J. Chalovich

发表

A long helix from the central region of smooth muscle caldesmon.

P. Graceffa, W. Stafford, K. Mabuchi, 1991, The Journal of biological chemistry.

Synaptopodin family of natively unfolded, actin binding proteins: physical properties and potential biological functions

J. Chalovich, M. Schroeter, 2010, Biophysical Reviews.

The actin binding protein, fesselin, is a member of the synaptopodin family.

H. Heid, J. Chalovich, M. Schroeter, 2008, Biochemical and biophysical research communications.

In vitro characterization of native mammalian smooth-muscle protein synaptopodin 2.

H. Heid, J. Chalovich, M. Schroeter, 2008, Bioscience reports.

Localization of the actin-binding protein fesselin in chicken smooth muscle

J. Chalovich, R. Renegar, M. Schroeter, 2009, Histochemistry and Cell Biology.

Equilibrium distribution of skeletal actin–tropomyosin–troponin states, determined by pyrene–tropomyosin fluorescence

J. Chalovich, B. Gafurov, 2007, The FEBS journal.

Regulation of striated muscle contraction: a discussion

J. Chalovich, 2004, Journal of Muscle Research & Cell Motility.

Response to the Letter by Geeves and Lehrer

B. Brenner, Yi-der Chen, B. Yan, 2002 .

Theoretical kinetic studies of models for binding myosin subfragment-1 to regulated actin: Hill model versus Geeves model.

B. Brenner, B. Yan, J. Chalovich, 2001, Biophysical journal.

Caldesmon reduces the apparent rate of binding of myosin S1 to actin-tropomyosin.

B. Yan, J. Chalovich, Y. Chen, 2001, Biochemistry.

Cycling Cross-Bridges Contribute to Thin Filament Activation in Human Slow-Twitch Fibers

B. Brenner, Anna Á. Rauscher, A. Málnási-Csizmadia, 2020, Frontiers in Physiology.

Effect of caldesmon on the ATPase activity and the binding of smooth and skeletal myosin subfragments to actin.

J. Chalovich, M. Hemric, 1988, The Journal of biological chemistry.

The Delta 14 mutation of human cardiac troponin T enhances ATPase activity and alters the cooperative binding of S1-ADP to regulated actin.

P. Chase, B. Brenner, J. Chalovich, 2004, Biochemistry.

Inhibition of Contraction and Myosin Light Chain Phosphorylation in Guinea‐Pig Smooth Muscle by p21‐Activated Kinase 1

E. Manser, G. Pfitzer, J. Chalovich, 2003, The Journal of physiology.

Natural abundance 13C NMR spectra of intact muscle

M. Bárány, J. Chalovich, D. Doyle, 1981, FEBS letters.

Caldesmon and a 20-kDa actin-binding fragment of caldesmon inhibit tension development in skinned gizzard muscle fiber bundles.

G. Pfitzer, J. Chalovich, C. Zeugner, 1993, Proceedings of the National Academy of Sciences of the United States of America.

Caldesmon ablation in mice causes umbilical herniation and alters contractility of fetal urinary bladder smooth muscle

J. Hescheler, G. Pfitzer, M. Koch, 2021, The Journal of general physiology.

Adenosine 5'-(gamma-thiotriphosphate): an ATP analog that should be used with caution in muscle contraction studies.

J. Chalovich, A. Resetar, 1995, Biochemistry.

A computational and experimental approach to investigate bepridil binding with cardiac troponin.

J. Chalovich, Yumin Li, Jayson F. Varughese, 2011, The journal of physical chemistry. B.

Disease causing mutations of troponin alter regulated actin state distributions

J. Chalovich, 2012, Journal of Muscle Research and Cell Motility.

Negative charges at protein kinase C sites of troponin I stabilize the inactive state of actin.

J. Chalovich, Tomoyoshi Kobayashi, Mohit C. Mathur, 2008, Biophysical journal.

Troponin C Mutations Partially Stabilize the Active State of Regulated Actin and Fully Stabilize the Active State When Paired with Δ14 TnT.

J. Chalovich, J. Pinto, Dylan Johnson, 2017, Biochemistry.

Interaction of isozymes of myosin subfragment 1 with actin: effect of ionic strength and nucleotide.

E. Eisenberg, L. Greene, J. Chalovich, 1984, Biochemistry.

Hypertrophic Cardiomyopathy Mutations of Troponin Reveal Details of Striated Muscle Regulation

J. Chalovich, D. Johnson, L. Zhu, 2022, Frontiers in Physiology.

Identification of an unknown 31P nuclear magnetic resonance from dystrophic chicken as L-serine ethanolamine phosphodiester.

M. Bárány, S. Cohen, T. Glonek, 1977, Archives of biochemistry and biophysics.

PHOSPHORUS NUCLEAR MAGNETIC RESONANCE OF DISEASED MUSCLE

M. Bárány, C. Burt, J. Chalovich, 1978 .

Calponin interaction with alpha-actinin-actin: evidence for a structural role for calponin.

W. Stafford, J. X. Tang, J. Chalovich, 1999, Biophysical journal.

Caldesmon inhibits skeletal actomyosin subfragment-1 ATPase activity and the binding of myosin subfragment-1 to actin.

J. Chalovich, C. Benson, P. Cornelius, 1987, The Journal of biological chemistry.

Inhibition of cross-bridge binding to actin by caldesmon fragments in skinned skeletal muscle fibers.

B. Brenner, R. Hartwell, J. Chalovich, 1997, Biophysical journal.

Smooth muscle α-actinin binds tightly to fesselin and attenuates its activity toward actin polymerization

J. Chalovich, Minh Pham, 2006, Journal of Muscle Research & Cell Motility.

Fesselin binds to actin and myosin and inhibits actin-activated ATPase activity

J. Chalovich, M. Schroeter, 2005, Journal of Muscle Research & Cell Motility.

Caldesmon: binding to actin and myosin and effects on elementary steps in the ATPase cycle.

J. Chalovich, B. Leinweber, Y. Chen, 1998, Acta physiologica Scandinavica.

Serine ethanolamine phosphodiester: a major component in chicken semen.

C. Burt, J. Chalovich, 1978, Biochimica et biophysica acta.

A mosaic multiple-binding model for the binding of caldesmon and myosin subfragment-1 to actin.

J. Chalovich, Y. Chen, 1992, Biophysical journal.

Parallel inhibition of active force and relaxed fiber stiffness in skeletal muscle by caldesmon: implications for the pathway to force generation.

B. Brenner, J. Chalovich, L. Yu, 1991, Proceedings of the National Academy of Sciences of the United States of America.

The binding of caldesmon to actin and its effect on the ATPase activity of soluble myosin subfragments in the presence and absence of tropomyosin.

J. Chalovich, C. Benson, M. Hemric, 1989, The Journal of biological chemistry.

Actin mediated regulation of muscle contraction.

J. Chalovich, 1992, Pharmacology & therapeutics.

Equilibrium binding of proteins to F-actin.

J. Chalovich, 2007, Methods in molecular biology.

Troponin-tropomyosin: an allosteric switch or a steric blocker?

J. Stephens, J. Chalovich, A. Resetar, 2002, Biophysical journal.

Characterization of a caldesmon fragment that competes with myosin-ATP binding to actin.

J. Chalovich, Y. Chen, L. Velaz, 1993, Biophysical journal.

Characterization of caldesmon binding to myosin.

J. Chalovich, M. Hemric, 1990, The Journal of biological chemistry.

Immunochemical evidence for the binding of caldesmon to the NH2-terminal segment of actin.

G. Dasgupta, S. Adams, E. Reisler, 1990, The Journal of biological chemistry.

Dissociation of the effect of caldesmon on the ATPase activity and on the binding of smooth heavy meromyosin to actin by partial digestion of caldesmon.

R. Ingraham, J. Chalovich, L. Velaz, 1990, The Journal of biological chemistry.

Crosslinked myosin subfragment 1: a stable analogue of the subfragment-1.ATP complex.

E. Eisenberg, L. Greene, J. Chalovich, 1983, Proceedings of the National Academy of Sciences of the United States of America.

Inhibition of actomyosin ATPase activity by troponin-tropomyosin without blocking the binding of myosin to actin.

E. Eisenberg, J. Chalovich, 1982, The Journal of biological chemistry.

Acrylodan-labeled smooth muscle tropomyosin reports differences in the effects of troponin and caldesmon in the transition from the active state to the inactive state.

J. Chalovich, M. Schroeter, Evan A. Lutz, 2011, Biochemistry.

Acrylodan smooth muscle tropomyosin reports differences in effects of troponin and caldesmon in the transition from the active state to the inactive state

J. Chalovich, M. Schroeter, Evan A. Lutz, 2011 .

Involvement of weak binding crossbridges in force production in muscle

B. Brenner, Leepo C. Yu, J. Chalovich, 1991, Journal of Muscle Research & Cell Motility.

Sarcomeric binding pattern of exogenously added intact caldesmon and its C-terminal 20-kDa fragment in skinned fibers of skeletal muscle

M. Reedy, B. Brenner, J. Chalovich, 1999, Journal of Muscle Research & Cell Motility.

Flexation of caldesmon: effect of conformation on the properties of caldesmon

E. Reisler, J. Chalovich, R. Crosbie, 1995, Journal of Muscle Research & Cell Motility.

Radial equilibrium lengths of actomyosin cross-bridges in muscle.

B. Brenner, J. Chalovich, L. Yu, 1996, Biophysical journal.

Role of ATP in the binding of caldesmon to smooth muscle myosin.

J. Chalovich, F. Lu, 1995, Biochemistry.

Caldesmon, N-terminal yeast actin mutants, and the regulation of actomyosin interactions.

E. Reisler, P. Rubenstein, J. Chalovich, 1994, Biochemistry.

Caldesmon Derived Polypeptides as Probes of Force Production in Skeletal Muscle

B. Brenner, Leepo C. Yu, J. Chalovich, 1991 .

Caldesmon and thin-filament regulation of muscle contraction

J. Chalovich, 2008, Cell Biophysics.

Interaction of caldesmon and myosin subfragment 1 with the C-terminus of actin.

E. Reisler, J. Chalovich, R. Crosbie, 1992, Biochemical and biophysical research communications.

Characterization of calponin binding to actin.

J. Chalovich, M. Freedman, F. Lu, 1995, Biochemistry.

The Positively Charged C-Terminal Region of Human Skeletal Troponin T Retards Activation and Decreases Calcium Sensitivity.

J. Chalovich, T. Kraft, Li Zhu, 2020, Biochemistry.

Stepwise C-Terminal Truncation of Cardiac Troponin T Alters Function at Low and Saturating Ca2+

W. Angus, J. Chalovich, D. Johnson, 2018, bioRxiv.

The C-terminus of troponin T is essential for maintaining the inactive state of regulated actin.

A. Franklin, J. Chalovich, Tomoyoshi Kobayashi, 2012, Biophysical journal.

Basic residues within the cardiac troponin T C terminus are required for full inhibition of muscle contraction and limit activation by calcium

J. Chalovich, Maicon Landim-Vieira, J. Pinto, 2019, The Journal of Biological Chemistry.

C-Terminal Basic Region of Troponin T Alters the Ca2+-Dependent Changes in Troponin I Interactions.

J. Chalovich, Li Zhu, Dylan Johnson, 2022, Biochemistry.

Commentary: Effect of Skeletal Muscle Native Tropomyosin on the Interaction of Amoeba Actin with Heavy Meromyosin

J. Chalovich, Dylan Johnson, 2016, Front. Physiol..

Kinetics of regulated actin transitions measured by probes on tropomyosin.

J. Chalovich, E. Borrego-Diaz, 2010, Biophysical journal.

Some cardiomyopathy-causing troponin I mutations stabilize a functional intermediate actin state.

J. Chalovich, Tomoyoshi Kobayashi, Mohit C. Mathur, 2009, Biophysical journal.

Evidence for cross-bridge attachment in relaxed muscle at low ionic strength.

E. Eisenberg, B. Brenner, L. Greene, 1982, Proceedings of the National Academy of Sciences of the United States of America.

Mechanism of action of troponin . tropomyosin. Inhibition of actomyosin ATPase activity without inhibition of myosin binding to actin.

E. Eisenberg, J M Chalovich, E Eisenberg, 1981, The Journal of biological chemistry.

Fesselin: a novel synaptopodin-like actin binding protein from muscle tissue

J. Chalovich, D. Hoffman, B. Leinweber, 1999, Journal of Muscle Research & Cell Motility.

Several cardiomyopathy causing mutations on tropomyosin either destabilize the active state of actomyosin or alter the binding properties of tropomyosin.

P. Chase, J. Chalovich, Mohit C. Mathur, 2011, Biochemical and biophysical research communications.

Kinetics of thin filament activation probed by fluorescence of N-((2-(iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2-oxa-1,3-diazole-labeled troponin I incorporated into skinned fibers of rabbit psoas muscle: implications for regulation of muscle contraction.

B. Brenner, J. Chalovich, 1999, Biophysical journal.

The Cardiomyopathy Mutation, R146G Troponin I, Stabilizes the Intermediate "C" State of Regulated Actin under High- and Low-Free Ca(2+) Conditions.

J. Chalovich, Tomoyoshi Kobayashi, Dylan Johnson, 2016, Biochemistry.

Structure of the shutdown state of myosin-2

N. Ranson, C. Scarff, P. Knight, 2020, Nature.

Tropomyosin dynamics in cardiac thin filaments: a multisite forster resonance energy transfer and anisotropy study.

G. Marriott, Hui Wang, J. Chalovich, 2008, Biophysical journal.

Factors Contributing to Troponin Exchange in Myofibrils and in Solution

Leepo C. Yu, J. Chalovich, M. She, 2004, Journal of Muscle Research & Cell Motility.

Eliminating the First Inactive State and Stabilizing the Active State of the Cardiac Regulatory System Alters Behavior in Solution and in Ordered Systems.

J. M. Robinson, J. Chalovich, Maicon Landim-Vieira, 2020, Biochemistry.

Structural Dynamics of Troponin I during Ca2+-Activation of Cardiac Thin Filaments: A Multi-Site Förster Resonance Energy Transfer Study

G. Marriott, Hui Wang, J. Chalovich, 2012, PloS one.

Disease causing mutations of troponin alter regulated actin state distributions

J. Chalovich, 2012, Journal of Muscle Research and Cell Motility.

Molecular Dynamics Studies on Troponin (Tnl-TnT-TnC) Complexes: Insight into the Regulation of Muscle Contraction

J. Chalovich, Jayson F. Varughese, Y. Lit, 2010, Journal of biomolecular structure & dynamics.

Parallel inhibition of active force and relaxed fiber stiffness by caldesmon fragments at physiological ionic strength and temperature conditions: additional evidence that weak cross-bridge binding to actin is an essential intermediate for force generation.

B. Brenner, J. Chalovich, T. Kraft, 1995, Biophysical journal.

Theoretical models for cooperative steady-state ATPase activity of myosin subfragment-1 on regulated actin.

T. L. Hill, E. Eisenberg, T L Hill, 1981, Biophysical journal.

Avian synaptopodin 2 (fesselin) stabilizes myosin filaments and actomyosin in the presence of ATP.

J. Chalovich, R. Renegar, N. L. Kingsbury, 2013, Biochemistry.

Ca2+ and ionic strength dependencies of S1-ADP binding to actin-tropomyosin-troponin: regulatory implications.

Yi-der Chen, J. Chalovich, B. Gafurov, 2004, Biophysical journal.

Cross-bridge attachment in relaxed muscle.

E. Eisenberg, B. Brenner, L. Greene, 1984, Advances in experimental medicine and biology.

Conservation of the regulated structure of folded myosin 2 in species separated by at least 600 million years of independent evolution

S. Burgess, P. Knight, H. Jung, 2008, Proceedings of the National Academy of Sciences.

Structure of the shutdown state of myosin-2

N. Ranson, C. Scarff, P. Knight, 2020, Nature.

Thermodynamics and molecular dynamics simulations of calcium binding to the regulatory site of human cardiac troponin C: evidence for communication with the structural calcium binding sites

A. Spuches, J. Chalovich, Yumin Li, 2012, JBIC Journal of Biological Inorganic Chemistry.

X-ray diffraction studies of the cross-bridge intermediate states.

B. Brenner, G. Rapp, J. Chalovich, 1998, Advances in experimental medicine and biology.

Purification and Partial Characterization of Relaxin and Relaxin Precursors from the Hamster Placenta 1

J. Chalovich, R. Renegar, C. R. Owens, 2008 .

Purification and partial characterization of relaxin and relaxin precursors from the hamster placenta.

J. Chalovich, R. Renegar, C. R. Owens, 1993, Biology of reproduction.

Distinct molecular processes associated with isometric force generation and rapid tension recovery after quick release.

B. Brenner, J. Chalovich, L. Yu, 1995, Biophysical journal.

Effect of nucleotide on the binding of N,N'-p-phenylenedimaleimide-modified S-1 to unregulated and regulated actin.

E. Eisenberg, L. Greene, J. Chalovich, 1986, Biochemistry.

Serine ethanolamine phosphate in avian muscular dystrophy: mechanism of accumulation in dystrophic muscle and relationship to phospholipid synthesis.

M. Bárány, J. Chalovich, M. Bárány, 1980, Archives of biochemistry and biophysics.

Michael Bárány: a recollection

J. Chalovich, 2012, Journal of Muscle Research and Cell Motility.

PHOSPHODIESTERS IN MUSCULAR DYSTROPHIES *

M. Bárány, T. Glonek, C. Burt, 1979, Annals of the New York Academy of Sciences.

Structures of smooth muscle myosin and heavy meromyosin in the folded, shutdown state.

Matt L. Walker, S. Burgess, P. Knight, 2007, Journal of molecular biology.

Calpain inhibition rescues troponin T3 fragmentation, increases Cav1.1, and enhances skeletal muscle force in aging sedentary mice

L. Purcell, M. Messi, Tan Zhang, 2016, Aging cell.

The effect of troponin-tropomyosin on the binding of heavy meromyosin to actin in the presence of ATP.

E. Eisenberg, J M Chalovich, E Eisenberg, 1986, The Journal of biological chemistry.

Dual thick and thin filament linked regulation of stretch- and L-NAME-induced tone in young and senescent murine basilar artery

J. Hescheler, N. Smyth, G. Pfitzer, 2023, Frontiers in Physiology.

Modulation of cross-bridge affinity for MgGTP by Ca2+ in skinned fibers of rabbit psoas muscle.

B. Brenner, J. Chalovich, L. Yu, 1997, Biophysical journal.

Characterizations of cross-bridges in the presence of saturating concentrations of MgAMP-PNP in rabbit permeabilized psoas muscle.

J. Chalovich, L. Yu, S. Xu, 1998, Biophysical journal.

Crosslinking of actin filaments and inhibition of actomyosin subfragment-1 ATPase activity by streptococcal M6 protein.

V. Fischetti, J. Chalovich, 1986, Archives of biochemistry and biophysics.

Role of the tail in the regulated state of myosin 2.

K. Thirumurugan, P. Knight, H. Jung, 2011, Journal of molecular biology.

Fesselin is a natively unfolded protein.

J. Kenney, J. Chalovich, M. Schroeter, 2007, Journal of proteome research.

Fesselin, a synaptopodin-like protein, stimulates actin nucleation and polymerization.

J. Chalovich, B. Beall, 2001, Biochemistry.

Kinetics of Binding of Caldesmon to Actin (*)

Yi-der Chen, J. Chalovich, Joseph M. Chalovich, 1995, The Journal of Biological Chemistry.

Phosphorylation-contraction coupling in smooth muscle: role of caldesmon.

G. Pfitzer, J. Chalovich, W. Fischer, 1993, Advances in experimental medicine and biology.

Stiffness of skinned rabbit psoas fibers in MgATP and MgPPi solution.

E. Eisenberg, B. Brenner, L. Greene, 1986, Biophysical journal.

Influence of ionic strength, actin state, and caldesmon construct size on the number of actin monomers in a caldesmon binding site.

J. Chalovich, B. Gafurov, S. Fredricksen, 2003, Biochemistry.

Phosphorylation of caldesmon at sites between residues 627 and 642 attenuates inhibitory activity and contributes to a reduction in Ca2+-calmodulin affinity.

J. Chalovich, M. Schroeter, Svetlana S. Hamden, 2010, Biophysical journal.

Thin filament activation probed by fluorescence of N-((2-(iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2-oxa-1,3-diazole-labeled troponin I incorporated into skinned fibers of rabbit psoas muscle.

B. Brenner, J. Chalovich, T. Kraft, 1999, Biophysical journal.

Organization of F-actin by Fesselin (avian smooth muscle synaptopodin 2).

E. Egelman, A. Orlova, J. Chalovich, 2013, Biochemistry.

Negative Charges Introduced Near the IT Helix of Cardiac Troponin T Stabilize the Active State of Actin Filaments.

J. Chalovich, Maicon Landim-Vieira, J. Pinto, 2023, Biochemistry.

Organization of F-actin by Fesselin (avian smooth muscle synaptopodin 2).

E. Egelman, A. Orlova, J. Chalovich, 2013, Biochemistry.