About: Phillip J. Robinson

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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	ikertzailea (eu) researcher (en) 연구원 (ko) ricercatore (it) গবেষক (bn) 研究者 (ja) ഗവേഷകൻ (ml) investigador (es) araştırmacı (tr) chercheur (fr) wetenschapper (nl) дослідник (uk) वैज्ञानिक (hi) изилдөөчү (ky) 研究者 (zh) հետազոտող (hy) hulumtues (sq) researcher (en-ca) researcher (en-gb) researcher (en-us) investigador (ca) investigador (gl) investigador (ast) investigador (pt)
rdfs:label	Phillip J. Robinson (en) Phillip J. Robinson (es) Phillip J. Robinson (nl) Phillip J. Robinson (sl) Phillip J. Robinson (ast)
skos:prefLabel	Phillip J. Robinson (en) Phillip J. Robinson (es) Phillip J. Robinson (nl) Phillip J. Robinson (sl) Phillip J. Robinson (ast)
name	Phillip J. Robinson (en) Phillip J. Robinson (es) Phillip J. Robinson (nl) Phillip J. Robinson (sl) Phillip J. Robinson (ast)
Scopus author ID	wds:Q41161320-ACEF1B70-86CF-47A9-98D7-415B9A0C691A wds:Q41161320-DDD3B9C1-01D9-4F66-BA04-3FF405A090AF
Scopus author ID	55069574500 7403720330
given name	wds:Q41161320-B14D1E1A-B33E-42F1-9733-5D5370459301
given name	Phillip
instance of	wds:Q41161320-C162DE72-D9B0-4608-9C7F-6EF69540B387
instance of	Homo sapiens
skos:altLabel	Phil Robinson (en) Phillip Robinson (en)
occupation	wds:Q41161320-98020653-01DA-4B8C-90E4-6D40C50FB347
employer	wds:Q41161320-19784B55-67C3-4C8B-894C-BBB198B2EE36 wds:Q41161320-1D091540-1960-4763-BF33-4B18D4028654
sex or gender	wds:Q41161320-94EB2A47-6AFD-4D15-AD8A-473CA8147784
educated at	wds:Q41161320-7DB89EB8-4F64-495C-B604-473E0AB7AAAE wds:Q41161320-ECF589E5-5B16-4F30-AFC5-5BE294AB8EC7
family name	wds:Q41161320-5E9F0AC7-4CBB-4E89-A5CF-71727A420527
official website	wds:Q41161320-F67BAE54-6928-4024-853A-DA1872BA7D54
occupation	researcher
employer	University of Sydney Children's Medical Research Institute
sex or gender	male
educated at	University of Newcastle University of Sydney
family name	Robinson
official website	http://www.cmri.org.au/Research/Research-Units/Cell-Signalling
ORCID iD	wds:Q41161320-AF9348FA-1352-4C88-84E8-847BA12C88B0
ORCID iD	https://orcid.org/0000-0002-7878-0313
ORCID iD	0000-0002-7878-0313
ResearcherID	wds:Q41161320-1C138722-0873-494C-8779-13F0863AB16F
Publons author ID	wds:Q41161320-b7ee7424-ec5b-440e-a5a5-47d1760b3991
ResearcherID	G-4008-2011
Publons author ID	2773943
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q41161320
is author of	PICK1 interacts with PACSIN to regulate AMPA receptor internalization and cerebellar long-term depression The in vivo phosphorylation and glycosylation of human insulin-like growth factor-binding protein-5. Intranuclear rod myopathy: molecular pathogenesis and mechanisms of weakness Involvement of novel autophosphorylation sites in ATM activation Clathrin-independent carriers form a high capacity endocytic sorting system at the leading edge of migrating cells Kruppel-associated Box (KRAB)-associated co-repressor (KAP-1) Ser-473 phosphorylation regulates heterochromatin protein 1β (HP1-β) mobilization and DNA repair in heterochromatin Ral: mediator of membrane trafficking Mammalian septins nomenclature Actin- and dynamin-dependent maturation of bulk endocytosis restores neurotransmission following synaptic depletion Dynamin inhibition blocks botulinum neurotoxin type A endocytosis in neurons and delays botulism Myristyl Trimethyl Ammonium Bromide and Octadecyl Trimethyl Ammonium Bromide Are Surface-Active Small Molecule Dynamin Inhibitors that Block Endocytosis Mediated by Dynamin I or Dynamin II Protein phosphorylation is required for endocytosis in nerve terminals: potential role for the dephosphins dynamin I and synaptojanin, but not AP180 or amphiphysin Dynamin GTPase regulated by protein kinase C phosphorylation in nerve terminals Enhanced Protein Recovery and Reproducibility from Pull-Down Assays and Immunoprecipitations Using Spin Columns Autophosphorylation and ATM activation: additional sites add to the complexity Protein composition of catalytically active human telomerase from immortal cells Cdk1/Erk2- and Plk1-dependent phosphorylation of a centrosome protein, Cep55, is required for its recruitment to midbody and cytokinesis. Increased levels of SNAP-25 and synaptophysin in the dorsolateral prefrontal cortex in bipolar I disorder. Dephosphin, a 96,000 Da substrate of protein kinase C in synaptosomal cytosol, is phosphorylated in intact synaptosomes Synapsin I-associated phosphatidylinositol 3-kinase mediates synaptic vesicle delivery to the readily releasable pool Role of the clathrin terminal domain in regulating coated pit dynamics revealed by small molecule inhibition Dephosphin/dynamin is a neuronal phosphoprotein concentrated in nerve terminals: Evidence from rat cerebellum Label-free quantitation of phosphopeptide changes during rat sperm capacitation. The pathogenesis of ACTA1-related congenital fiber type disproportion Superfluous role of mammalian septins 3 and 5 in neuronal development and synaptic transmission Phosphorylation of syndapin I F-BAR domain at two helix-capping motifs regulates membrane tubulation

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