About: Jens Peter Andersen

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

About: Jens Peter Andersen Goto Sponge NotDistinct Permalink

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

researcher ORCID ID = 0000-0003-0654-4300

Attributes	Values
rdf:type	Item
description	forskare (sv) 연구원 (ko) 研究者 (ja) araştırmacı (tr) wetenschapper (nl) дослідник (uk) эрдэмтэн (mn) वैज्ञानिक (hi) изилдөөчү (ky) 研究者 (zh) researcher ORCID ID = 0000-0003-0654-4300 (en)
rdfs:label	Jens Peter Andersen (da) Jens Peter Andersen (en) Jens Peter Andersen (ast) Jens Peter Andersen (es) Jens Peter Andersen (nl)
skos:prefLabel	Jens Peter Andersen (da) Jens Peter Andersen (en) Jens Peter Andersen (ast) Jens Peter Andersen (es) Jens Peter Andersen (nl)
name	Jens Peter Andersen (da) Jens Peter Andersen (en) Jens Peter Andersen (ast) Jens Peter Andersen (es) Jens Peter Andersen (nl)
Scopus author ID	wds:Q58879057-EF25FF41-E353-46D8-B9FB-DE50B0DE308A
Scopus author ID	55042486100
given name	wds:Q58879057-ADA7BD1C-E727-4289-9DB1-BB2ACA2BF8E1
given name	Jens
instance of	wds:Q58879057-7AD4DD74-F5DF-4E4F-9DB2-E81EC1DF5B8D
instance of	Homo sapiens
Loop ID	wds:Q58879057-1A73ABCF-CC8D-4BC6-94F9-BDF0595633D8
Loop ID	301866
occupation	wds:Q58879057-D620EC5F-8898-4A55-ACCE-107745A67A9F
employer	wds:Q58879057-0C8E6EFB-460B-43E8-838D-8ABE724ED98F wds:Q58879057-2369F85D-F234-49B2-B17A-90060A3AC128 wds:Q58879057-26EA2EE2-F7D6-494C-AFF3-43ED3B0DF83B wds:Q58879057-3A026956-43B4-4D28-8AE7-4E851DAB885A
sex or gender	wds:Q58879057-7DC91D84-6EC9-4204-86FD-9944DFA1071F
VIAF ID	wds:Q58879057-3AF0B4EA-25F0-4A5F-A3C5-D27A64665B61
GND ID	wds:Q58879057-cbeaa292-cff7-400d-9838-e636b2dacd56
IdRef ID	wds:Q58879057-2FA7F47A-25C7-4D60-9EB3-FA83A23CA6D5
on focus list of Wikimedia project	wds:Q58879057-B0B70B0E-BE2C-4BFE-9002-DD29DDEDF991
educated at	wds:Q58879057-6F0BDA67-028C-4513-A298-55311034C31D
family name	wds:Q58879057-B90C39D3-66AA-4989-B88C-23150F55B577
VIAF ID	http://viaf.org/viaf/6031149108476868780004
GND ID	https://d-nb.info/gnd/1128766264
IdRef ID	http://www.idref.fr/05579999X/id
occupation	researcher
employer	Aarhus University Aarhus Faculty of Health Sciences Aalborg Hospital
sex or gender	male
VIAF ID	6031149108476868780004
GND ID	1128766264
IdRef ID	05579999X
on focus list of Wikimedia project	WikiProject COVID-19
educated at	Aarhus Faculty of Health Sciences
family name	Andersen
ORCID iD	wds:Q58879057-A4F6F86C-7118-4428-929D-17E0EDEF350C wds:Q58879057-BAE20DEA-518D-4BE3-854C-CA324AC7B38C
ORCID iD	https://orcid.org/0000-0003-0654-4300 https://orcid.org/0000-0003-2444-6210
ORCID iD	0000-0003-0654-4300 0000-0003-2444-6210
is owl:sameAs of	Jens Peter Andersen
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q58879057
is author of	A structural overview of the plasma membrane Na+,K+-ATPase and H+-ATPase ion pumps. Conformational states of sarcoplasmic reticulum Ca2+-ATPase as studied by proteolytic cleavage P-type ATPases as drug targets: tools for medicine and science. Functional consequences of mutations in the transmembrane core region for cation translocation and energy transduction in the Na+,K(+)-ATPase and the SR Ca(2+)-ATPase Effect of Hailey-Hailey Disease mutations on the function of a new variant of human secretory pathway Ca2+/Mn2+-ATPase (hSPCA1) Functional comparison between secretory pathway Ca2+/Mn2+-ATPase (SPCA) 1 and sarcoplasmic reticulum Ca2+-ATPase (SERCA) 1 isoforms by steady-state and transient kinetic analyses Coarse-grained simulations of transitions in the E2-to-E1 conformations for Ca ATPase (SERCA) show entropy-enthalpy compensation. Crystal structure of the sodium–potassium pump Dissection of the functional domains of the sarcoplasmic reticulum Ca(2+)-ATPase by site-directed mutagenesis. Amino acids Asn796 and Thr799 of the Ca(2+)-ATPase of sarcoplasmic reticulum bind Ca2+ at different sites. Kinetic characterization of the normal and detergent-perturbed reaction cycles of the sarcoplasmic reticulum calcium pump. Rate-limiting step(s) under different conditions. The role of Mg2+ and Ca2+ in the simultaneous binding of vanadate and ATP at the phosphorylation site of sarcoplasmic reticulum Ca2+-ATPase Functional consequences of alterations to Glu309, Glu771, and Asp800 in the Ca(2+)-ATPase of sarcoplasmic reticulum Localization of E1-E2 conformational transitions of sarcoplasmic reticulum Ca-ATPase by tryptic cleavage and hydrophobic labeling Functional consequences of alterations to amino acids at the M5S5 boundary of the Ca(2+)-ATPase of sarcoplasmic reticulum. Mutation Tyr763-->Gly uncouples ATP hydrolysis from Ca2+ transport Fast kinetic analysis of conformational changes in mutants of the Ca(2+)-ATPase of sarcoplasmic reticulum Importance of stalk segment S5 for intramolecular communication in the sarcoplasmic reticulum Ca2+-ATPase Functional consequences of proline mutations in the cytoplasmic and transmembrane sectors of the Ca2(+)-ATPase of sarcoplasmic reticulum The C terminus of Na+,K+-ATPase controls Na+ affinity on both sides of the membrane through Arg935. Identification and function of a cytoplasmic K+ site of the Na+, K+ -ATPase. Mutational analysis of the conserved TGES loop of sarcoplasmic reticulum Ca2+-ATPase. Crystal structure of D351A and P312A mutant forms of the mammalian sarcoplasmic reticulum Ca(2+) -ATPase reveals key events in phosphorylation and Ca(2+) release Critical role of a transmembrane lysine in aminophospholipid transport by mammalian photoreceptor P4-ATPase ATP8A2 Localization of a K+ -binding site involved in dephosphorylation of the sarcoplasmic reticulum Ca2+ -ATPase. A combined zinc/cadmium sensor and zinc/cadmium export regulator in a heavy metal pump. The sarcoplasmic reticulum Ca2+-ATPase The functional unit of sarcoplasmic reticulum Ca2+-ATPase. Active site titration and fluorescence measurements Mode of interaction of polyoxyethyleneglycol detergents with membrane proteins Monomer-oligomer equilibrium of sarcoplasmic reticulum Ca-ATPase and the role of subunit interaction in the Ca2+ pump mechanism. Roles of transmembrane segment M1 of Na+,K+-ATPase and Ca2-ATPase, the gatekeeper and the pivot. Occlusion of Ca2+ in soluble monomeric sarcoplasmic reticulum Ca2+-ATPase

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, 188 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software