About: Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity

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About: Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity Goto Sponge NotDistinct Permalink

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scientific article published on 31 August 2006

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в серпні 2006 (uk) scientific article published on 31 August 2006 (en) artículu científicu espublizáu n'agostu de 2006 (ast)
publication date	wds:Q80198530-E5FB2979-6203-4621-9C50-E00C44C0CA20
publication date	2006-08-31 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q80198530-8F3A7D03-1943-4D75-9BC4-5F22A4138445
language of work or name	English
cites work	wds:Q80198530-B26B5A13-7228-43B9-95B1-469F63C52825
cites work	Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
author name string	wds:Q80198530-16422E05-83E0-4405-B028-02E2FEE9838B wds:Q80198530-1973FE15-BF6E-49C2-ACB8-BA245D2B232A wds:Q80198530-1A75CFA6-DDA1-4413-B300-266E77379C6E wds:Q80198530-B9488CD7-85C6-4AD1-920C-48C20C496E47
author name string	Thomas A Steitz Jon S Morrow Carol D Cianci Zhushan Zhang
rdfs:label	Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity (en) Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity (nl)
skos:prefLabel	Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity (en) Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity (nl)
name	Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity (en) Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity (nl)
author	wds:Q80198530-EE2EFD54-71E8-41B6-8CED-B7B971A4FA69
author	Miljan Simonovic
title	wds:Q80198530-A044CC72-BC63-4B3A-B053-6DA9C9CE4FE2
title	Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity (en)
page(s)	wds:Q80198530-19A9C187-A27E-473B-9E60-980673D99C81
page(s)	34333-34340
instance of	wds:Q80198530-479A286E-7BD5-47BB-A63E-695952D5719A
instance of	scholarly article
PubMed ID	wds:Q80198530-53A9E1B0-8853-4A20-8EBC-1F7F2F305775
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/16945920
PubMed ID	16945920
published in	wds:Q80198530-8FAEB085-C24F-448A-898C-4D5DCAA95B9C
published in	Journal of Biological Chemistry
issue	wds:Q80198530-B72672E0-E032-4C3B-8CE7-D31D621F8F0A
volume	wds:Q80198530-1769EB77-F1F8-4360-9251-C941FE19046E
issue	45
volume	281
DOI	wds:Q80198530-9E3D8188-7F14-421E-AE28-7612774AB73E
DOI	http://dx.doi.org/10.1074/JBC.M604613200
DOI	10.1074/JBC.M604613200
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q80198530
is cites work of	The spectrin-ankyrin-4.1-adducin membrane skeleton: adapting eukaryotic cells to the demands of animal life Head of myosin IX binds calmodulin and moves processively toward the plus-end of actin filaments Membrane domains based on ankyrin and spectrin associated with cell-cell interactions Caspases rather than calpains mediate remodelling of the fodrin skeleton during human placental trophoblast fusion The structure of the ankyrin-binding site of -spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties Effects of the plasmid-encoded toxin of enteroaggregative Escherichia coli on focal adhesion complexes Regulation of interdomain interactions by calmodulin in inducible nitric-oxide synthase Calpain-mediated breakdown of cytoskeletal proteins contributes to cholecystokinin-induced damage of rat pancreatic acini Calmodulin Wraps around Its Binding Domain in the Plasma Membrane Ca2+ Pump Anchored by a Novel 18-1 Motif Calmodulin and S100A1 protein interact with N terminus of TRPM3 channel Protein 4.2 binds to the carboxyl-terminal EF-hands of erythroid alpha-spectrin in a calcium- and calmodulin-dependent manner Sequential degradation of alphaII and betaII spectrin by calpain in glutamate or maitotoxin-stimulated cells Proximal giant neurofilamentous axonopathy in mice genetically engineered to resist calpain and caspase cleavage of α-II spectrin Nonenzymatic domains of Kalirin7 contribute to spine morphogenesis through interactions with phosphoinositides and Abl Structure-based domain assignment in Leishmania infantum EndoG: characterization of a pH-dependent regulatory switch and a C-terminal extension that largely dictates DNA substrate preferences. The Physiological Molecular Shape of Spectrin: A Compact Supercoil Resembling a Chinese Finger Trap Knockdown of mu-calpain in Fanconi anemia, FA-A, cells by siRNA restores alphaII spectrin levels and corrects chromosomal instability and defective DNA interstrand cross-link repair Spectrin and its interacting partners in nuclear structure and function. Lipid raft-dependent endocytosis of close homolog of adhesion molecule L1 (CHL1) promotes neuritogenesis Fodrin in centrosomes: implication of a role of fodrin in the transport of gamma-tubulin complex in brain A 10-minute prototype assay for tissue degradation monitoring in clinical specimens Quantitative studies of caspase-3 catalyzed αII-spectrin breakdown The functional importance of lamins, actin, myosin, spectrin and the LINC complex in DNA repair
is cites work of	wds:Q35990275-20F408E1-7C7D-4C21-8B6F-2C5F4F0D1136 wds:Q41626369-847AE8A6-56A9-47FD-A2CD-4088A411D1EA wds:Q52349345-2DC4240D-C1ED-4513-A2CB-080E11D04735 wds:Q28262887-3C7537C7-98A4-4BCA-B476-6502F0A78106 wds:Q33674822-959D38D4-8F24-425B-9C72-3679F9012B71 wds:Q36492830-E04FED45-737A-46CA-A502-E206EF139470 wds:Q37776425-D53AA4BF-95C2-4112-8C3D-70E8AC9D887D wds:Q34663429-FBBCDB4E-B1A9-4730-80F8-28E06EA43A04 wds:Q35009590-121E336D-1E0D-4FBA-8E03-AB2BF9BB6B8F wds:Q33974355-93C41C09-8593-4DAC-88B1-434626022FA7 wds:Q27653516-D32DAD68-C79B-4EF1-965D-9BCDEE50E41B wds:Q43297643-0D8A9AA9-74A3-46D4-BBEA-16071A622322 wds:Q37206086-8F6A48C7-ECD2-4A4D-81EA-6FFDDAAE860B wds:Q37431868-A5B734BD-256C-4C62-BBD7-D852D1C09236 wds:Q33717604-5F6A0F09-1A2E-41E5-9A6F-9D9633FAC314 wds:Q39792490-A5BE304A-16BA-4BF9-91ED-BC64EE0AC789 wds:Q28548168-F126BACA-9F81-4C67-949B-03686BA7146E wds:Q30495863-66F517BB-C3E4-45CB-8233-4A6D8E763A29 wds:Q37732166-4E00CBA6-69C4-4454-8CDB-6466AE6B95ED wds:Q40880104-D163368D-9F18-4873-B2A4-E4A090E77133 wds:Q27658550-2C6240D3-E6FC-40B7-B4BE-089C1B610B29 wds:Q37748235-CA6FE04E-3DC5-4EF5-BED4-9838DD8518B5 wds:Q90462509-30ECFC22-9A81-43BA-8830-875F07FE7313

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