4A7CF0712C61 wds:Q68034798-9B9CFD09-2DCE-4937-870A-0E250779896E
VIAF ID	http://viaf.org/viaf/86279474
IdRef ID	http://www.idref.fr/25271847X/id
occupation	biophysicist pharmacologist researcher
employer	Purdue University
sex or gender	male
VIAF ID	86279474
IdRef ID	25271847X
country of citizenship	United States of America
educated at	Purdue University Rice University
ORCID iD	wds:Q68034798-FFB47BF7-2DB7-4437-BEB4-D4E8EE25F890
ORCID iD	https://orcid.org/0000-0003-1125-3727
ORCID iD	0000-0003-1125-3727
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q68034798
is author of	Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysis Keeping G proteins at bay: a complex between G protein-coupled receptor kinase 2 and Gbetagamma G protein-coupled receptor Kinase 2/G alpha q/11 interaction. A novel surface on a regulator of G protein signaling homology domain for binding G alpha subunits. Structural insights into phospholipase C-β function. GRK2 activation by receptors: role of the kinase large lobe and carboxyl-terminal tail. Monomeric rhodopsin is sufficient for normal rhodopsin kinase (GRK1) phosphorylation and arrestin-1 binding The role of G beta gamma and domain interfaces in the activation of G protein-coupled receptor kinase 2. A conserved hydrophobic surface of the LARG pleckstrin homology domain is critical for RhoA activation in cells. Trio's Rho-specific GEF domain is the missing Galpha q effector in C. elegans Feedback inhibition of G protein-coupled receptor kinase 2 (GRK2) activity by extracellular signal-regulated kinases. Unique hydrophobic extension of the RGS2 amphipathic helix domain imparts increased plasma membrane binding and function relative to other RGS R4/B subfamily members. Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS Constitutively active rhodopsin mutants causing night blindness are effectively phosphorylated by GRKs but differ in arrestin-1 binding Molecular basis for P-site inhibition of adenylyl cyclase Identification of a Gialpha binding site on type V adenylyl cyclase The structure, catalytic mechanism and regulation of adenylyl cyclase Identification and structure-function analysis of subfamily selective G protein-coupled receptor kinase inhibitors Preliminary X-ray analysis of Escherichia coli GMP synthetase: determination of anomalous scattering factors for a cysteinyl mercury derivative. C-terminal threonines and serines play distinct roles in the desensitization of rhodopsin, a G protein-coupled receptor The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families Crystal structure of the adenylyl cyclase activator Gsalpha A new approach to producing functional G alpha subunits yields the activated and deactivated structures of G alpha(12/13) proteins Galpha q allosterically activates and relieves autoinhibition of p63RhoGEF. Cluster cytometry for high-capacity bioanalysis. Preliminary structure analysis of the DH/PH domains of leukemia-associated RhoGEF. Characterization of GRK2 RH domain-dependent regulation of GPCR coupling to heterotrimeric G proteins Recognition in the face of diversity: interactions of heterotrimeric G proteins and G protein-coupled receptor (GPCR) kinases with activated GPCRs Structural insights into G protein-coupled receptor kinase function. Crystal Structure of G Protein-coupled Receptor Kinase 5 in Complex with a Rationally Designed Inhibitor Using iterative fragment assembly and progressive sequence truncation to facilitate phasing and crystal structure determination of distantly related proteins Mapping the putative G protein-coupled receptor (GPCR) docking site on GPCR kinase 2: insights from intact cell phosphorylation and recruitment assays Membrane orientation and binding determinants of G protein-coupled receptor kinase 5 as assessed by combined vibrational spectroscopic studies. G Protein-Coupled Receptor Kinase 2 (GRK2) and 5 (GRK5) Exhibit Selective Phosphorylation of the Neurotensin Receptor in Vitro Hitchhiking on the heptahelical highway: structure and function of 7TM receptor complexes. Structural and Biochemical Characterization of the Catalytic Core of the Metastatic Factor P-Rex1 and Its Regulation by PtdIns(3,4,5)P3. Identification and characterization of amlexanox as a G protein-coupled receptor kinase 5 inhibitor

Faceted Search & Find service v1.16.117 as of May 05 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3239 as of May 5 2024, on Linux (x86_64-centos_6-linux-gnu), Single-Server Edition (378 GB total memory, 196 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software