about
WASP suppresses the growth defect of Saccharomyces cerevisiae las17Delta strain in the presence of WIPMolecular difference between WASP and N-WASP critical for chemotaxis of T-cells towards SDF-1α.Interaction between human BAP31 and respiratory syncytial virus small hydrophobic (SH) proteinCharacterization of Wiskott-Aldrich syndrome (WAS) mutants using Saccharomyces cerevisiaeMyogenic differentiation depends on the interplay of Grb2 and N-WASP.Insulin receptor substrate protein 53kDa (IRSp53) is a negative regulator of myogenic differentiation.The mammalian verprolin, WIRE induces filopodia independent of N-WASP through IRSp53.Cloning, sequencing, and expression of a gene encoding a 100-kilodalton mosquitocidal toxin from Bacillus sphaericus SSII-1.X-linked thrombocytopenia causing mutations in WASP (L46P and A47D) impair T cell chemotaxis.Functions of Vrp1p in cytokinesis and actin patches are distinct and neither requires a WH2/V domain.Hypoxia activated EGFR signaling induces epithelial to mesenchymal transition (EMT).Cytotoxicity and ADP-ribosylating activity of the mosquitocidal toxin from Bacillus sphaericus SSII-1: possible roles of the 27- and 70-kilodalton peptidesProteolytic processing of the mosquitocidal toxin from Bacillus sphaericus SSII-1Conditional knockout of N-WASP in mouse fibroblast caused keratinocyte hyper proliferation and enhanced wound closure.Verprolin: a cool set of actin-binding sites and some very HOT prolines.WIP promotes in-vitro invasion ability, anchorage independent growth and EMT progression of A549 lung adenocarcinoma cells by regulating RhoA levels.Myogenesis defect due to Toca-1 knockdown can be suppressed by expression of N-WASP.Gene from tropical Bacillus sphaericus encoding a protease closely related to subtilisins from Antarctic bacilli.N-WASP plays a critical role in fibroblast adhesion and spreading.Conditional knock out of N-WASP in keratinocytes causes skin barrier defects and atopic dermatitis-like inflammation.Expression of N-WASP is regulated by HiF1α through the hypoxia response element in the N-WASP promoter.Vrp1p-Las17p interaction is critical for actin patch polarization but is not essential for growth or fluid phase endocytosis in S. cerevisiae.Erratum to "Conditional N-WASP knockout in mouse brain implicates actin cytoskeleton regulation in hydrocephalus pathology"[Experimental Neurology (2014) 29-40].Verprolin function in endocytosis and actin organization. Roles of the Las17p (yeast WASP)-binding domain and a novel C-terminal actin-binding domain.Las17p-Vrp1p but not Las17p-Arp2/3 interaction is important for actin patch polarization in yeast.Conditional N-WASP knockout in mouse brain implicates actin cytoskeleton regulation in hydrocephalus pathologyOverexpression of GRB2 Enhances Epithelial to Mesenchymal Transition of A549 Cells by Upregulating SNAIL ExpressionOverexpression of CDC42SE1 in A431 Cells Reduced Cell Proliferation by Inhibiting the Akt PathwayActin binding and proline rich motifs of CR16 play redundant role in growth of vrp1Delta cellsAnalysis of conformational changes in WASP using a split YFPWiskott-Aldrich Syndrome causing mutation, Pro373Ser restricts conformational changes essential for WASP activity in T-cellsCatalase-Integrated Hyaluronic Acid as Nanocarriers for Enhanced Photodynamic Therapy in Solid Tumor
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Q24305123-D681BBA2-A40A-4091-B1F5-D538BB4FFBB9Q27308645-A04923EB-7804-4F9A-AFC7-993385F716F0Q28118849-6E2B46BB-A0D9-430E-9268-CABBCE4806B3Q28261035-21C1AC46-BD88-4D4A-98F2-A7AB373AF9A4Q30008805-46CAAFC5-B493-485E-A3A6-892095F16E9AQ30010146-599179C4-D888-4B78-A59C-5D1488E896F5Q30156083-469BFDBD-F2C2-4199-BD80-A2ABFB2CCA46Q33327813-AB25B5B7-4DCB-422C-9AC3-59E585FC3069Q33417562-A8B3A637-741E-4485-BB90-52B9DC0B86ECQ34085322-416A1C6D-5816-4746-B5BD-597ED6884D2BQ34490499-DB7E31D4-F0C8-4C75-A55F-ACE766613DC8Q36098374-5F6D168E-9CB6-4BC5-9CFD-917C5EFF54E8Q36115717-3D1B313C-D37A-4467-B545-6DBB6310F87DQ37464535-7693655E-9FCD-4193-8F05-7EA6B61E4193Q37512017-7AB151EF-4188-4F13-8CB1-CDBBF8A47391Q38726792-AC6F3209-F59B-4CB6-B71F-A48596C003ABQ38991543-4947081F-6B39-4818-9F29-0E7E1B475B3CQ39580950-713522F1-10DF-431D-A439-44E97E70C1A1Q40061628-CB50EBBC-39A6-45B8-AC52-7654B2454680Q41260707-72DE2308-5A80-4AA0-B0F0-4A1B9D830354Q41682503-F4E1120C-DEC2-4858-8C32-11094B3F5EF5Q44584165-7619BA6D-6B71-43FD-ACD5-FC9ED3BCC04BQ48733568-C170EBFC-3515-442D-933F-BCE08AF9D7F5Q50673178-CF19F108-2F6F-4E0D-A295-25917F023B8CQ51777047-14115DAE-0A59-4BC2-BE29-F032B1D6A57DQ57202128-37BB9C13-8F11-4B2F-8A5C-935EBE4595BBQ57752474-2E992C5B-3F23-481E-BFC5-C82DF50828F9Q64243535-6684A59A-9211-4014-9483-8DEA03574A82Q80120185-026A68C2-9D12-4D28-AD6A-18688CB09916Q81158107-C939CCAD-75CF-450B-9A39-341275185E0AQ87123058-F3451B80-ABFF-48EB-9A9A-FB2226A2853AQ92970315-4B24B52E-F4CA-48C3-8E54-905AD6A51AD5
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Thirumaran Thanabalu
@ast
Thirumaran Thanabalu
@en
Thirumaran Thanabalu
@es
Thirumaran Thanabalu
@nl
Thirumaran Thanabalu
@sl
type
label
Thirumaran Thanabalu
@ast
Thirumaran Thanabalu
@en
Thirumaran Thanabalu
@es
Thirumaran Thanabalu
@nl
Thirumaran Thanabalu
@sl
prefLabel
Thirumaran Thanabalu
@ast
Thirumaran Thanabalu
@en
Thirumaran Thanabalu
@es
Thirumaran Thanabalu
@nl
Thirumaran Thanabalu
@sl
P1053
A-2216-2011
P106
P31
P3829
P496
0000-0001-5871-3829