About: Maja Köhn

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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
description	forskare (sv) researcher (en) 연구원 (ko) গবেষক (bn) 研究者 (ja) araştırmacı (tr) wetenschapper (nl) дослідниця (uk) वैज्ञानिक (hi) изилдөөчү (ky) 研究者 (zh) հետազոտող (hy) hulumtuese (sq) ricercatrice (it)
rdfs:label	Maja Köhn (en) Maja Köhn (nl) Maja Köhn (ast) Maja Köhn (es) Maja Köhn (fr) Maja Köhn (sl)
skos:prefLabel	Maja Köhn (en) Maja Köhn (nl) Maja Köhn (ast) Maja Köhn (es) Maja Köhn (fr) Maja Köhn (sl)
name	Maja Köhn (en) Maja Köhn (nl) Maja Köhn (ast) Maja Köhn (es) Maja Köhn (fr) Maja Köhn (sl)
given name	wds:Q42366817-1F77AF8D-AD51-4181-B5DE-BB3EEF802C5E
given name	Maja
instance of	wds:Q42366817-A32F1566-B416-43F1-AF53-B24F4D6BA97A
instance of	Homo sapiens
skos:altLabel	Maja Koehn (en) Maja Kohn (en)
occupation	wds:Q42366817-C327A9CA-8475-4ADE-89BA-5F9E6858F051
employer	wds:Q42366817-3BDCC5F5-BB5F-4229-B618-2FB2F288E18C wds:Q42366817-919E5076-981A-4034-921B-39B98650F9CB wds:Q42366817-B52CE64F-EEB5-47BE-BD6E-9A2B35FCD288
sex or gender	wds:Q42366817-99219C0D-0792-4D9B-8336-E67959DF1FD2
VIAF ID	wds:Q42366817-B9F94C38-5EAE-4040-BA81-72AD811FD06D
GND ID	wds:Q42366817-a149d53c-39cd-48cd-8ba4-3bb32519777c
educated at	wds:Q42366817-6B6B24FC-BD02-44DB-A063-342178CADDA4
WorldCat Identities ID (superseded)	wds:Q42366817-F7BEE5E2-F158-4104-AAB5-6C3452B51789
VIAF ID	http://viaf.org/viaf/1116173
GND ID	https://d-nb.info/gnd/130328367
occupation	researcher
employer	Harvard University University of Freiburg European Molecular Biology Laboratory
sex or gender	female organism
VIAF ID	1116173
GND ID	130328367
educated at	Max Planck Institute for Molecular Physiology
WorldCat Identities ID (superseded)	viaf-1116173
ORCID iD	wds:Q42366817-6FB46BCD-F5D7-49A7-B189-65B396B6C50C
ORCID iD	https://orcid.org/0000-0001-8142-3504
ORCID iD	0000-0001-8142-3504
ResearcherID	wds:Q42366817-1BA34BFC-4D24-429B-A3D0-3C0DDF75025B
Publons author ID	wds:Q42366817-4b4baabd-9db3-4470-b1c3-8d258510f65b
ResearcherID	G-5131-2012
Publons author ID	2715563
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q42366817
is author of	The metastasis-promoting phosphatase PRL-3 shows activity toward phosphoinositides Rapid erasure of hippocampal memory following inhibition of dentate gyrus granule cells The Staudinger ligation-a gift to chemical biology. Staudinger ligation: a new immobilization strategy for the preparation of small-molecule arrays Biochemical evaluation of virtual screening methods reveals a cell-active inhibitor of the cancer-promoting phosphatases of regenerating liver. Functional evaluation of carbohydrate-centred glycoclusters by enzyme-linked lectin assay: ligands for concanavalin A. Molecular mechanisms of the PRL phosphatases Targeting the untargetable: recent advances in the selective chemical modulation of protein phosphatase-1 activity. Challenges and opportunities in the development of protein phosphatase-directed therapeutics. Site-Selective Protein Immobilization by Staudinger Ligation Immobilization strategies for small molecule, peptide and protein microarrays. Diels-Alder ligation and surface immobilization of proteins. Development of a Peptide that Selectively Activates Protein Phosphatase-1 in Living Cells The human DEPhOsphorylation database DEPOD: a 2015 update. Elucidating human phosphatase-substrate networks Photochemical surface patterning by the thiol-ene reaction A generic building block for C- and N-terminal protein-labeling and protein-immobilization. Dual-specificity phosphatases as molecular targets for inhibition in human disease Phosphatases: Their Roles in Cancer and Their Chemical Modulators A Microarray Strategy for Mapping the Substrate Specificity of Protein Tyrosine Phosphatase Activation of protein phosphatase 1 by a selective phosphatase disrupting peptide reduces sarcoplasmic reticulum Ca leak in human heart failure Synthesis of Highly Selective Submicromolar Microcystin-Based Inhibitors of Protein Phosphatase (PP)2A over PP1. Mouse Rif1 is a regulatory subunit of protein phosphatase 1 (PP1). PRL-3 disrupts epithelial architecture by altering the post-mitotic midbody position Mutational Analysis of a Conserved Glutamate Reveals Unique Mechanistic and Structural Features of the Phosphatase PRL-3 VHR/DUSP3 phosphatase: structure, function and regulation Molecular mechanism of SHP2 activation by PD-1 stimulation The <i>Leishmania donovani LDBPK_220120.1</i> Gene Encodes for an Atypical Dual Specificity Lipid-Like Phosphatase Expressed in Promastigotes and Amastigotes; Substrate Specificity, Intracellular Localizations, and Putative Role(s) Preparation of biomolecule microstructures and microarrays by thiol-ene photoimmobilization Development of accessible peptidic tool compounds to study the phosphatase PTP1B in intact cells Unnatural amino acid mutagenesis reveals dimerization as a negative regulatory mechanism of VHR's phosphatase activity. Regulatory mechanisms of phosphatase of regenerating liver (PRL)-3 Microcystins: Synthesis and structure-activity relationship studies toward PP1 and PP2A.

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