About: Synapsin I bundles F-actin in a phosphorylation-dependent manner

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scientific article published in Nature

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rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) article publié dans la revue scientifique Nature (fr) scientific article published in Nature (en) im April 1987 veröffentlichter wissenschaftlicher Artikel (de) наукова стаття, опублікована в Nature у квітні 1987 (uk)
publication date	wds:Q59077332-4706C925-A436-4117-A0FE-C7CED00E5636
publication date	1987-04-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q59077332-17C790E2-53F7-4AFA-92C4-DFBE0E144151
language of work or name	English
exact match	wds:Q59077332-CC1858F9-5E88-40F8-8FF2-213025B07BB0
exact match	https://scigraph.springernature.com/pub.10.1038/326704a0
cites work	wds:Q59077332-1D6971B5-23C1-4308-B484-0A1D3BE97B92 wds:Q59077332-1E12DDB4-10D8-4555-A970-75AA9AF46BE7 wds:Q59077332-294F485D-C643-4979-B450-18FC87A0B0F5 wds:Q59077332-37E5BAD6-CB6A-412C-BB9E-130DC8DE279D wds:Q59077332-394A545D-C797-45B5-8D08-1634E26A7D4C wds:Q59077332-39A485CE-FB36-4DE7-B1D8-D3BAA4A08D7B wds:Q59077332-3D3356AD-6F58-445D-838A-CF3004462B6A wds:Q59077332-3F732502-6AE9-4794-B645-06A62306DCCD wds:Q59077332-482E1DA7-2472-4C1A-878E-9FCB87333E56 wds:Q59077332-5CA9F86F-60D1-488A-AC2C-4038AEE64AE5 wds:Q59077332-61B9DF11-9633-4C3D-897E-C5B8A126A119 wds:Q59077332-6F9FD540-A192-4CCF-BE6A-469E9675EE12 wds:Q59077332-72AF7282-3FC4-4C09-8794-415295DE3198 wds:Q59077332-7528DFB0-B2BA-40DB-B99D-96D6D3C60716 wds:Q59077332-7D482BB5-574C-4CA6-AE31-6B77D6D7AA55 wds:Q59077332-7ED1EDBD-792C-48B3-95E9-DB1AE957E9BA wds:Q59077332-A6BCF10A-0629-4CB3-8B32-71D7C747C535 wds:Q59077332-BD4337C9-B7E6-4F01-AA89-0491EB6AAC27 wds:Q59077332-DCB5F7C1-B258-440A-9F24-4F334C52EBCA wds:Q59077332-E9312B48-79E6-441C-B7D1-CAD5565E062B wds:Q59077332-EFAF85BF-3019-4416-85E0-B565BD3F7420 wds:Q59077332-F93517FF-386B-436A-A84C-22B0D40317AA wds:Q59077332-FEA990A4-A949-4257-901F-1E4B3AC5FA31
cites work	Synapsin I (protein I), a nerve terminal-specific phosphoprotein. III. Its association with synaptic vesicles studied in a highly purified synaptic vesicle preparation Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association Spectrin plus band 4.1 cross-link actin. Regulation by micromolar calcium In vitro formation of a complex between cytoskeletal proteins of the human erythrocyte Partial purification and characterization of an actin-bundling protein, band 4.9, from human erythrocytes Synapsin I (Protein I), a nerve terminal-specific phosphoprotein. II. Its specific association with synaptic vesicles demonstrated by immunocytochemistry in agarose-embedded synaptosomes A quantitative dot-immunobinding assay for proteins using nitrocellulose membrane filters Pyrene actin: documentation of the validity of a sensitive assay for actin polymerization Synapsin I is a spectrin-binding protein immunologically related to erythrocyte protein 4.1. Synapsin I is a microtubule-bundling protein. Two calcium/calmodulin-dependent protein kinases, which are highly concentrated in brain, phosphorylate protein I at distinct sites Intraterminal injection of synapsin I or calcium/calmodulin-dependent protein kinase II alters neurotransmitter release at the squid giant synapse Multiple phosphorylation sites in protein I and their differential regulation by cyclic AMP and calcium Serotonin stimulates phosphorylation of protein I in the facial motor nucleus of rat brain Polymorphism of actin paracrystals induced by polylysine Anti-actin stains synapses. Phosphorylation reduces the affinity of protein 4.1 for spectrin Microinjection of catalytic subunit of cyclic AMP-dependent protein kinase enhances calcium action potentials of bag cell neurons in cell culture Nerve growth factor potentiates actomyosin adenosinetriphosphatase Synapsin I: a synaptic vesicle-associated neuronal phosphoprotein Neurofilament Accumulation Induced in Synapses by Leupeptin A re-examination of the interaction of vinculin with actin Spectrin and protein 4.1 as an actin filament capping complex
author name string	wds:Q59077332-EC2AEA4C-0F1D-4AD9-AECD-E394DF20F186
author name string	Bähler M
rdfs:label	Synapsin I bundles F-actin in a phosphorylation-dependent manner (en) Synapsin I bundles F-actin in a phosphorylation-dependent manner (nl)
skos:prefLabel	Synapsin I bundles F-actin in a phosphorylation-dependent manner (en) Synapsin I bundles F-actin in a phosphorylation-dependent manner (nl)
name	Synapsin I bundles F-actin in a phosphorylation-dependent manner (en) Synapsin I bundles F-actin in a phosphorylation-dependent manner (nl)
author	wds:Q59077332-9E03FABA-F944-443A-8D9B-E2552D64D5D5 wds:Q59077332-C64C98E8-E126-4C0F-A473-7ECB9D9B1263
author	Paul Greengard
title	wds:Q59077332-19F0B2B4-963C-4DFB-AE5F-86056B09948A
title	Synapsin I bundles F-actin in a phosphorylation-dependent manner (en)
page(s)	wds:Q59077332-4D2FF2AA-AE3F-44BE-8B6D-6A32F5E282B6
page(s)	704-707
instance of	wds:Q59077332-01987A2A-5626-4554-BB96-F094853BA369
instance of	scholarly article
main subject	wds:Q59077332-7E736F48-8283-4F87-92E4-DCD5781A8982
main subject	phosphorylation
PubMed ID	wds:Q59077332-E04C1543-A1D8-4BDD-87B0-45B7F74A7EB1
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3104800
PubMed ID	3104800
published in	wds:Q59077332-F152284B-F338-4B23-ABCA-0FC40A0854D6
published in	Nature
issue	wds:Q59077332-802026BF-CF33-41F0-A3E5-D483403FF21F
volume	wds:Q59077332-B5A9F708-FBF4-4677-A440-FC21ED4EECBA
issue	6114
volume	326
DOI	wds:Q59077332-02D8918B-7315-4B6A-AE15-2F14D510CE83
DOI	http://dx.doi.org/10.1038/326704A0
DOI	10.1038/326704A0
Dimensions Publication ID	wds:Q59077332-96BD2B02-A821-4AAE-9018-F9D4543A11A7
Dimensions Publication ID	1004402623
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q59077332
is cites work of	The synaptic vesicle cycle: a cascade of protein-protein interactions Proteins of synaptic vesicles involved in exocytosis and membrane recycling Modulation of presynaptic plasticity and learning by the H-ras/extracellular signal-regulated kinase/synapsin I signaling pathway Invertebrate synapsins: a single gene codes for several isoforms in Drosophila. Exogenous synapsin I promotes functional maturation of developing neuromuscular synapses Regulation of synaptic transmission by presynaptic CaMKII and BK channels Induction of neuron-specific tropomyosin mRNAs by nerve growth factor is dependent on morphological differentiation

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