Results 31 to 40 of about 225,378 (345)

Tubulin acetylation protects long-lived microtubules against mechanical aging

open access: yesNature Cell Biology, 2017
Long-lived microtubules endow the eukaryotic cell with long-range transport abilities. While long-lived microtubules are acetylated on Lys40 of α-tubulin (αK40), acetylation takes place after stabilization and does not protect against depolymerization ...
D. Portran   +4 more
semanticscholar   +1 more source

Actin–microtubule coordination at growing microtubule ends [PDF]

open access: yesNature Communications, 2014
To power dynamic processes in cells, the actin and microtubule cytoskeletons organize into complex structures. Although it is known that cytoskeletal coordination is vital for cell function, the mechanisms by which cross-linking proteins coordinate actin and microtubule activities remain poorly understood.
Preciado López, Magdalena   +6 more
openaire   +6 more sources

Microtubules acquire resistance from mechanical breakage through intralumenal acetylation

open access: yesScience, 2017
Acetylation keeps microtubules strong Cells need microtubules for intracellular transport and to avoid being crushed. On investigating microtubule breakage in live fibroblasts, Xu et al.
Zhenjie Xu   +8 more
semanticscholar   +1 more source

Microtubule heterogeneity of <i>Ornithogalum umbellatum</i> ovary epidermal cells: non-stable cortical microtubules and stable lipotubuloid microtubules

open access: yesFolia Histochemica et Cytobiologica, 2011
Lipotubuloids, structures containing lipid bodies and microtubules, are described in ovary epidermal cells of <i>Ornithogalum umbellatum</i>.
Agnieszka Wojtczak   +4 more
doaj   +1 more source

Suppression of detyrosinated microtubules improves cardiomyocyte function in human heart failure

open access: yesNature Network Boston, 2018
Detyrosinated microtubules provide mechanical resistance that can impede the motion of contracting cardiomyocytes. However, the functional effects of microtubule detyrosination in heart failure or in human hearts have not previously been studied.
C. Y. Chen   +12 more
semanticscholar   +1 more source

Formins and microtubules

open access: yesBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2010
Formins have recently been recognized as prominent regulators of the microtubule (MT) cytoskeleton where they modulate the dynamics of selected MTs in interphase and mitosis. The association of formins with the MT cytoskeleton and their action on MT dynamics are relatively unexplored areas, yet growing evidence supports a direct role in their ...
Gregg G. Gundersen, Francesca Bartolini
openaire   +3 more sources

A "MICROTUBULE" IN A BACTERIUM [PDF]

open access: yesThe Journal of Cell Biology, 1967
A study of the anchorage of the flagella in swarmers of Proteus mirabilis led to the incidental observation of microtubules. These microtubules were found in thin sections and in whole mount preparations of cells from which most of the content had been released by osmotic shock before staining negatively with potassium phosphotungstate (PTA).
Judith F. M. Hoeniger   +2 more
openaire   +3 more sources

Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape

open access: yesJournal of Cell Biology, 1993
Microtubules are long, proteinaceous filaments that perform structural functions in eukaryotic cells by defining cellular shape and serving as tracks for intracellular motor proteins.
F. Gittes   +3 more
semanticscholar   +1 more source

Involvement of cytoskeleton microtubules in the formation of induced aerenchyma in adventitious roots of Zea mays (Poaceae)

open access: yesUkrainian Botanical Journal, 2020
Plants of Zea mays were grown for 12 days in sulfur-deficient medium according to a standard technique applied specifically for formation of aerenchyma cavities in the adventitious roots.
Shevchenko G.V.
doaj   +1 more source

Microtubules Gate Tau Condensation to Spatially Regulate Microtubule Functions

open access: yesNature Cell Biology, 2018
Tau is an abundant microtubule-associated protein in neurons. Tau aggregation into insoluble fibrils is a hallmark of Alzheimer’s disease and other types of dementia1, yet the physiological state of tau molecules within cells remains unclear.
Ruensern Tan   +8 more
semanticscholar   +1 more source

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