About: Matthew John Tyska

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An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

cell biologist

Attributes	Values
rdf:type	Item
description	Forscher (de) 연구원 (ko) investigador (es) chercheur (fr) дослідник (uk) изилдөөчү (ky) 研究者 (zh) 研究員 (ja) onderzoeker (nl) cell biologist (en)
rdfs:label	Matthew John Tyska (en) Matthew John Tyska (it) Matthew John Tyska (nl)
skos:prefLabel	Matthew John Tyska (en) Matthew John Tyska (it) Matthew John Tyska (nl)
name	Matthew John Tyska (en) Matthew John Tyska (it) Matthew John Tyska (nl)
affiliation	wds:Q90406485-71C2A969-4781-4098-9CFC-64547E6C4C03
affiliation	Vanderbilt Department of Cell and Developmental Biology
given name	wds:Q90406485-0159B273-9348-4E20-9523-DE2F37755D9A
given name	Matthew
instance of	wds:Q90406485-F04AAF40-E9D0-4DF2-A9D7-65AB8CEAA30A
instance of	Homo sapiens
skos:altLabel	Matthew J Tyska (en) Matthew J Tyska (nl) Matthew Tyska (en)
occupation	wds:Q90406485-31DC4A53-F4B3-4C56-BC11-6BE05A52C3D9
employer	wds:Q90406485-8E7B8550-AABF-49FD-8137-3385AF740269
sex or gender	wds:Q90406485-250D972A-5C8E-4D95-A7F9-B74752B1A814
occupation	researcher
employer	Vanderbilt University
sex or gender	male
ORCID iD	wds:Q90406485-C21D5AD9-854A-405F-8DCE-2E1C6F18CF87
Dimensions author ID	wds:Q90406485-BF606176-C0B8-489F-B2CA-D35F727D64A3
ORCID iD	https://orcid.org/0000-0003-2238-6189
ORCID iD	0000-0003-2238-6189
Dimensions author ID	01113240543.99
is owl:sameAs of	Matthew John Tyska
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q90406485
is author of	Focal adhesions control cleavage furrow shape and spindle tilt during mitosis Myosin motor function: the ins and outs of actin-based membrane protrusions. Myosin-V motility: these levers were made for walking Amphiregulin exosomes increase cancer cell invasion. A role for myosin-1A in the localization of a brush border disaccharidase Expression and localization of myosin-1d in the developing nervous system Control of cell membrane tension by myosin-I. Intestinal brush border assembly driven by protocadherin-based intermicrovillar adhesion ANKS4B Is Essential for Intermicrovillar Adhesion Complex Formation A structural model for binding of the serine-rich repeat adhesin GspB to host carbohydrate receptors Myosin-1a is critical for normal brush border structure and composition Differential localization and dynamics of class I myosins in the enterocyte microvillus The myosin power stroke Leveraging the membrane - cytoskeleton interface with myosin-1. Myosin-IXb is a single-headed and processive motor Constitutively active ezrin increases membrane tension, slows migration, and impedes endothelial transmigration of lymphocytes in vivo in mice Detection of rare antigen-presenting cells through T cell-intrinsic meandering motility, mediated by Myo1g. Extracellular vesicles: communication, coercion, and conditioning The enterocyte microvillus is a vesicle-generating organelle Myosin-1a powers the sliding of apical membrane along microvillar actin bundles. Myosin-1A targets to microvilli using multiple membrane binding motifs in the tail homology 1 (TH1) domain Human deafness mutation E385D disrupts the mechanochemical coupling and subcellular targeting of myosin-1a Myosin-1a: A motor for microvillar membrane movement and mechanics Exosome secretion is enhanced by invadopodia and drives invasive behavior Cortactin promotes exosome secretion by controlling branched actin dynamics Proteomic analysis of the enterocyte brush border Myosin Vb uncoupling from RAB8A and RAB11A elicits microvillus inclusion disease Differential gene expression in normal esophagus and Barrett's esophagus Enterocyte microvillus-derived vesicles detoxify bacterial products and regulate epithelial-microbial interactions. Myosin at work: motor adaptations for a variety of cellular functions Shaping the intestinal brush border Membrane-bound myo1c powers asymmetric motility of actin filaments Optimized multiplex immunofluorescence single-cell analysis reveals tuft cell heterogeneity Ready…aim…fire into the lumen: a new role for enterocyte microvilli in gut host defense Disruption of Rab8a and Rab11a causes formation of basolateral microvilli in neonatal enteropathy. Apical vesicle trafficking takes center stage in neonatal enteropathies. Impact of cordon-bleu expression on actin cytoskeleton architecture and dynamics Structure of Myo7b/USH1C complex suggests a general PDZ domain binding mode by MyTH4-FERM myosins. Muscle-specific stress fibers give rise to sarcomeres in cardiomyocytes Dynamics of brush border remodeling induced by enteropathogenic E. coli Loss of myosin Vb promotes apical bulk endocytosis in neonatal enterocytes Loss of MYO5B Leads to Reductions in Na+ Absorption With Maintenance of CFTR-Dependent Cl- Secretion in Enterocytes Cordon bleu promotes the assembly of brush border microvilli IRTKS (BAIAP2L1) Elongates Epithelial Microvilli Using EPS8-Dependent and Independent Mechanisms Profilin-Mediated Actin Allocation Regulates the Growth of Epithelial Microvilli An alternative N-terminal fold of the intestine-specific annexin A13a induces dimerization and regulates membrane-binding Motor and tail homology 1 (Th1) domains antagonistically control myosin-1 dynamics Brush Border Destruction by Enterohemorrhagic Escherichia coli (EHEC): New Insights From Organoid Culture MyTH4-FERM myosins in the assembly and maintenance of actin-based protrusions Myosin-7b Promotes Distal Tip Localization of the Intermicrovillar Adhesion Complex Brush border protocadherin CDHR2 promotes the elongation and maximized packing of microvilli in vivo Non-muscle myosin-2 contractility-dependent actin turnover limits the length of epithelial microvilli Actin assembly and non-muscle myosin activity drive dendrite retraction in an UNC-6/Netrin dependent self-avoidance response Shear stress induces noncanonical autophagy in intestinal epithelial monolayers. PACSIN2-dependent apical endocytosis regulates the morphology of epithelial microvilli The Huntingtin-interacting protein SETD2/HYPB is an actin lysine methyltransferase Actin Dynamics Drive Microvillar Motility and Clustering during Brush Border Assembly A heterologous in-cell assay for investigating intermicrovillar adhesion complex interactions reveals a novel protrusion length matching mechanism

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