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Microtubule function in morphological differentiation: growth zones and growth cones

Article Abstract:

Experiments on the functions of microtubules in the cytoskeletal structure of cells show notable results. Cells of animals which grow in culture usually have symmetric form and structure but when the growth media are altered or changed, they can cause asymmetric morphology on the shape of animal cells. Certain drugs that depolymerize microtubules curb the acquisition of differentiated form of cells. The probable reason for this is the existence of molecules that are accountable for motile specializations at the cell border and whose area relies on intact microtubules.

Author: Vega, Leticia R., Solomon, Frank
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1997
Morphogenesis, Morphology (Animals), Animal morphology

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RbI2p, a yeast protein that binds to beta-tubulin and participates in microtubule function in vivo

Article Abstract:

Three non-tubulin yeast genes are capable, when overexpressed, of rescuing cellus from the toxic excess beta-tubulin. RbI2p, a yeast protein that binds to beta-tubulin participates in microtubule morphogenesis. RbI2p binds to beta-tubulin in vivo. RbI2p has functional homology with murine cofactor A, a protein essential for in vitro assays of beta-tubulin folding. Another, RBL2, rescues beta-tubulin lethality as well as alpha-tubulin does.

Author: Vega, Leticia R., Archer, Julie E., Solomon, Frank
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
Analysis

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CLIP-170 highlights growing microtubule ends in vivo

Article Abstract:

A chimera with the green fluorescent protein (GFP) was produced to examine the dynamic characteristics of the endosome-microtubule linker protein CLIP-170 (GFP-CLIP170). GFP-CLIP170 was observed to bind in stretches along a subset of microtubule ends. Findings suggest that GFP-CLIP170 emphasizes growing microtubule ends by specifically recognizing the structure of a portion of newly polymerized tubulin.

Author: Kreis, Thomas E., Perez, Franck, Diamantopoulos, Georgios S., Stalder, Romaine
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1999

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Subjects list: Research, Microtubules, Proteins, Tubulins, Tubulin
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