About: Banafshé Larijani

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

researcher ORCID ID = 0000-0003-4735-1169

Attributes	Values
rdf:type	Item
description	forskare (sv) ikertzailea (eu) 연구원 (ko) 研究者 (ja) wetenschapper (nl) дослідниця (uk) эрдэмтэн (mn) वैज्ञानिक (hi) 研究者 (zh) researcher ORCID ID = 0000-0003-4735-1169 (en)
rdfs:label	Banafshé Larijani (en) Banafshé Larijani (es) Banafshé Larijani (nl) Banafshé Larijani (ast)
skos:prefLabel	Banafshé Larijani (en) Banafshé Larijani (es) Banafshé Larijani (nl) Banafshé Larijani (ast)
name	Banafshé Larijani (en) Banafshé Larijani (es) Banafshé Larijani (nl) Banafshé Larijani (ast)
Scopus author ID	wds:Q60845365-916AAA30-35CA-47E1-B19A-5914C6B0657F
Scopus author ID	7004018604
instance of	wds:Q60845365-33D8C0FA-60CA-499D-B89C-B30C9F360B9D
instance of	Homo sapiens
Nationale Thesaurus voor Auteursnamen ID	wds:Q60845365-9470cdaf-763b-4778-9845-71c2447a6f17
occupation	wds:Q60845365-E5CE3431-585D-4AA3-AA9C-8A73B47EFEA3
employer	wds:Q60845365-142E1D85-B021-47C6-BFBB-9E59FCBB8213 wds:Q60845365-35284C19-9C22-4466-8DD4-5861363349D4 wds:Q60845365-99E7C340-8E2A-46EE-9C6E-D2AD2B113D71
NUKAT ID	wds:Q60845365-48503B27-3FE0-4D62-89DB-D1C89F1344EA
sex or gender	wds:Q60845365-F03AF9F1-6BB0-490D-93FD-67C238F4C291
ISNI	wds:Q60845365-F8AD394A-AE16-458F-AD05-B31F5713FC76
VIAF ID	wds:Q60845365-F9B6D8B1-8A2F-4D12-8C19-E25B123EED53
IdRef ID	wds:Q60845365-0D9FADC9-EBFF-4D1D-8FE1-E0EF6A58FB56
WorldCat Identities ID (superseded)	wds:Q60845365-7E0BB2BB-E7F8-43F5-BC0B-0ACC069055A9
National Library of Israel J9U ID	wds:Q60845365-AD816A02-71E7-4F61-9A0E-643BBC389442
Nationale Thesaurus voor Auteursnamen ID	http://data.bibliotheken.nl/id/thes/p31634334X
VIAF ID	http://viaf.org/viaf/1907723
IdRef ID	http://www.idref.fr/109135660/id
Nationale Thesaurus voor Auteursnamen ID	31634334X
occupation	researcher
employer	University of Bath Cancer Research UK Ikerbasque
NUKAT ID	n2006109509
sex or gender	female organism
ISNI	0000000117908881
VIAF ID	1907723
IdRef ID	109135660
WorldCat Identities ID (superseded)	lccn-n2006181479
National Library of Israel J9U ID	987007380829505171
ORCID iD	wds:Q60845365-E5D24ABD-A452-48AA-A503-A8BA43F37901
ORCID iD	https://orcid.org/0000-0003-4735-1169
ORCID iD	0000-0003-4735-1169
Gateway to Research person ID	wds:Q60845365-07A72900-76C8-4D90-8709-568C445BA80C
Gateway to Research person ID	AA58ECFA-6487-4399-BC15-5F3788825C09
ResearcherID	wds:Q60845365-AE89C004-00D8-46AF-A0D4-E3351CBDBC69
ResearcherID	H-3909-2015
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q60845365
is author of	HER2 phosphorylation is maintained by a PKB negative feedback loop in response to anti-HER2 herceptin in breast cancer Regulation of 3-phosphoinositide-dependent protein kinase 1 activity by homodimerization in live cells Spatial regulation of membrane fusion controlled by modification of phosphoinositides Acute manipulation of diacylglycerol reveals roles in nuclear envelope assembly & endoplasmic reticulum morphology Compartmental signal modulation: Endosomal phosphatidylinositol 3-phosphate controls endosome morphology and selective cargo sorting. Phosphatidylinositol metabolism and membrane fusion Nuclear envelope formation: mind the gaps Diacylglycerol induces fusion of nuclear envelope membrane precursor vesicles. Phospholipid identification and quantification of membrane vesicle subfractions by 31P-1H two-dimensional nuclear magnetic resonance Correlative and integrated light and electron microscopy of in-resin GFP fluorescence, used to localise diacylglycerol in mammalian cells. Nuclear actin regulates dynamic subcellular localization and activity of the SRF cofactor MAL. Monitoring conformational changes of proteins in cells by fluorescence lifetime imaging microscopy EGF regulation of PITP dynamics is blocked by inhibitors of phospholipase C and of the Ras-MAP kinase pathway 3-D structure and dynamics of protein kinase B-new mechanism for the allosteric regulation of an AGC kinase Role of a novel PH-kinase domain interface in PKB/Akt regulation: structural mechanism for allosteric inhibition Protein kinases, from B to C. Prognostic Value of an Activation State Marker for Epidermal Growth Factor Receptor in Tissue Microarrays of Head and Neck Cancer Intramolecular and intermolecular interactions of protein kinase B define its activation in vivo Endomembrane PtdIns(3,4,5)P3 activates the PI3K-Akt pathway. PINCH1 regulates Akt1 activation and enhances radioresistance by inhibiting PP1alpha RPEL motifs link the serum response factor cofactor MAL but not myocardin to Rho signaling via actin binding Multiple factors contribute to inefficient prenylation of Rab27a in Rab prenylation diseases GGA function is required for maturation of neuroendocrine secretory granules Acute depletion of plasma membrane phospholipids-dissecting the roles of PtdIns(4)P and PtdIns(4,5)P2 Detecting protein-phospholipid interactions. Epidermal growth factor-induced activation of phospholipase D1b in situ Patient-derived xenografts of triple-negative breast cancer reproduce molecular features of patient tumors and respond to mTOR inhibition HER2 oncogenic function escapes EGFR tyrosine kinase inhibitors via activation of alternative HER receptors in breast cancer cells Accumulated bending energy elicits neutral sphingomyelinase activity in human red blood cells Nuclear envelope assembly is promoted by phosphoinositide-specific phospholipase C with selective recruitment of phosphatidylinositol-enriched membranes PLCgamma is enriched on poly-phosphoinositide-rich vesicles to control nuclear envelope assembly. Effects of phosphoinositides and their derivatives on membrane morphology and function Identification of a novel phosphonocarboxylate inhibitor of Rab geranylgeranyl transferase that specifically prevents Rab prenylation in osteoclasts and macrophages. Dynamics of PLCγ and Src family kinase 1 interactions during nuclear envelope formation revealed by FRET-FLIM. Polyunsaturated phosphatidylinositol and diacylglycerol substantially modify the fluidity and polymorphism of biomembranes: a solid-state deuterium NMR study Acute regulation of PDK1 by a complex interplay of molecular switches The PH domain of phosphoinositide-dependent kinase-1 exhibits a novel, phospho-regulated monomer-dimer equilibrium with important implications for kinase domain activation: single-molecule and ensemble studies Differential activation of the PI 3-kinase effectors AKT/PKB and p70 S6 kinase by compound 48/80 is mediated by PKCalpha A structural role for lipids in organelle shaping

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