Stathmin
Mostrando 1-12 de 24 artigos, teses e dissertações.
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1. Coexpressão relevante de STMN1, MELK e FOXM1 em glioblastoma e revisão do impacto de stmn1 na biologia do câncer
OBJETIVO: Analisar as expressões associadas de STMN1, MELK e FOXM1 na procura de alvos alternativos de tratamento em glioblastoma (GBM) e revisar os papeis funcionais relevantes de STMN1 na biologia do câncer. MÉTODO: As expressões de STMN1, MELK e FOXM1 foram estudadas por PCR quantitativo e suas coexpressões foram analisadas em dois coortes independ
MedicalExpress (São Paulo, online). Publicado em: 2017-10
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2. Stathmin 1 expression in plasma cell neoplasms
Rev. Bras. Hematol. Hemoter.. Publicado em: 2017-06
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3. Drosophila Stathmin: A Microtubule-destabilizing Factor Involved in Nervous System Formation
Stathmin is a ubiquitous regulatory phosphoprotein, the generic element of a family of neural phosphoproteins in vertebrates that possess the capacity to bind tubulin and interfere with microtubule dynamics. Although stathmin and the other proteins of the family have been associated with numerous cell regulations, their biological roles remain elusive, as in
The American Society for Cell Biology.
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4. Stathmin/Op18 Phosphorylation Is Regulated by Microtubule Assembly
Stathmin/Op 18 is a microtubule (MT) dynamics-regulating protein that has been shown to have both catastrophe-promoting and tubulin-sequestering activities. The level of stathmin/Op18 phosphorylation was proved both in vitro and in vivo to be important in modulating its MT-destabilizing activity. To understand the in vivo regulation of stathmin/Op18 act
The American Society for Cell Biology.
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5. Regulation of Microtubule Dynamic Instability in Vitro by Differentially Phosphorylated Stathmin*
Stathmin is an important regulator of microtubule polymerization and dynamics. When unphosphorylated it destabilizes microtubules in two ways, by reducing the microtubule polymer mass through sequestration of soluble tubulin into an assembly-incompetent T2S complex (two α:β tubulin dimers per molecule of stathmin), and by increasing the switching frequency
American Society for Biochemistry and Molecular Biology.
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6. Stathmin interaction with a putative kinase and coiled-coil-forming protein domains.
Stathmin is a ubiquitous, cytosolic 19-kDa protein, which is phosphorylated on up to four sites in response to many regulatory signals within cells. Its molecular characterization indicates a functional organization including an N-terminal regulatory domain that bears the phosphorylation sites, linked to a putative alpha-helical binding domain predicted to p
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7. Model for stathmin/OP18 binding to tubulin
Stathmin/OP18 is a regulatory phosphoprotein that controls microtubule (MT) dynamics. The protein does not have a defined three-dimensional structure, although it contains three distinct regions (an unstructured N–terminus, N: 1–44; a region with high helix propensity, H 1: 44–89; and a region with low helix propensity, H 2: 90–142). The full protein
Oxford University Press.
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8. Stathmin is expressed by the proliferating hepatocytes during liver regeneration
Aim—To determine the liver cell populations that express the phylogenetically conserved cytosolic protein stathmin during liver regeneration.
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9. Deciphering the Cellular Functions of the Op18/Stathmin Family of Microtubule-Regulators by Plasma Membrane-targeted Localization
The Op18/stathmin family of microtubule regulators includes the ubiquitous cytosolic Op18/stathmin (Op18) and the neuronal, primarily Golgi-associated proteins SCG10 and RB3, which all form ternary complexes with two head-to-tail–aligned tubulin heterodimers. To understand the physiological significance of previously observed differences in ternary complex
The American Society for Cell Biology.
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10. Phosphorylation disrupts the central helix in Op18/stathmin and suppresses binding to tubulin
Protein phosphorylation represents a ubiquitous control mechanism in living cells. The structural prerequisites and consequences of this important post-translational modification, however, are poorly understood. Oncoprotein 18/stathmin (Op18) is a globally disordered phosphoprotein that is involved in the regulation of the microtubule (MT) filament system. H
Oxford University Press.
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11. STAT3-Stathmin Interactions Control Microtubule Dynamics in Migrating T-cells*S⃞
T-cell migration is a complex highly coordinated process that involves cell adhesion to the high endothelial venules or to the extracellular matrix by surface receptor/ligand interactions, cytoskeletal rearrangements, and phosphorylation-dependent signaling cascades. The mechanism(s) that regulates T-cell migration is of considerable relevance for unders
American Society for Biochemistry and Molecular Biology.
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12. Op18/stathmin caps a kinked protofilament-like tubulin tetramer
Oncoprotein 18/stathmin (Op18), a regulator of microtubule dynamics, was recombinantly expressed and its structure and function analysed. We report that Op18 by itself can fold into a flexible and extended α-helix, which is in equilibrium with a less ordered structure. In complex with tubulin, however, all except the last seven C-terminal residues of Op18 a
Oxford University Press.