Cryo-EM unveils kinesin KIF1A's processivity mechanism and the impact of its pathogenic variant P305L.

Autor: Benoit MPMH; Department of Biochemistry and Gruss-Lipper Biophotonics Center, Albert Einstein College of Medicine, Bronx, NY, 10461, USA. matthieu.benoit@univ-rennes.fr., Rao L; Department of Biochemistry and Gruss-Lipper Biophotonics Center, Albert Einstein College of Medicine, Bronx, NY, 10461, USA., Asenjo AB; Department of Biochemistry and Gruss-Lipper Biophotonics Center, Albert Einstein College of Medicine, Bronx, NY, 10461, USA., Gennerich A; Department of Biochemistry and Gruss-Lipper Biophotonics Center, Albert Einstein College of Medicine, Bronx, NY, 10461, USA. arne.gennerich@einsteinmed.edu., Sosa H; Department of Biochemistry and Gruss-Lipper Biophotonics Center, Albert Einstein College of Medicine, Bronx, NY, 10461, USA. hernando.sosa@einsteinmed.edu.

Publikováno v: Nature communications [Nat Commun] 2024 Jul 02; Vol. 15 (1), pp. 5530. Date of Electronic Publication: 2024 Jul 02.

Nucleotide-free structures of KIF20A illuminate atypical mechanochemistry in this kinesin-6.

Autor: Ranaivoson FM; Structural Motility, CNRS UMR144, Institut Curie, Université Paris Sciences et Lettres, Sorbonne Université, 75248 Paris, France., Crozet V; Structural Motility, CNRS UMR144, Institut Curie, Université Paris Sciences et Lettres, Sorbonne Université, 75248 Paris, France., Benoit MPMH; Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, USA., Abdalla Mohammed Khalid A; Third Institute of Physics-Biophysics, Georg August University Göttingen, 37077 Göttingen, Germany., Kikuti C; Structural Motility, CNRS UMR144, Institut Curie, Université Paris Sciences et Lettres, Sorbonne Université, 75248 Paris, France., Sirkia H; Structural Motility, CNRS UMR144, Institut Curie, Université Paris Sciences et Lettres, Sorbonne Université, 75248 Paris, France., El Marjou A; Structural Motility, CNRS UMR144, Institut Curie, Université Paris Sciences et Lettres, Sorbonne Université, 75248 Paris, France., Miserey-Lenkei S; Structural Motility, CNRS UMR144, Institut Curie, Université Paris Sciences et Lettres, Sorbonne Université, 75248 Paris, France., Asenjo AB; Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, USA., Sosa H; Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, USA., Schmidt CF; Third Institute of Physics-Biophysics, Georg August University Göttingen, 37077 Göttingen, Germany.; Department of Physics and Soft Matter Center, Duke University, Durham, NC 27708, USA., Rosenfeld SS; Department of Pharmacology, Mayo Clinic, Jacksonville, FL 32224, USA., Houdusse A; Structural Motility, CNRS UMR144, Institut Curie, Université Paris Sciences et Lettres, Sorbonne Université, 75248 Paris, France.

Publikováno v: Open biology [Open Biol] 2023 Sep; Vol. 13 (9), pp. 230122. Date of Electronic Publication: 2023 Sep 20.

Kinesin-8-specific loop-2 controls the dual activities of the motor domain according to tubulin protofilament shape.

Autor: Hunter B; Department of Biomedical and Molecular Sciences, Queen's University, Kingston, ON, K7L 3N6, Canada., Benoit MPMH; Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY, 10461, USA., Asenjo AB; Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY, 10461, USA., Doubleday C; Department of Biomedical and Molecular Sciences, Queen's University, Kingston, ON, K7L 3N6, Canada., Trofimova D; Department of Biomedical and Molecular Sciences, Queen's University, Kingston, ON, K7L 3N6, Canada., Frazer C; Department of Molecular Microbiology and Immunology, Brown University, Providence, RI, 02912, USA., Shoukat I; Department of Biomedical and Molecular Sciences, Queen's University, Kingston, ON, K7L 3N6, Canada., Sosa H; Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY, 10461, USA. hernando.sosa@einsteinmed.edu., Allingham JS; Department of Biomedical and Molecular Sciences, Queen's University, Kingston, ON, K7L 3N6, Canada. allinghj@queensu.ca.

Publikováno v: Nature communications [Nat Commun] 2022 Jul 20; Vol. 13 (1), pp. 4198. Date of Electronic Publication: 2022 Jul 20.

Author Correction: Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s.

Autor: Benoit MPMH; Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY, 10461, USA., Asenjo AB; Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY, 10461, USA., Sosa H; Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY, 10461, USA. hernando.sosa@einstein.yu.edu.

Publikováno v: Nature communications [Nat Commun] 2018 Jul 11; Vol. 9 (1), pp. 2748. Date of Electronic Publication: 2018 Jul 11.

Use of Single Molecule Fluorescence Polarization Microscopy to Study Protein Conformation and Dynamics of Kinesin-Microtubule Complexes.

Autor: Benoit MPMH; Department of Physiology and Biophysics, Albert Einstein College of Medicine, Jack and Pearl Resnick Campus, 1300 Morris Park Avenue, Bronx, NY, 10461, USA., Sosa H; Department of Physiology and Biophysics, Albert Einstein College of Medicine, Jack and Pearl Resnick Campus, 1300 Morris Park Avenue, Bronx, NY, 10461, USA. hernando.sosa@einstein.yu.edu.

Publikováno v: Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2018; Vol. 1665, pp. 199-216.