Results 351 to 360 of about 1,320,439 (381)

Microtubule-Associated Proteins and the Flexibility of Microtubules

Biochemistry, 1995
Experiments were conducted to learn whether the binding of microtubule-associated proteins (MAPs) to microtubules alters the flexibility of the microtubules. Flexibility was measured in vitro by two established techniques. The first employed measurement of the bending of the microtubule in a flow of buffer; the second involved repeated measurement of ...
Robley C. Williams, Jeffrey C. Kurz
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Structure and elasticity of microtubule-associated protein tau [PDF]

Nature, 1988
Tau is one of the diverse group of microtubule-associated proteins that bind to microtubules and may thereby influence their structure and function. It occurs in the mammalian brain, mainly in axons, and is a component of the neurofibrillary tangles of Alzheimer's disease.
Lichtenberg, B., Mandelkow, E.-M., Hagestedt, T., Mandelkow, E.   +3 more
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Characterization of microtubule-associated proteins in teleosts

Cell Motility and the Cytoskeleton, 1999
Although microtubules are known to play an important role in many cellular processes, they have been virtually neglected in fish. In this report, microtubule-associated proteins (MAPs) in fish (teleost) were characterized using antibodies (Abs) directed against the mammalian MAPs tau, MAP1A and B, and MAP 2.
John G. Wood, Henry Tomasiewicz
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Isolation of Microtubules and Microtubule-Associated Proteins

2016
Microtubules are essential cellular structures in plant cells. They are polymerized from tubulin dimers and are regulated by microtubule-associated proteins (MAPs). Here, we describe a protocol for purifying tubulin dimers and MAPs from plant cells.
Seiji Sonobe, Takahiro Hamada
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A new class of microtubule-associated proteins in plants [PDF]

Nature Cell Biology, 2000
In plants there are three microtubule arrays involved in cellular morphogenesis that have no equivalent in animal cells. In animals, microtubules are decorated by another class of proteins - the structural MAPS - which serve to stabilize microtubules and assist in their organization.
Isolde Häuser-Hahn, Chang-Jie Jiang, Hisako Igarashi, Hisako Igarashi, Clive W. Lloyd, Andrei Smertenko, Norihan Saleh, Patrick J. Hussey, Patrick J. Hussey, Seiji Sonobe, Hitoshi Mori   +10 more
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Non-motor microtubule-associated proteins

Current Opinion in Cell Biology, 1991
Cloning of primary sequences has generated information on the structures of the non-motor microtubule-associated proteins and their relationship to one another. Questions about how classes of microtubule-associated proteins interact are starting to be addressed in vitro and, in vivo, tests of function are being pursued using a variety of cellular and ...
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Non-motor microtubule-associated proteins

Current Opinion in Cell Biology, 1993
This past year, the structure and function of microtubule-associated proteins (MAPs) have been investigated in studies probing their phosphorylation, patterns of expression, and the function of the microtubule-binding domain. Cellular studies have also contributed new insights into the roles of these proteins in process outgrowth.
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Tubulin and Microtubule-Associated Proteins [PDF]

, 1995
A 75 kDa spherical molecule of ~9 nm in diameter, probably dimeric (~150 kDa) in its native form. A heat unstable, non-calmodulin binding MAP of sea urchin eggs.
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Microtubule-associated proteins in higher plants

Journal of Plant Research, 2007
A variety of microtubule-associated proteins (MAPs) have been reported in higher plants. Microtubule (MT) polymerization starts from the gamma-tubulin complex (gammaTuC), a component of the MT nucleation site. MAP200/MOR1 and katanin regulate the length of the MT by promoting the dynamic instability of MTs and cutting MTs, respectively. In construction
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Microtubule-associated proteins and neuronal morphogenesis

Journal of Cell Science, 1991
ABSTRACT The microtubule-associated proteins (MAPs) are a set of structural proteins that bind to microtubules in vitro. Several of them occur at high levels in neurons where their expression is under strong developmental regulation, suggesting that they are involved in neuronal morphogenesis. Recently cDNAs for several of them have been
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