Results 71 to 80 of about 47,063 (259)

Dynamics of heterodimeric kinesins and cooperation of kinesins

open access: yes, 2004
18 pages, 5 ...
Xie, Ping, Dou, Shuo-Xing, Wang, Peng-Ye
openaire   +2 more sources

Oncogenic role of kinesin proteins and targeting kinesin therapy

open access: yesCancer Science, 2013
The kinesin superfamily (KIF) is a group of proteins that share a highly conserved motor domain. Except for some members, many KIF proteins have adenosine triphosphatase activity and microtubule‐dependent plus‐end motion ability. Kinesins participate in several essential cellular functions, including mitosis, meiosis and the transport of macromolecules.
Xinran, Liu, Hao, Gong, Kun, Huang
openaire   +3 more sources

A new kinesin tree [PDF]

open access: yesJournal of Cell Science, 2004
Dagenbach, E. M. and Endow, S. A. (2004). A new kinesin tree. J. Cell Sci. 117 , [3-7][1]. The neck analysis entries in Table 1 were not aligned correctly in both the print and online versions of this paper. The corrected [Table 1][2] is shown below. We apologise for any inconvenience caused.
Elise M, Dagenbach, Sharyn A, Endow
openaire   +2 more sources

Nuclear Entanglement: New Insights Into the Role of Cytoskeleton and Nucleoskeleton in Plant Nuclear Function

open access: yesCytoskeleton, EarlyView.
ABSTRACT Of the three types of cytoskeleton known in animals—actin, microtubules, and intermediate filaments—only actin and microtubules exist in plants. Both play important roles in cellular shaping, organelle movement, organization of the endomembrane system, and cell signaling.
Norman R. Groves   +3 more
wiley   +1 more source

Optogenetic control of kinesin-1, -2, -3 and dynein reveals their specific roles in vesicular transport

open access: yesCell Reports
Summary: Each cargo in a cell employs a unique set of motor proteins for its transport. To dissect the roles of each type of motor, we developed optogenetic inhibitors of endogenous kinesin-1, -2, -3 and dynein motors and examined their effect on the ...
Sahil Nagpal   +7 more
doaj   +1 more source

Kinesin's second step [PDF]

open access: yesProceedings of the National Academy of Sciences, 2004
We have identified dimeric kinesin mutants that become stalled on the microtubule after one ATP turnover, unable to bind and hydrolyze ATP at their second site. We have used these mutants to determine the regulatory signal that allows ATP to bind to the forward head, such that processive movement can continue.
Lisa M, Klumpp   +2 more
openaire   +2 more sources

In vivo Imaging of oskar mRNA transport reveals the mechanism of posterior localization [PDF]

open access: yes, 2008
oskar mRNA localization to the posterior of the Drosophila oocyte defines where the abdomen and germ cells form in the embryo. Although this localization requires microtubules and the plus end-directed motor, kinesin, its mechanism is controversial and ...
Zimyanin, Vitaly L   +16 more
core   +1 more source

Making Two out of One: Kinesin Motors Driving Plant Cell Division

open access: yesCytoskeleton, EarlyView.
ABSTRACT The Kinesin superfamily of microtubule dependent motors is present in all eukaryotes. Not all of the subfamilies are represented in all kingdoms, and the ones that are do not always show conserved functions. Tight control of the cytoskeleton is essential for proper progression and completion of mitosis and cytokinesis, and key functions are ...
Choy Kriechbaum, Sabine Müller
wiley   +1 more source

Purification, Fluorescent Labeling, and Detyrosination of Mammalian Cell Tubulin for Biochemical Assays

open access: yesCytoskeleton, EarlyView.
ABSTRACT Microtubules play essential roles in numerous cellular processes. All microtubules are built from the protein tubulin, yet individual microtubules can differ spatially and temporally due to their tubulin isotype composition and post‐translational modifications (PTMs).
Ezekiel C. Thomas   +5 more
wiley   +1 more source

Recombinant Monoclonal Antibodies for Detecting the Tubulin Post‐Translational Modifications Glutamylation and Lysine‐40 Acetylation

open access: yesCytoskeleton, EarlyView.
ABSTRACT Post‐translational modifications (PTMs) to tubulin subunits in microtubule filaments are thought to comprise a component of the tubulin code that specifies microtubule functions in cell physiology and animal development. Acetylation of Lysine‐40 (K40) on α‐tubulin (αTub‐K40ac) and glutamylation of both α‐ and β‐tubulin are two tubulin PTMs of ...
Lynne Blasius   +6 more
wiley   +1 more source

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