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Exome sequencing identifies DYNC2H1 mutations as a common cause of asphyxiating thoracic dystrophy (Jeune syndrome) without major polydactyly, renal or retinal involvement
Exome sequencing identifies DYNC2H1 mutations as a common cause of asphyxiating thoracic dystrophy (Jeune syndrome) without major polydactyly, renal or retinal involvement
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Exome sequencing identifies DYNC2H1 mutations as a common cause of asphyxiating thoracic dystrophy (Jeune syndrome) without major polydactyly, renal or retinal involvement

Schmidts, Miriam ; Arts, Heleen H ; Bongers, Ernie M H F ; Yap, Zhimin ; Oud, Machteld M ; Antony, Dinu ; Duijkers, Lonneke ; Emes, Richard D ; Stalker, Jim ; Yntema, Jan-Bart L ; Plagnol, Vincent ; Hoischen, Alexander ; Gilissen, Christian ; Forsythe, Elisabeth ; Lausch, Ekkehart ; Veltman, Joris A ; Roeleveld, Nel ; Superti-Furga, Andrea ; Kutkowska-Kazmierczak, Anna ; Kamsteeg, Erik-Jan ; Elçioğlu, Nursel ; van Maarle, Merel C ; Graul-Neumann, Luitgard M ; Devriendt, Koenraad ; Smithson, Sarah F ; Wellesley, Diana ; Verbeek, Nienke E ; Hennekam, Raoul C M ; Kayserili, Hulya ; Scambler, Peter J ; Beales, Philip L ; Knoers, Nine VAM ; Roepman, Ronald ; Mitchison, Hannah M

Journal of medical genetics, 2013-05, Vol.50 (5), p.309-323 [Periódico revisado por pares]

England: BMJ Publishing Group Ltd

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12
Small stepping motion of processive dynein revealed by load-free high-speed single-particle tracking
Small stepping motion of processive dynein revealed by load-free high-speed single-particle tracking
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Small stepping motion of processive dynein revealed by load-free high-speed single-particle tracking

Ando, Jun ; Shima, Tomohiro ; Kanazawa, Riko ; Shimo-Kon, Rieko ; Nakamura, Akihiko ; Yamamoto, Mayuko ; Kon, Takahide ; Iino, Ryota

Scientific reports, 2020-01, Vol.10 (1), p.1080, Article 1080 [Periódico revisado por pares]

England: Nature Publishing Group

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13
Mutually Exclusive Cytoplasmic Dynein Regulation by NudE-Lis1 and Dynactin
Mutually Exclusive Cytoplasmic Dynein Regulation by NudE-Lis1 and Dynactin
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Mutually Exclusive Cytoplasmic Dynein Regulation by NudE-Lis1 and Dynactin

McKenney, Richard J. ; Weil, Sarah J. ; Scherer, Julian ; Vallee, Richard B.

The Journal of biological chemistry, 2011-11, Vol.286 (45), p.39615-39622 [Periódico revisado por pares]

United States: Elsevier Inc

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14
Angular measurements of the dynein ring reveal a stepping mechanism dependent on a flexible stalk
Angular measurements of the dynein ring reveal a stepping mechanism dependent on a flexible stalk
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Angular measurements of the dynein ring reveal a stepping mechanism dependent on a flexible stalk

Lippert, Lisa G. ; Dadosh, Tali ; Hadden, Jodi A. ; Karnawat, Vishakha ; Diroll, Benjamin T. ; Murray, Christopher B. ; Holzbaur, Erika L. F. ; Schulten, Klaus ; Reck-Peterson, Samara L. ; Goldman, Yale E.

Proceedings of the National Academy of Sciences - PNAS, 2017-06, Vol.114 (23), p.E4564-E4573 [Periódico revisado por pares]

United States: National Academy of Sciences

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15
DYNLT (Tctex‐1) forms a tripartite complex with dynein intermediate chain and RagA, hence linking this small GTPase to the dynein motor
DYNLT (Tctex‐1) forms a tripartite complex with dynein intermediate chain and RagA, hence linking this small GTPase to the dynein motor
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DYNLT (Tctex‐1) forms a tripartite complex with dynein intermediate chain and RagA, hence linking this small GTPase to the dynein motor

Merino‐Gracia, Javier ; García‐Mayoral, María Flor ; Rapali, Peter ; Valero, Ruth Ana ; Bruix, Marta ; Rodríguez‐Crespo, Ignacio

The FEBS journal, 2015-10, Vol.282 (20), p.3945-3958 [Periódico revisado por pares]

England: Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies

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16
Reconstitution of the human cytoplasmic dynein complex
Reconstitution of the human cytoplasmic dynein complex
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Reconstitution of the human cytoplasmic dynein complex

Trokter, Martina ; Mücke, Norbert ; Surrey, Thomas

Proceedings of the National Academy of Sciences - PNAS, 2012-12, Vol.109 (51), p.20895-20900 [Periódico revisado por pares]

United States: National Academy of Sciences

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17
N-acetyl-D-glucosamine kinase binds dynein light chain roadblock 1 and promotes protein aggregate clearance
N-acetyl-D-glucosamine kinase binds dynein light chain roadblock 1 and promotes protein aggregate clearance
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N-acetyl-D-glucosamine kinase binds dynein light chain roadblock 1 and promotes protein aggregate clearance

Ripon, Md Kamal Hossain ; Lee, HyunSook ; Dash, Raju ; Choi, Ho Jin ; Oktaviani, Diyah Fatimah ; Moon, Il Soo ; Haque, Md Nazmul

Cell death & disease, 2020-08, Vol.11 (8), p.619, Article 619 [Periódico revisado por pares]

England: Springer Nature B.V

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18
Multivalent IDP assemblies: Unique properties of LC8-associated, IDP duplex scaffolds
Multivalent IDP assemblies: Unique properties of LC8-associated, IDP duplex scaffolds
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Multivalent IDP assemblies: Unique properties of LC8-associated, IDP duplex scaffolds

Clark, Sarah A. ; Jespersen, Nathan ; Woodward, Clare ; Barbar, Elisar

FEBS letters, 2015-09, Vol.589 (19), p.2543-2551 [Periódico revisado por pares]

England: Elsevier B.V

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19
A Ras-like domain in the light intermediate chain bridges the dynein motor to a cargo-binding region
A Ras-like domain in the light intermediate chain bridges the dynein motor to a cargo-binding region
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A Ras-like domain in the light intermediate chain bridges the dynein motor to a cargo-binding region

Schroeder, Courtney M ; Ostrem, Jonathan M L ; Hertz, Nicholas T ; Vale, Ronald D

eLife, 2014-10, Vol.3, p.e03351-e03351 [Periódico revisado por pares]

England: eLife Sciences Publications Ltd

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20
Analytical ultracentrifugation: A versatile tool for the characterisation of macromolecular complexes in solution
Analytical ultracentrifugation: A versatile tool for the characterisation of macromolecular complexes in solution
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Analytical ultracentrifugation: A versatile tool for the characterisation of macromolecular complexes in solution

Patel, Trushar R. ; Winzor, Donald J. ; Scott, David J.

Methods (San Diego, Calif.), 2016-02, Vol.95, p.55-61 [Periódico revisado por pares]

United States: Elsevier Inc

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