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Identification of an actin binding region and a protein kinase C phosphorylation site on human fascinA mutation of beta -actin that alters depolymerization dynamics is associated with autosomal dominant developmental malformations, deafness, and dystoniaTwo distinct myosin II populations coordinate ovulatory contraction of the myoepithelial sheath in the Caenorhabditis elegans somatic gonadMuscle-specific splicing factors ASD-2 and SUP-12 cooperatively switch alternative pre-mRNA processing patterns of the ADF/cofilin gene in Caenorhabditis elegansThe RNA-binding protein SUP-12 controls muscle-specific splicing of the ADF/cofilin pre-mRNA in C. elegansTroponin I controls ovulatory contraction of non-striated actomyosin networks in the C. elegans somatic gonad.The Caenorhabditis elegans unc-78 gene encodes a homologue of actin-interacting protein 1 required for organized assembly of muscle actin filaments.Two actin-interacting protein 1 isoforms function redundantly in the somatic gonad and are essential for reproduction in Caenorhabditis elegansThe minus-end actin capping protein, UNC-94/tropomodulin, regulates development of the Caenorhabditis elegans intestineThe C-terminal tail of UNC-60B (actin depolymerizing factor/cofilin) is critical for maintaining its stable association with F-actin and is implicated in the second actin-binding site.A plague of actin disassembly.Distinct roles of four gelsolin-like domains of Caenorhabditis elegans gelsolin-like protein-1 in actin filament severing, barbed end capping, and phosphoinositide binding.Regulation of structure and function of sarcomeric actin filaments in striated muscle of the nematode Caenorhabditis elegans.Tropomyosin and troponin are required for ovarian contraction in the Caenorhabditis elegans reproductive system.Enhancement of actin-depolymerizing factor/cofilin-dependent actin disassembly by actin-interacting protein 1 is required for organized actin filament assembly in the Caenorhabditis elegans body wall muscleCaenorhabditis elegans kettin, a large immunoglobulin-like repeat protein, binds to filamentous actin and provides mechanical stability to the contractile apparatuses in body wall muscle.Solution structures and dynamics of ADF/cofilins UNC-60A and UNC-60B from Caenorhabditis elegansThe two actin-interacting protein 1 genes have overlapping and essential function for embryonic development in Caenorhabditis elegansDual roles of tropomyosin as an F-actin stabilizer and a regulator of muscle contraction in Caenorhabditis elegans body wall muscleCalcium-sensitive activity and conformation of Caenorhabditis elegans gelsolin-like protein 1 are altered by mutations in the first gelsolin-like domain.Regulation of actin filament dynamics by actin depolymerizing factor/cofilin and actin-interacting protein 1: new blades for twisted filaments.Biochemical and cell biological analysis of actin in the nematode Caenorhabditis elegansNMR assignments of actin depolymerizing factor (ADF) like UNC-60A and cofilin like UNC-60B proteins of Caenorhabditis elegansBasic Methods to Visualize Actin Filaments In Vitro Using Fluorescence Microscopy for Observation of Filament Severing and Bundling.The two Caenorhabditis elegans actin-depolymerizing factor/cofilin proteins differently enhance actin filament severing and depolymerizationStructural components of the nonstriated contractile apparatuses in the Caenorhabditis elegans gonadal myoepithelial sheath and their essential roles for ovulation.UNC-60B, an ADF/cofilin family protein, is required for proper assembly of actin into myofibrils in Caenorhabditis elegans body wall muscle.CAS-1, a C. elegans cyclase-associated protein, is required for sarcomeric actin assembly in striated muscle.Muscle contraction phenotypic analysis enabled by optogenetics reveals functional relationships of sarcomere components in Caenorhabditis elegansActin-interacting Protein 1 Promotes Disassembly of Actin-depolymerizing Factor/Cofilin-bound Actin Filaments in a pH-dependent Manner.Actin depolymerization under force is governed by lysine 113:glutamic acid 195-mediated catch-slip bonds.Mechanism of depolymerization and severing of actin filaments and its significance in cytoskeletal dynamics.Regulatory role of the second gelsolin-like domain of Caenorhabditis elegans gelsolin-like protein 1 (GSNL-1) in its calcium-dependent conformation and actin-regulatory activities.Caenorhabditis elegans gelsolin-like protein 1 is a novel actin filament-severing protein with four gelsolin-like repeatsActivation of ADF/cofilin by phosphorylation-regulated Slingshot phosphatase is required for the meiotic spindle assembly in Xenopus laevis oocytesEssential role of ADF/cofilin for assembly of contractile actin networks in the C. elegans somatic gonadCaenorhabditis elegans expresses three functional profilins in a tissue-specific manner.Sarcomeric actin organization is synergistically promoted by tropomodulin, ADF/cofilin, AIP1 and profilin in C. elegansThe role of cyclase-associated protein in regulating actin filament dynamics - more than a monomer-sequestration factor.Actin-ADF/cofilin rod formation in Caenorhabditis elegans muscle requires a putative F-actin binding site of ADF/cofilin at the C-terminus.
P50
Q24314478-15FF4FB3-795B-42E3-BE6E-E9AEDF2ADB3BQ24546532-D20522FC-FDAA-4467-8E3B-9D462CA33256Q27305022-32C05ED1-08F1-42C3-823F-EC7DBD3CDF4AQ28484356-0DDB8794-5C11-4582-90E3-F262EE2DFC27Q28763775-081B0529-EEDC-4D9B-9FAC-48279F1C39E7Q30494196-EA17C88F-6EE1-445B-9B0B-A45636B4E6CEQ30494543-B2D60803-496A-4693-B7E8-100E03C05490Q30582807-065AA3A1-85EE-47B2-9AB0-F8AEBEDCF222Q30587126-6054334B-1C96-4DA7-9C0D-0B3B5FD62963Q31492863-AE350DEA-B029-4E43-8F0C-767CECEE8C9FQ33666166-0020DCFA-509D-4D0D-A76F-CD780B4DA6BEQ33967799-75AE708A-B6DC-46A3-8ABE-54A112075C4FQ34180309-1EB0AE8D-776F-48DC-9819-57E55F4B4AF8Q34359408-0B9CFAFF-B529-47FF-8EBF-2AD396144B2DQ34559649-A168040D-0D0D-4258-93F5-B185F1514F5BQ34661750-7A5FE5DF-6BA2-4574-BF47-D606D2484EADQ35077481-3F0ADD79-24A7-4B69-ACA6-1B79B3FD2011Q35083442-0AE226CA-7190-45A0-BF76-1F783E8365E2Q35230851-F3475D60-1CBA-4E42-B934-984EAE2C76F8Q35310424-6D297336-FE21-4BCC-8822-6C43C0FD70BCQ35586078-5E8FF2DB-53C3-4A4E-A532-138E31B26BF4Q35673187-FAEED44C-6DED-4CAA-BBBE-916EBB7C900BQ35736228-392DBC8B-8231-472C-BDC7-D841F00EB6BFQ35820472-D4B0A875-FE79-426A-A464-31759173893FQ35875042-38CD038E-7BBA-4C52-900A-41775901C62BQ36013308-757BD471-4223-4E1B-9FB4-24F187CD9115Q36342163-B83EF66B-3479-4B49-9ACF-20C88113C7B3Q36350840-2E020B7F-E11F-4BE5-A765-538B2D3374FDQ36517109-BB9F1CBD-E27B-4590-AFA7-CC78A0E38DFEQ36650336-4C5D4053-35B6-48A6-997C-E71674F78EDBQ36729688-7CE62AF4-7E85-4CB8-911A-C8D3A7B7FD14Q36752288-EED8063B-C6B9-4D59-95A9-34FCB489A872Q36849236-B2D2A145-2E9E-481F-96E7-F0EEE5BB0EA0Q36871671-842B41D0-1BF6-4CED-8389-024914FCFC82Q36926636-C63976B8-5BEB-4892-9B06-79617F00C976Q36946937-8574F5FF-6F5D-44B4-9ABA-94DC36D8A77BQ36954788-2400D648-2EBE-4C3D-8B24-B84E906AF3A7Q37041560-600A4DE0-F8C1-4A76-939B-147F82532ADBQ37061517-E2A7952B-FBCB-4BEA-8E01-93979E31C6D5Q37322303-888CD055-DD1B-42EC-9517-FDF48375C73F
P50
description
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Shoichiro Ono
@ast
Shoichiro Ono
@en
Shoichiro Ono
@es
Shoichiro Ono
@nl
Shoichiro Ono
@sl
type
label
Shoichiro Ono
@ast
Shoichiro Ono
@en
Shoichiro Ono
@es
Shoichiro Ono
@nl
Shoichiro Ono
@sl
prefLabel
Shoichiro Ono
@ast
Shoichiro Ono
@en
Shoichiro Ono
@es
Shoichiro Ono
@nl
Shoichiro Ono
@sl
P1053
A-6475-2015
P106
P1153
35518924000
P31
P3829
P496
0000-0002-4763-0398