Results 91 to 100 of about 5,717 (230)

Axonemal Dynein Arms [PDF]

open access: yesCold Spring Harbor Perspectives in Biology, 2016
Axonemal dyneins form the inner and outer rows of arms associated with the doublet microtubules of motile cilia. These enzymes convert the chemical energy released from adenosine triphosphate (ATP) hydrolysis into mechanical work by causing the doublets to slide with respect to each other.
openaire   +2 more sources

Bicaudal D Family Adaptor Proteins Control the Velocity of Dynein-Based Movements

open access: yesCell Reports, 2014
Cargo transport along microtubules is driven by the collective function of microtubule plus- and minus-end-directed motors (kinesins and dyneins). How the velocity of cargo transport is driven by opposing teams of motors is still poorly understood. Here,
Max A. Schlager   +7 more
doaj   +1 more source

Identification and Validation of Biomarkers in Chronic Rhinosinusitis With Nasal Polyps and Study of Their Associated Mechanisms

open access: yesWorld Journal of Otorhinolaryngology - Head and Neck Surgery, EarlyView.
ABSTRACT Background Cell senescence (CS) and lipid metabolism (LM) disorders have been reported in chronic rhinosinusitis with nasal polyps (CRSwNP). However, the mechanism is still unclear. Methods Data were obtained from public databases; differential expression analysis and machine learning were performed to identify biomarkers and to understand the
Hui‐Yi Deng   +3 more
wiley   +1 more source

Sea urchin dyneins

open access: yes, 1989
Dynein is a large, complex microtubule mechanochemical translocator. Although discovered over 25 years ago in the axonemes of protozoa and sea urchin sperm flagella, relatively little is known about the structure and function of this important motor ...
Foltz, Kathleen Rae
core  

Tubulin Polyglutamylation Regulates Axonemal Motility by Modulating Activities of Inner-Arm Dyneins

open access: yes, 2010
SummaryTubulin polyglutamylation is a modification that adds multiple glutamates to the γ-carboxyl group of a glutamate residue in the C-terminal tails of α- and β-tubulin [1, 2].
Kubo, Tomohiro   +4 more
core   +1 more source

CRISPR/Cas9‐mediated Genome‐editing Reveals 10 Testis‐enriched Genes and One Non‐testis‐enriched Gene are Dispensable for Male Fecundity in Mice

open access: yesAndrology, EarlyView.
ABSTRACT Background More than 1000 genes have been identified as predominantly expressed in the human testis. Advances in gene editing technologies have enabled the rapid and efficient generation of genetically engineered mice. This approach facilitates the screening of genes essential for spermatogenesis by analyzing knockout mouse models.
Yumiao Qiu   +2 more
wiley   +1 more source

C11orf70 Mutations Disrupting the Intraflagellar Transport-Dependent Assembly of Multiple Axonemal Dyneins Cause Primary Ciliary Dyskinesia [PDF]

open access: yes, 2018
Primary ciliary dyskinesia (PCD) is a genetically and phenotypically heterogeneous disorder characterized by destructive respiratory disease and laterality abnormalities due to randomized left-right body asymmetry.
Aubusson-Fleury, Anne   +56 more
core   +1 more source

Axonemal Dyneins

open access: yes, 2009
Ritsu Kamiya, Stephen M. King
core   +2 more sources

Microtubule Inner Protein CFAP77 Contributes to Sperm Motility and Male Fertility in Mice

open access: yesAndrology, EarlyView.
ABSTRACT Background Sperm motility is essential for male fertility, and its regulation is dependent on the structural integrity of the axoneme. The axoneme consists of a conserved “9+2” microtubule arrangement and is supported by microtubule inner proteins. However, the functional significance of many microtubule inner proteins remains unclear.
Haoting Wang   +4 more
wiley   +1 more source

Registry alteration in Dynein's microtubule-binding domain: A AAA domain-guided event

open access: yesChemical Physics Impact
Dynein, a motor protein, harnesses chemical energy from ATP hydrolysis to generate mechanical output as it travels along microtubular tracks. Essential to this process is the microtubule-binding domain (MTBD), which facilitates the interaction with and ...
Pradipta Kumar Das, Biman Jana
doaj   +1 more source

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