Výsledky vyhledávání - "Karoly Trombitás"

Hierarchical Extensibility in the PEVK Domain of Skeletal-Muscle Titin

Autor: Attila Nagy, Karoly Trombitás, Tamás Huber, Henk Granzier, László Grama, Miklós S.Z. Kellermayer, Pasquale Bianco

Publikováno v: Biophysical Journal. 89:329-336

Titin is the main determinant of passive muscle force. Physiological extension of titin derives largely from its PEVK (Pro-Glu-Val-Lys) domain, which has a different length in different muscle types. Here we characterized the elasticity of the full-l

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::146a01746ac98ba2ef1fcccdbddc4696
https://doi.org/10.1529/biophysj.104.057737

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Cellular and molecular mechanisms of systolic and diastolic dysfunction in an avian model of dilated cardiomyopathy

Autor: Kenneth Bell, Yiming Wu, Anthony H. Tobias, Russell L. Tucker, William T. Barry, Henk Granzier, Michiel Helmes, Karoly Trombitás, Kenneth B. Campbell

Publikováno v: Journal of Molecular and Cellular Cardiology. 37:111-119

We investigated the cellular and molecular mechanisms of systolic and diastolic dysfunction in a furazolidone (Fz)-induced model of dilated cardiomyopathy (DCM) in turkey poults. Serial echocardiograms disclosed marked systolic dysfunction in the Fz-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f21975c3fb204e638f69029854ff9f15
https://doi.org/10.1016/j.yjmcc.2004.04.010

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Changes in Titin Isoform Expression in Pacing-Induced Cardiac Failure Give Rise to Increased Passive Muscle Stiffness

Autor: Christian C. Witt, Yiming Wu, Henk Granzier, Siegfried Labeit, Karoly Trombitás, Stephen P. Bell, Martin M. LeWinter

Publikováno v: Circulation. 106:1384-1389

Background— Titin contains a molecular spring segment that underlies passive myocardial stiffness. Myocardium coexpresses titin isoforms with molecular spring length variants and, consequently, distinct stiffness characteristics: the stiff N2B isof

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ace963f0440eb1844da2df5c08c23511
https://doi.org/10.1161/01.cir.0000029804.61510.02

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Mutations of TTN, encoding the giant muscle filament titin, cause familial dilated cardiomyopathy

Autor: Jonathan G. Seidman, Henk Granzier, Christine E. Seidman, Brenda Gerull, John Atherton, Mark McNabb, Siegfried Labeit, Ludwig Thierfelder, Sabine Sasse-Klaassen, Michael Gramlich, Michael P. Frenneaux, Karoly Trombitás

Publikováno v: Nature Genetics. 30:201-204

Congestive heart failure (CHF) can result from various disease states with inadequate cardiac output. CHF due to dilated cardiomyopathy (DCM) is a familial disease in 20-30% of cases and is associated with mutations in genes encoding cytoskeletal, co

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec131cc36593625e7db55c19bf992678
https://doi.org/10.1038/ng815

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X-ray diffraction from flight muscle with a headless myosin mutation: implications for interpreting reflection patterns

Autor: Sanford I. Bernstein, Naoto Yagi, Hiroyuki Iwamoto, Karoly Trombitás, Jennifer A. Suggs

Publikováno v: Frontiers in Physiology, Vol 5 (2014)
Frontiers in Physiology

Fruit fly (Drosophila melanogaster) is one of the most useful animal models to study the causes and effects of hereditary diseases because of its rich genetic resources. It is especially suitable for studying myopathies caused by myosin mutations, be

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afc3e8f368c2aa2d750a20f313ab39d7
http://journal.frontiersin.org/Journal/10.3389/fphys.2014.00416/full

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Titin–Actin Interaction in Mouse Myocardium: Passive Tension Modulation and Its Regulation by Calcium/S100A1

Autor: Rob Yamasaki, Siegfried Labeit, M. Berri, Karoly Trombitás, Christian Witt, Yiming Wu, Miklós S.Z. Kellermayer, Marion L. Greaser, Dietmar Labeit, Mark McNabb, Henk Granzier

Publikováno v: Biophysical Journal. 81:2297-2313

Passive tension in striated muscles derives primarily from the extension of the giant protein titin. However, several studies have suggested that, in cardiac muscle, interactions between titin and actin might also contribute to passive tension. We ex

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59bb120d5e94187658fb91ef3ce8f7d8
https://doi.org/10.1016/s0006-3495(01)75876-6

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Cardiac titin isoforms are coexpressed in the half-sarcomere and extend independently

Autor: Karoly Trombitás, Henk Granzier, Dietmar Labeit, Siegfried Labeit, Yiming Wu

Publikováno v: American Journal of Physiology-Heart and Circulatory Physiology. 281:H1793-H1799

Titin, the third myofilament type of cardiac muscle, contains a molecular spring segment that gives rise to passive forces in stretched myocardium and to restoring forces in shortened myocardium. We studied cardiac titin isoforms (N2B and N2BA) that

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b4b3141fc2155321f418c577c2ccf95d
https://doi.org/10.1152/ajpheart.2001.281.4.h1793

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Myopalladin, a Novel 145-Kilodalton Sarcomeric Protein with Multiple Roles in Z-Disc and I-Band Protein Assemblies

Autor: Siegfried Labeit, Rob Yamasaki, Ryan E. Mudry, Marie Louise Bang, Henk Granzier, Adam J. Geach, Carol C. Gregorio, Hiroyuki Sorimachi, Karoly Trombitás, Abigail S. McElhinny

Publikováno v: The Journal of Cell Biology

We describe here a novel sarcomeric 145-kD protein, myopalladin, which tethers together the COOH-terminal Src homology 3 domains of nebulin and nebulette with the EF hand motifs of α-actinin in vertebrate Z-lines. Myopalladin's nebulin/nebulette and

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https://doi.org/10.1083/jcb.153.2.413

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Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain

Autor: Christian Witt, Hiroyuki Sorimachi, Siegfried Labeit, Carol C. Gregorio, Eiichi Kimura, Marie Louise Bang, Thomas Centner, Henk Granzier, Abigail S. McElhinny, Katarina Pelin, Karoly Trombitás, Junko Yano

Publikováno v: Journal of Molecular Biology. 306:717-726

The giant myofibrillar protein titin contains within its C-terminal region a serine-threonine kinase of unknown function. We have identified a novel muscle specific RING finger protein, referred to as MURF-1, that binds in vitro to the titin repeats

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ed7eceac0831d10cbb9d4cae7c49ce2
https://doi.org/10.1006/jmbi.2001.4448

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Extensibility of Isoforms of Cardiac Titin: Variation in Contour Length of Molecular Subsegments Provides a Basis for Cellular Passive Stiffness Diversity

Autor: Henk Granzier, Thomas Centner, Alka Redkar, Karoly Trombitás, Siegfried Labeit, Yiming Wu

Publikováno v: Biophysical Journal. 79:3226-3234

Titin is a giant polypeptide that spans between the Z- and M-lines of the cardiac muscle sarcomere and that develops force when extended. This force arises from titin's extensible I-band region, which consists mainly of three segment types: serially

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9705bd72e1ddd1f6ff4cc2df401154ed
https://doi.org/10.1016/s0006-3495(00)76555-6

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