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Human Polyclonal DYNC1H1 Primary Antibody pour ELISA - ABIN4268688
Chen, Levedakou, Millen, Wollmann, Soliven, Popko: Proprioceptive sensory neuropathy in mice with a mutation in the cytoplasmic Dynein heavy chain 1 gene. dans The Journal of neuroscience : the official journal of the Society for Neuroscience 2007
Human Polyclonal DYNC1H1 Primary Antibody pour ICC, IF - ABIN4306503
Barisic, Aguiar, Geley, Maiato: Kinetochore motors drive congression of peripheral polar chromosomes by overcoming random arm-ejection forces. dans Nature cell biology 2014
Data show that basal body docking was unaffected in dynein 1 (dync1h1) mutation, but rab GTP-binding protein Rab6 expression was reduced.
dync1h1 promotes axon ensheathment and myelin gene expression.
This study provided evidence that Dync1h1 is also required for efficient myelination of peripheral axons by Schwann cells, perhaps by facilitating signal transduction necessary for myelination.
These observations, combined with protein localization studies, suggest that Dynein1 may have direct and essential functions in photoreceptor outer segments, in addition to inner segment functions.
demonstrate that the outward transport of dynein from soma to axon terminal is driven by direct interactions with the anterograde motor kinesin-1.
The Swl/Swl mutation of Dync1h1 gene led to embryonic mal-development and lethality, whereas the Swl/+ DRG neurons demonstrated deficient retrograde transport in dynein-driven cargos and excessive apoptosis during mid- to late-developmental stages.
These data unveil a previously unrecognized role for the dynein-dynactin motor complex in osteoclast formation and function.
The Loa heterozygote phenotype is morphometrically depleted; in addition to dendritic axonal defects, the Loa mutation in a mouse model for mixed motor-sensory loss considers the entire neuraxis and is not a model for sensory loss.
Snapin-dynein coupling is one of the primary mechanisms driving BDNF-TrkB retrograde transport, thus providing mechanistic insights into the regulation of neuronal growth and survival.
Data show that amyloid precursor protein (APP) levels are well-correlated with the amount of the light chain of kinesin-1 (KLC1).
neuromuscular junction defects in mice with mutation of dynein heavy chain 1
Results provide genetic evidence that dynein plays a key role in lipid metabolism and thermogenesis.
These results suggest a potential role for the dynein tail in motor function, and provide direct evidence for a link between single-motor processivity and disease.
Impairment of retrograde transport by knockdown of DHC1 or BicD1 inhibits stress-granule formation and P-body growth upon stress.
results show that missense point mutations result in progressive motor neuron degeneration in heterozygous mice, and in homozygotes this is accompanied by the formation of Lewy-like inclusion bodies, resembling key features of human pathology
Results describe the gene encoding the dynein axonemal light intermediate chain Dnali1, and suggest that the C-terminal part of the cytoplasmic dynein heavy chain 1 is a putative interacting polypeptide of Dnali1.
This study provide in vivo evidence that distinct mutations in cytoplasmic dynein can either result in a pure sensory neuropathy or in a sensory neuropathy with motor neuron involvement.
A new mouse mutation, Sprawling, highlights an essential role for the dynein heavy chain in sensory neuron function.
Mice with a mutation in the dynein heavy chain 1 gene display sensory neuropathy but lack motor neuron disease.
Using in vitro total internal reflection fluorescence microscopy, the study observed that higher concentrations of Ndc80 inhibited dynein binding to microtubules, providing evidence that Ndc80 and dynein antagonize each other's function.
Taken together, these results demonstrate DYNC1H1 as a strong candidate and RTP1 as a potential candidate on the onset of epileptic encephalopathies.
Here, the authors use quantitative imaging and laser ablation to show that NuMA targets dynactin to spindle microtubule minus-ends, localizing dynein activity there.
Structural and functional mutations and hotspots for DYNC1H1.
This observation offers an explanation for the dominant effects of DYNC1H1 mutations in vivo.
This cohort demonstrates that mutations in DYNC1H1 can mimic a congenital myopathy.
These results suggest that cytoplasmic dynein 1 binds to BRCA2 through the latter's centrosomal localization signal and BRCA2 mediates the cohesion between centrosomes during the S phase, potentially serving as a cell-cycle checkpoint.
A novel de novo mutation (c.2327C > T, p.P776L) in the DYNC1H1 gene identified and confirmed it as the causal variant of Spinal muscular atrophy with lower extremity predominance.
Our findings suggest that DYNC1H1 variants can cause not only lower, but also upper motor neuron disease.
The mutations in DYNC1H1 increase the interaction with its adaptor BICD2.
Dynactin functions as both a dynamic tether and brake during dynein-driven motility.
These findings also reveal a possible new target for Amblyomin-X, i.e., dynein, and may serve as a tool for investigating tumor cell death associated with proteasome inhibition.
These results reveal that conformational changes involving hexon hypervariable region 1 are the basis for a novel viral mechanism controlling capsid transport to the nucleus by dynein.
Report expands the clinical spectrum of DYNC1H1-related spinal muscular atrophy to include generalized arthrogryposis
Authors propose that Snapin connects chlamydial inclusions with the microtubule network by interacting with both Chlamydia psittaci IncB and dynein.
Authors find that pharmacological or small interfering RNA (siRNA)-mediated inhibition of cytoplasmic dynein or the kinesin 1 heavy chain KIF5B delays HIV-1 uncoating.
single dynein molecules in the cell are autoinhibited through intramolecular head-head stacking
Our results expand the set of pathological mutations in DYNC1H1, reinforce the role of cytoplasmic dynein in disorders of neuronal migration, and provide evidence for a syndrome including spinal nerve degeneration and brain developmental problems.
This study demonistrated that DYNC1H1 mutation alters transport kinetics and ERK1/2-cFos signalling in a mouse model of distal spinal muscular atrophy.
It focus on cytoplasmic dynein, which is required for a myriad of cellular functions in interphase, mitosis and meiosis, ranging from transport of organelles and functioning of the mitotic spindle to chromosome movements in meiotic prophase.
Dyneins are a group of microtubule-activated ATPases that function as molecular motors. They are divided into two subgroups of axonemal and cytoplasmic dyneins. The cytoplasmic dyneins function in intracellular motility, including retrograde axonal transport, protein sorting, organelle movement, and spindle dynamics. Molecules of conventional cytoplasmic dynein are comprised of 2 heavy chain polypeptides and a number of intermediate and light chains.This gene encodes a member of the cytoplasmic dynein heavy chain family.
cytoplasmic dynein 1 heavy chain 1
, cytoplasmic dynein
, MAP 1C
, cytoplasmic dynein heavy chain 1
, dynein heavy chain, cytosolic
, dynein, cytoplasmic, heavy chain 1
, dynein heavy chain, retrograde transport
, legs at odd angle
, dynein, cytoplasmic, heavy polypeptide 1