Dyneins

"Dyneins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure, which enables searching at various levels of specificity.

MeSH information

Definition | Details | More General Concepts | Related Concepts | More Specific Concepts

A family of multisubunit cytoskeletal motor proteins that use the energy of ATP hydrolysis, generated by a ring of AAA ATPASES in the dynein heavy chain, to power a variety of cellular functions. Dyneins fall into two major classes based upon structural and functional criteria.

Descriptor ID	D004398
MeSH Number(s)	D08.811.277.040.013.500.063 D08.811.277.040.025.024.063 D08.811.277.040.025.193.249 D12.776.157.025.750.063 D12.776.220.600.200
Concept/Terms	Dyneins Dyneins Adenosine Triphosphatase, Dynein Dynein Adenosine Triphosphatase Adenosinetriphosphatase, Dynein ATPase, Dynein Dynein ATPase Dynein Dynein Adenosinetriphosphatase Dynein Light Intermediate Chains Dynein Light Intermediate Chains Dynein Light Chains Dynein Light Chains Chains, Dynein Light Light Chains, Dynein Dynein Heavy Chains Dynein Heavy Chains Chains, Dynein Heavy Heavy Chains, Dynein Dynein Intermediate Chains Dynein Intermediate Chains Chains, Dynein Intermediate Intermediate Chains, Dynein

Below are MeSH descriptors whose meaning is more general than "Dyneins".

Chemicals and Drugs [D]
Enzymes and Coenzymes [D08]
Enzymes [D08.811]
Hydrolases [D08.811.277]
Acid Anhydride Hydrolases [D08.811.277.040]
AAA Proteins [D08.811.277.040.013]
ATPases Associated with Diverse Cellular Activities [D08.811.277.040.013.500]
Dyneins [D08.811.277.040.013.500.063]
Adenosine Triphosphatases [D08.811.277.040.025]
ATPases Associated with Diverse Cellular Activities [D08.811.277.040.025.024]
Dyneins [D08.811.277.040.025.024.063]
Molecular Motor Proteins [D08.811.277.040.025.193]
Dyneins [D08.811.277.040.025.193.249]
Amino Acids, Peptides, and Proteins [D12]
Proteins [D12.776]
Carrier Proteins [D12.776.157]
AAA Proteins [D12.776.157.025]
ATPases Associated with Diverse Cellular Activities [D12.776.157.025.750]
Dyneins [D12.776.157.025.750.063]
Cytoskeletal Proteins [D12.776.220]
Microtubule Proteins [D12.776.220.600]
Dyneins [D12.776.220.600.200]

Below are MeSH descriptors whose meaning is related to "Dyneins".

Below are MeSH descriptors whose meaning is more specific than "Dyneins".

publications

Timeline | Most Recent

This graph shows the total number of publications written about "Dyneins" by people in this website by year, and whether "Dyneins" was a major or minor topic of these publications.

Bar chart showing 69 publications over 25 distinct years, with a maximum of 6 publications in 2009

To see the data from this visualization as text, click here.

Year	Major Topic	Minor Topic	Total
1994	2	0	2
1995	5	0	5
1997	3	0	3
1998	1	0	1
1999	2	1	3
2000	0	2	2
2001	2	0	2
2002	2	0	2
2003	2	2	4
2004	4	0	4
2005	4	1	5
2006	2	1	3
2007	3	2	5
2008	3	1	4
2009	5	1	6
2010	1	1	2
2011	1	0	1
2012	2	1	3
2013	1	0	1
2014	1	1	2
2015	3	0	3
2016	1	1	2
2017	2	0	2
2018	0	1	1
2022	1	0	1

Below are the most recent publications written about "Dyneins" by people in Profiles.

Braschi B, Omran H, Witman GB, Pazour GJ, Pfister KK, Bruford EA, King SM. Consensus nomenclature for dyneins and associated assembly factors. J Cell Biol. 2022 02 07; 221(2).

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Kubo T, Hou Y, Cochran DA, Witman GB, Oda T. A microtubule-dynein tethering complex regulates the axonemal inner dynein f (I1). Mol Biol Cell. 2018 05 01; 29(9):1060-1074.

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Hou Y, Witman GB. The N-terminus of IFT46 mediates intraflagellar transport of outer arm dynein and its cargo-adaptor ODA16. Mol Biol Cell. 2017 Sep 01; 28(18):2420-2433.

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Brown JM, Mosley M, Montes-Berrueta D, Hou Y, Yang F, Scarbrough C, Witman GB, Wirschell M. Characterization of a new oda3 allele, oda3-6, defective in assembly of the outer dynein arm-docking complex in Chlamydomonas reinhardtii. PLoS One. 2017; 12(3):e0173842.

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Mann BJ, Balchand SK, Wadsworth P. Regulation of Kif15 localization and motility by the C-terminus of TPX2 and microtubule dynamics. Mol Biol Cell. 2017 01 01; 28(1):65-75.

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Dougherty GW, Loges NT, Klinkenbusch JA, Olbrich H, Pennekamp P, Menchen T, Raidt J, Wallmeier J, Werner C, Westermann C, Ruckert C, Mirra V, Hjeij R, Memari Y, Durbin R, Kolb-Kokocinski A, Praveen K, Kashef MA, Kashef S, Eghtedari F, H?ffner K, Valmari P, Baktai G, Aviram M, Bentur L, Amirav I, Davis EE, Katsanis N, Brueckner M, Shaposhnykov A, Pigino G, Dworniczak B, Omran H. DNAH11 Localization in the Proximal Region of Respiratory Cilia Defines Distinct Outer Dynein Arm Complexes. Am J Respir Cell Mol Biol. 2016 08; 55(2):213-24.

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Schmidts M, Hou Y, Cort?s CR, Mans DA, Huber C, Boldt K, Patel M, van Reeuwijk J, Plaza JM, van Beersum SE, Yap ZM, Letteboer SJ, Taylor SP, Herridge W, Johnson CA, Scambler PJ, Ueffing M, Kayserili H, Krakow D, King SM, Beales PL, Al-Gazali L, Wicking C, Cormier-Daire V, Roepman R, Mitchison HM, Witman GB. TCTEX1D2 mutations underlie Jeune asphyxiating thoracic dystrophy with impaired retrograde intraflagellar transport. Nat Commun. 2015 Jun 05; 6:7074.

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Hou Y, Witman GB. Dynein and intraflagellar transport. Exp Cell Res. 2015 May 15; 334(1):26-34.

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Song K, Awata J, Tritschler D, Bower R, Witman GB, Porter ME, Nicastro D. In situ localization of N and C termini of subunits of the flagellar nexin-dynein regulatory complex (N-DRC) using SNAP tag and cryo-electron tomography. J Biol Chem. 2015 Feb 27; 290(9):5341-53.

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Ott KM, Nguyen T, Navarro C. The DExH box helicase domain of spindle-E is necessary for retrotransposon silencing and axial patterning during Drosophila oogenesis. G3 (Bethesda). 2014 Sep 19; 4(11):2247-57.

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