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Robert W. Kensler

Faculty RankProfessor
InstitutionUniversity of Puerto Rico
DepartmentSchool of Medicine
AddressUPR-Medical Sciences Campus, School of Medicine
San Juan PR 936
Phone7877582525, x1507
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    In my laboratory, the primary research objective is to elucidate the structure of the myosin-containing thick filaments found in striated muscles. The goal of the work is to understand how differences in the packing of myosin and accessory proteins in thick filaments from different muscles may relate to differences in the physiological properties of the muscles and to understand the mechanism of force production at the molecular level. The key principle guiding much of the work is the observation from X-ray diffraction studies that the heads of the myosin molecules on the filament in living muscle are helically arranged. We have been one of the pioneering laboratories in the development of procedures which allow filaments from some muscles to be biochemically isolated with the helical arrangements of heads largely preserves, thus making the structure of the filaments amenable to analysis by a combination of electron microscopy with computer image analysis of the electron micrographs. This approach utilizes the principles of helical diffraction and computer image analysis of helical structures to determine the helical parameters and to compute a three-dimensional reconstruction of the electro density of the proteins in the thick filament.

    Using this approach we have computed three-dimensional reconstructions both of several invertebrate (horseshoe crab and scorpion) and vertebrate (frog and fish) skeletal muscle thick filaments. The primary goal of the current research is to elucidate the structure of the mammalian cardiac muscle thick filament; and to study the effects of phosphorylation of myosin light chain and other thick filaments accessory proteins on the structure of the thick filaments and their interactions with actin to produce contraction. Determination of the structure of the cardiac thick filament as compared to the skeletal muscle thick filament is important for understanding the differences in physiological properties of cardiac muscle and skeletal muscle.

    The techniques employed in the laboratory include electron microscopy (negative staining and platinum shadowing), computer image analysis both Fourier analysis and single particle analysis, cell fractionation, centrifugation, and SDS gel electrophoresis. Training opportunities are available for graduate students, undergraduates, and medical students.

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    Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Faculty can login to make corrections and additions.
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    PMC Citations indicate the number of times the publication was cited by articles in PubMed Central, and the Altmetric score represents citations in news articles and social media. (Note that publications are often cited in additional ways that are not shown here.) Fields are based on how the National Library of Medicine (NLM) classifies the publication's journal and might not represent the specific topic of the publication. Translation tags are based on the publication type and the MeSH terms NLM assigns to the publication. Some publications (especially newer ones and publications not in PubMed) might not yet be assigned Field or Translation tags.) Click a Field or Translation tag to filter the publications.
    1. Kensler RW, Craig R, Moss RL. Phosphorylation of cardiac myosin binding protein C releases myosin heads from the surface of cardiac thick filaments. Proc Natl Acad Sci U S A. 2017 02 21; 114(8):E1355-E1364. PMID: 28167762.
      Citations: 21     Fields:    Translation:AnimalsCells
    2. Mun JY, Kensler RW, Harris SP, Craig R. The cMyBP-C HCM variant L348P enhances thin filament activation through an increased shift in tropomyosin position. J Mol Cell Cardiol. 2016 Feb; 91:141-7. PMID: 26718724.
      Citations: 6     Fields:    Translation:HumansAnimalsCells
    3. González-Solá M, Al-Khayat HA, Behra M, Kensler RW. Zebrafish cardiac muscle thick filaments: isolation technique and three-dimensional structure. Biophys J. 2014 Apr 15; 106(8):1671-80. PMID: 24739166.
      Citations: 14     Fields:    Translation:Animals
    4. Al-Khayat HA, Kensler RW, Squire JM, Marston SB, Morris EP. Atomic model of the human cardiac muscle myosin filament. Proc Natl Acad Sci U S A. 2013 Jan 02; 110(1):318-23. PMID: 23251030.
      Citations: 61     Fields:    Translation:HumansCells
    5. Kensler RW, Shaffer JF, Harris SP. Binding of the N-terminal fragment C0-C2 of cardiac MyBP-C to cardiac F-actin. J Struct Biol. 2011 Apr; 174(1):44-51. PMID: 21163356.
      Citations: 47     Fields:    Translation:AnimalsCells
    6. Al-Khayat HA, Kensler RW, Morris EP, Squire JM. Three-dimensional structure of the M-region (bare zone) of vertebrate striated muscle myosin filaments by single-particle analysis. J Mol Biol. 2010 Nov 12; 403(5):763-76. PMID: 20851129.
      Citations: 13     Fields:    Translation:AnimalsCells
    7. Paul DM, Morris EP, Kensler RW, Squire JM. Structure and orientation of troponin in the thin filament. J Biol Chem. 2009 May 29; 284(22):15007-15. PMID: 19321455.
      Citations: 18     Fields:    Translation:AnimalsCells
    8. Shaffer JF, Kensler RW, Harris SP. The myosin-binding protein C motif binds to F-actin in a phosphorylation-sensitive manner. J Biol Chem. 2009 May 01; 284(18):12318-27. PMID: 19269976.
      Citations: 109     Fields:    Translation:AnimalsCells
    9. Al-Khayat HA, Morris EP, Kensler RW, Squire JM. Myosin filament 3D structure in mammalian cardiac muscle. J Struct Biol. 2008 Aug; 163(2):117-26. PMID: 18472277.
      Citations: 18     Fields:    Translation:AnimalsCells
    10. Kensler RW, Harris SP. The structure of isolated cardiac Myosin thick filaments from cardiac Myosin binding protein-C knockout mice. Biophys J. 2008 Mar 01; 94(5):1707-18. PMID: 17993479.
      Citations: 21     Fields:    Translation:AnimalsCells
    11. Al-Khayat HA, Morris EP, Kensler RW, Squire JM. 3D structure of relaxed fish muscle myosin filaments by single particle analysis. J Struct Biol. 2006 Aug; 155(2):202-17. PMID: 16731006.
      Citations: 18     Fields:    Translation:AnimalsCells
    12. Kensler RW. The mammalian cardiac muscle thick filament: backbone contributions to meridional reflections. J Struct Biol. 2005 Mar; 149(3):313-24. PMID: 15721585.
      Citations: 8     Fields:    Translation:AnimalsCells
    13. Kensler RW. The mammalian cardiac muscle thick filament: crossbridge arrangement. J Struct Biol. 2005 Mar; 149(3):303-12. PMID: 15721584.
      Citations: 12     Fields:    Translation:AnimalsCells
    14. Kensler RW. Mammalian cardiac muscle thick filaments: their periodicity and interactions with actin. Biophys J. 2002 Mar; 82(3):1497-508. PMID: 11867464.
      Citations: 10     Fields:    Translation:AnimalsCells
    15. Eakins F, AL-Khayat HA, Kensler RW, Morris EP, Squire JM. 3D Structure of fish muscle myosin filaments. J Struct Biol. 2002 Jan-Feb; 137(1-2):154-63. PMID: 12064942.
      Citations: 9     Fields:    Translation:AnimalsCells
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