Recombinant Human Cytoplasmic dynein 1 heavy chain 1 (DYNC1H1), partial

1. Taken together, these results demonstrate DYNC1H1 as a strong candidate and RTP1 as a potential candidate on the onset of epileptic encephalopathies. PMID: 28325891
2. Here, the authors use quantitative imaging and laser ablation to show that NuMA targets dynactin to spindle microtubule minus-ends, localizing dynein activity there. PMID: 29185983
3. Structural and functional mutations and hotspots for DYNC1H1. PMID: 28455235
4. This observation offers an explanation for the dominant effects of DYNC1H1 mutations in vivo. PMID: 28196890
5. This cohort demonstrates that mutations in DYNC1H1 can mimic a congenital myopathy. PMID: 28554554
6. 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. PMID: 27433848
7. 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. PMID: 26846447
8. Our findings suggest that DYNC1H1 variants can cause not only lower, but also upper motor neuron disease. PMID: 26100331
9. The mutations in DYNC1H1 increase the interaction with its adaptor BICD2. PMID: 25512093
10. 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. PMID: 25479096
11. 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. PMID: 25355895
12. Report expands the clinical spectrum of DYNC1H1-related spinal muscular atrophy to include generalized arthrogryposis PMID: 25609763
13. Authors propose that Snapin connects chlamydial inclusions with the microtubule network by interacting with both Chlamydia psittaci IncB and dynein. PMID: 24751478
14. 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. PMID: 25231297
15. single dynein molecules in the cell are autoinhibited through intramolecular head-head stacking PMID: 25266423
16. 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. PMID: 24307404
17. This study demonistrated that DYNC1H1 mutation alters transport kinetics and ERK1/2-cFos signalling in a mouse model of distal spinal muscular atrophy. PMID: 24755273
18. 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. PMID: 24256283
19. In conclusion, association with microtubules and the translocation activity of dynein motor complexes are required to achieve efficient retrovirus restriction by TRIM5alpha. PMID: 24600008
20. This study demonistrated that Dynein mutations associated with hereditary motor neuropathies impair mitochondrial morphology and function with age. PMID: 23742762
21. Data indicate that dynein- and astral microtubule-mediated transport of Galphai/LGN/nuclear mitotic apparatus (NuMA) complex from cell cortex to spindle poles. PMID: 23389635
22. The cytoplasmic Dynein Heavy Chain 1 (DHC) was found to interact with NF1 along microtubules in vesicular structures identified to be melanosomes. PMID: 23583712
23. Dynein forms distinct complexes requiring specific recruiters and activators to promote orderly progression through mitosis. PMID: 23589491
24. this study has demonstrated that the same DYNC1H1 mutation could cause spinal muscular atrophy as well as distal neuropathy, indicating pleotropic effects of the mutation. PMID: 22847149
25. analysis of reconstitution of the human cytoplasmic dynein complex PMID: 23213255
26. study demonstrates that mutations in the tail domain of the heavy chain of cytoplasmic dynein (DYNC1H1) cause spinal muscular atrophy and provide experimental evidence that a DYNC1H1 mutation disrupts dynein complex assembly and function PMID: 22459677
27. Mutations in DYNC1H1 can lead to a broad phenotypic spectrum, confirming the importance of DYNC1H1 in both central and peripheral neuronal functions. PMID: 22368300
28. Exome sequencing of three affected individuals separated by eight meioses identified a single shared novel heterozygous variant, c.917A>G, in DYNC1H1, which encodes the cytoplasmic dynein heavy chain 1. PMID: 21820100
29. In an in vitro MT gliding assay, both dynein-1 and dynein-2 showed minus-end-directed motor activities. PMID: 21723285
30. mediates the perinuclear aggregation of phagocytosed melanosomes, participates in the formation of the supranuclear melanin cap or "microparasol" and serves as a mechanism to help protect the nucleus from ultraviolet-induced DNA damage. PMID: 14632200
31. these results suggest that complexes of dynein, Lis1 and CLIP-170 crosslink and slide microtubules within the spindle, thereby producing an inward force that pulls centrosomes together. PMID: 19020519

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HGNC: 2961

OMIM: 158600

KEGG: hsa:1778

STRING: 9606.ENSP00000348965

UniGene: Hs.614080