Results 291 to 300 of about 296,624 (347)

Post‐LECA Origin and Diversification of an Axonemal Outer Arm Dynein Motor

open access: yesCytoskeleton, EarlyView.
ABSTRACT Dyneins were present in the last eukaryotic common ancestor (LECA) and play key roles in eukaryotic biology. Axonemal dyneins form the inner and outer arms that power ciliary beating, and it has long been recognized that outer arms in some organisms contain two different heavy chain motors, whereas those from other species contain a third unit
Stephen M. King
wiley   +1 more source

Discovery of an Atypical Arp2/3 Complex in Malaria Parasites Sheds New Light on Nuclear Actin

open access: yesCytoskeleton, EarlyView.
ABSTRACT The Arp2/3 complex is a key actin nucleator essential for cytoskeletal dynamics in eukaryotes. Previously believed absent in apicomplexan parasites, we recently identified an atypical Arp2/3 complex in malaria parasites consisting of five divergent subunits and a putative kinetochore‐associated factor.
Franziska Hentzschel   +2 more
wiley   +1 more source

Titin Is Present in the Elastic Tethers That Connect Separating Anaphase Chromosomes in Crane‐Fly Spermatocytes

open access: yesCytoskeleton, EarlyView.
ABSTRACT Elastic tethers connect telomeres of separating chromosomes in anaphase of animal cells. Immunofluorescence staining of titin in crane‐fly spermatocytes, using 4 different antibodies, shows that the giant elastic protein titin seems to be a component of mitotic tethers: titin “strands” extend between separating chromosomes, connecting their ...
Demetra Economopoulos   +5 more
wiley   +1 more source

Isoform Specificity of a Compound Targeting Actin Filaments Containing Tropomyosin Tpm1.8/1.9

open access: yesCytoskeleton, EarlyView.
ABSTRACT The unbranched actin filaments in mammalian cells are usually composed of co‐polymers of a specific tropomyosin isoform with actin. Genetic manipulation has revealed that the tropomyosins largely define the functional properties of actin filaments in an isoform‐specific, non‐redundant manner.
Jeff Hook   +2 more
wiley   +1 more source

The C‐Terminal Regions of TRAK Proteins Contain MIRO‐Independent Mitochondrial Localization Domains

open access: yesCytoskeleton, EarlyView.
ABSTRACT Current models suggest that MIRO GTPases anchor cytoskeletal motors to the mitochondrial outer membrane (MOM). However, our previous findings indicate that the unconventional myosin, MYO19, interacts with MIRO weakly and that a MIRO‐independent MOM‐localizing domain interacts more tightly with the MOM.
Lili Mitchell   +4 more
wiley   +1 more source
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Microtubules and microtubule-associated proteins

Current Opinion in Cell Biology, 1995
Microtubule research is becoming increasingly diverse, reflecting the many isoforms and modifications of tubulin and the many proteins with which microtubules interact. Recent advances are particularly visible in four areas: microtubule motor proteins (their structures, stepping modes, and forces); microtubule nucleation (the roles of centrosomes and ...
Mandelkow, Eckhard, Mandelkow, Eva
openaire   +3 more sources

Phosphorylation of Microtubule‐Associated Proteins

European Journal of Biochemistry, 1976
1. Tubulin is not an adenosine-3':5'-monophosphate-dependent (cyclic-AMP-dependent) protein kinase. Both entities have been clearly separated by sucrose gradient ultracentrifugation. With a tubulin preparation obtained by the polymerization-depolymerization technique protein kinase had a sedimentation coefficient of 8.7 S whereas tubulin sedimented ...
L, Rappaport   +4 more
openaire   +2 more sources

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 ...
openaire   +2 more sources

Regulation of microtubule-associated proteins

2001
Microtubule-associated proteins (MAPs) function to regulate the assembly dynamics and organization of microtubule polymers. Upstream regulation of MAP activities is the major mechanism used by cells to modify and control microtubule assembly and organization.
L, Cassimeris, C, Spittle
openaire   +2 more sources

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