Sanford I Bernstein
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Explore the profile of Sanford I Bernstein including associated specialties, affiliations and a list of published articles.
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69
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1134
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Recent Articles
1.
Bell K, Brown A, Van Houten S, Blice-Baum A, Kronert W, Loya A, et al.
Biophys J
. 2025 Jan;
124(4):651-666.
PMID: 39799399
Stretch activation (SA), a delayed increase in force production after rapid muscle lengthening, is critical to the function of vertebrate cardiac muscle and insect asynchronous indirect flight muscle. SA enables...
2.
Viswanathan M, Dutta D, Kronert W, Chitre K, Padron R, Craig R, et al.
Genetics
. 2024 Nov;
229(1):1-34.
PMID: 39485824
Myosin storage myopathy (MSM) is a rare skeletal muscle disorder caused by mutations in the slow muscle/β-cardiac myosin heavy chain (MHC) gene. MSM missense mutations frequently disrupt the tail's stabilizing...
3.
Neal C, Kronert W, Camillo J, Suggs J, Huxford T, Bernstein S
Aging Cell
. 2024 Mar;
23(6):e14134.
PMID: 38506610
The molecular motor myosin is post-translationally modified in its globular head, its S2 hinge, and its thick filament domain during human skeletal muscle aging. To determine the importance of such...
4.
Kronert W, Hsu K, Madan A, Sarsoza F, Cammarato A, Bernstein S
Biology (Basel)
. 2022 Aug;
11(8).
PMID: 36009764
The R249Q mutation in human β-cardiac myosin results in hypertrophic cardiomyopathy. We previously showed that inserting this mutation into indirect flight muscle myosin yields mechanical and locomotory defects. Here, we...
5.
Trujillo A, Hsu K, Viswanathan M, Cammarato A, Bernstein S
Int J Mol Sci
. 2022 Mar;
23(5).
PMID: 35269675
The myosin molecular motor interacts with actin filaments in an ATP-dependent manner to yield muscle contraction. Myosin heavy chain residue R369 is located within loop 4 at the actin-tropomyosin interface...
6.
Trujillo A, Hsu K, Puthawala J, Viswanathan M, Loya A, Irving T, et al.
Mol Biol Cell
. 2021 Jun;
32(18):1690-1706.
PMID: 34081531
Dilated cardiomyopathy (DCM), a life-threatening disease characterized by pathological heart enlargement, can be caused by myosin mutations that reduce contractile function. To better define the mechanistic basis of this disease,...
7.
Prolonged myosin binding increases muscle stiffness in Drosophila models of Freeman-Sheldon syndrome
Bell K, Huang A, Kronert W, Bernstein S, Swank D
Biophys J
. 2021 Feb;
120(5):844-854.
PMID: 33524372
Freeman-Sheldon syndrome (FSS) is characterized by congenital contractures resulting from dominant point mutations in the embryonic isoform of muscle myosin. To investigate its disease mechanism, we used Drosophila models expressing...
8.
Bloemink M, Hsu K, Geeves M, Bernstein S
J Biol Chem
. 2020 Aug;
295(42):14522-14535.
PMID: 32817166
We investigated the biochemical and biophysical properties of one of the four alternative exon-encoded regions within the myosin catalytic domain. This region is encoded by alternative exons 3a and 3b...
9.
Guo Y, Kronert W, Hsu K, Huang A, Sarsoza F, Bell K, et al.
Skelet Muscle
. 2020 Aug;
10(1):24.
PMID: 32799913
Background: Distal arthrogryposis (DA) is a group of autosomal dominant skeletal muscle diseases characterized by congenital contractures of distal limb joints. The most common cause of DA is a mutation...
10.
Caldwell J, Mermelstein D, Walker R, Bernstein S, Huxford T
J Mol Biol
. 2019 Dec;
432(2):427-447.
PMID: 31786266
Drosophila melanogaster is a powerful system for characterizing alternative myosin isoforms and modeling muscle diseases, but high-resolution structures of fruit fly contractile proteins have not been determined. Here we report...