Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Matthew P. Nicholas"'
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-17 (2019)
The cytoplasmic motor protein dynein senses directional tension; its microtubule-binding domains bind microtubules more strongly when under backward load. Here the authors use optical tweezers to show that the linker, buttress, and stalk domains toge
Externí odkaz:
https://doaj.org/article/325aff2c653c44afabe5feb61e8dc048
Publikováno v:
Essentials in Ophthalmology ISBN: 9783031117190
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ac9e417482035d6c88c4239f534a9c56
https://doi.org/10.1007/978-3-031-11720-6_11
https://doi.org/10.1007/978-3-031-11720-6_11
Publikováno v:
Journal of Glaucoma. 30:e344-e346
A 57-year-old woman presented with photophobia and complaint of a persistent white light in the inferior field of her left eye for 18 months following laser peripheral iridotomy both eyes. In primary gaze, the upper lid margin was noted to bisect the
Autor:
Matthew P. Nicholas, Naveen Mysore
Publikováno v:
Experimental Eye Research. 202:108363
The optical clarity of the cornea is essential for maintaining good visual acuity. Corneal neovascularization, which is a major cause of vision loss worldwide, leads to corneal opacification and often contributes to a cycle of chronic inflammation. W
Publikováno v:
Science Advances
Science advances, 6(15), 1. American Association for the Advancement of Science
Science advances, 6(15), 1. American Association for the Advancement of Science
We present a novel experimental framework allowing for determination of the maximal force generation of weakly processive motors.
Cytoplasmic dynein is a highly complex motor protein that generates forces toward the minus end of microtubules. Us
Cytoplasmic dynein is a highly complex motor protein that generates forces toward the minus end of microtubules. Us
Publikováno v:
Nature Communications
Nature Communications, Vol 10, Iss 1, Pp 1-17 (2019)
Nature Communications, Vol 10, Iss 1, Pp 1-17 (2019)
Cytoplasmic dynein is the most complex cytoskeletal motor protein and is responsible for numerous biological functions. Essential to dynein’s function is its capacity to respond anisotropically to tension, so that its microtubule-binding domains bi
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Cytoplasmic dynein is a homodimeric microtubule (MT) motor protein responsible for most MT minus-end-directed motility. Dynein contains four AAA+ ATPases (AAA: ATPase associated with various cellular activities) per motor domain (AAA1-4). The main si
Publikováno v:
Biophysical Journal. 112:5a
Cytoskeletal motor protein motility requires coordination of ATPase and filament-binding cycles. Mechanical tension strongly influences these processes, and likely regulates motor stepping as external forces resist motor movement and intramolecular t
Autor:
Arne Gennerich, Matthew P. Nicholas, Richard B. Vallee, Caitlin L. Wynne, Sibylle Brenner, Peter Höök
Publikováno v:
Nature Communications
Cytoplasmic dynein is a microtubule motor involved in cargo transport, nuclear migration and cell division. Despite structural conservation of the dynein motor domain from yeast to higher eukaryotes, the extensively studied S. cerevisiae dynein behav
Publikováno v:
Methods in Molecular Biology ISBN: 9781493903283
Numerous microtubule-associated molecular motors, including several kinesins and cytoplasmic dynein, produce opposing forces that regulate spindle and chromosome positioning during mitosis. The motility and force generation of these motors are theref