Results 71 to 80 of about 29,043 (290)

The divergent mitotic kinesin MKLP2 exhibits atypical structure and mechanochemistry

open access: yeseLife, 2017
MKLP2, a kinesin-6, has critical roles during the metaphase-anaphase transition and cytokinesis. Its motor domain contains conserved nucleotide binding motifs, but is divergent in sequence (~35% identity) and size (~40% larger) compared to other kinesins.
Joseph Atherton   +11 more
doaj   +1 more source

Two kinesins drive anterograde neuropeptide transport

open access: yesMolecular Biology of the Cell, 2017
Current anterograde transport models focus on one type of plus-end–directed kinesin for each type of cargo. This study shows that two anterograde motors, kinesin-1 and kinesin-3, both contribute to the transport of neuropeptide-filled vesicles in axons ...
Angeline Lim, A. Rechtsteiner, W. Saxton
semanticscholar   +1 more source

A look into kinesin's powerhouse [PDF]

open access: yesFEBS Letters, 2001
Kinesins are microtubule‐dependent motors that serve a multitude of cellular purposes. The conserved motor domain provides the energy required for these processes. Shortly after the solution of the first kinesin motor domain crystal structures the similarity to myosin and G‐proteins was noted.
openaire   +3 more sources

Proposed Mechanism of Kinesin Backstepping [PDF]

open access: yesBiophysical Journal, 2019
AbstractKinesin-1 is an ATP-driven molecular motor that transports cellular cargo along microtubules. At low loads, kinesin-1 almost always steps forwards, towards microtubule plus ends, but at higher loads, it can also step backwards. Backsteps are usually 8 nm, but can be larger. These larger backwards events of 16 nm, 24 nm or more are thought to be
Algirdas Toleikis   +2 more
openaire   +9 more sources

Carbon Quantum Dots Assisted Virus Tracking: From Skin to Brain

open access: yesAdvanced Materials, EarlyView.
A novel carbon quantum dots‐dissolvable microneedle, CQDs‐dMN system, enables painless delivery and real‐time tracking of HSV‐1. The HSV‐1 is labeled with fluorescent CQDs and delivered to the skin dermis, minimizing damage compared to traditional methods.
Yaxiu Feng   +11 more
wiley   +1 more source

Microfilament‐Myosin II Regulates the Differentiation of Multinucleated Cysts into Oocytes and Influences Oocyte Developmental Potential in Mice

open access: yesAdvanced Science, EarlyView.
In this study, we provided new evidence identifying multinucleated cysts as precursors for oocyte differentiation. Within these cysts, organelles migrate and aggregate to form Balbiani body (B‐body) and establish early cellular polarity. Concurrently, excess nuclei are expelled, enabling cyst‐to‐oocyte differentiation. The microfilament‐myosin II plays
Rui Xu   +7 more
wiley   +1 more source

Histone Lactylation‐Driven Upregulation of VRK1 Expression Promotes Stemness and Proliferation of Glioma Stem Cells

open access: yesAdvanced Science, EarlyView.
Glioblastoma (GBM) is the most aggressive primary brain tumor, with glioma stem cells (GSCs) driving treatment resistance. This study reveals that lactate promotes histone lactylation (H3K18la) at the VRK1 promoter, regulating GSC stemness and proliferation via the H3K18la/VRK1/YBX1/SOX2 pathway. The VRK1‐targeted nanoliposome A/TMZ‐siVRK1 demonstrates
Jinna Li   +4 more
wiley   +1 more source

Phylogenetic analysis of the kinesin superfamily from Physcomitrella

open access: yesFrontiers in Plant Science, 2012
Kinesins are an ancient superfamily of microtubule dependent motors. They participate in an ex-tensive and diverse list of essential cellular functions, including mitosis, cytokinesis, cell polari-zation, cell elongation, flagellar development, and ...
Zhiyuan eShen   +4 more
doaj   +1 more source

Understanding the emergence of collective motion of microtubules driven by kinesins: role of concentration of microtubules and depletion force

open access: yes, 2017
We investigated the role of the concentration of microtubules and depletion force in the emergence of collective motion of microtubules driven by kinesins.
Ai Saito   +6 more
semanticscholar   +1 more source

ATP Hydrolysis by α‐Synuclein Amyloids is Mediated by Enclosing β‐Strand

open access: yesAdvanced Science, EarlyView.
Pathological amyloids have been considered chemically inert until recently. Here it is shown that α‐synuclein amyloids catalyze the hydrolysis of the universal energy molecule, ATP. The cryo‐EM structure of the complex reveals an additional β‐strand (purple) that encloses the ATP‐binding site. Within the cavity, several lysine residues are required for
Lukas Frey   +6 more
wiley   +1 more source

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