Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Patti L. Engel"'
Autor:
Jack Chang, Gwendolyn M. Pais, Patti L. Engel, Patryk Klimek, Sylwia Marianski, Kimberly Valdez, Marc H. Scheetz
Vancomycin induced kidney injury is common, and outcomes in humans are well predicted by animal models. This study employed our translational rat model to investigate temporal changes in glomerular filtration rate (GFR) and correlation with kidney in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a366b6b9ce624a3c97cd597c5687f2ac
https://doi.org/10.1101/2022.09.26.509628
https://doi.org/10.1101/2022.09.26.509628
Autor:
Steven C. Wu, R. John Solaro, Svetlana B. Tikunova, Brandon J. Biesiadecki, Patti L. Engel, Tomoyoshi Kobayashi, Jonathan P. Davis
Publikováno v:
Journal of Biological Chemistry. 282:183-193
Force generating strong cross-bridges are required to fully activate cardiac thin filaments, but the molecular signaling mechanism remains unclear. Evidence demonstrating differential extents of cross-bridge-dependent activation of force, especially
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee559b085aa7ccddf2deddcfa5360b4b
https://doi.org/10.1074/jbc.m512337200
https://doi.org/10.1074/jbc.m512337200
Autor:
James D. Potter, Gayathri Venkatraman, R. John Solaro, Aldrin V. Gomes, Svetlana B. Tikunova, Patti L. Engel, Jonathan P. Davis
Publikováno v:
Journal of Biological Chemistry. 279:49579-49587
In this study we investigated the physiological role of the cardiac troponin T (cTnT) isoforms in the presence of human slow skeletal troponin I (ssTnI). ssTnI is the main troponin I isoform in the fetal human heart. In reconstituted fibers containin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::62a6ad9189d22a3b0fbf615808b513f0
https://doi.org/10.1074/jbc.m407340200
https://doi.org/10.1074/jbc.m407340200
Autor:
Jeffery D. Molkentin, Beata M. Wolska, Hajer N. Sheikh, R. John Solaro, Jo El J. Schultz, Patti L. Engel, Emily M. Schulz, Marcos S. Lofrano-Alves, David F. Wieczorek, Gilbert Newman, Richard N.. Correll
Phosphorylation of tropomyosin (Tm) has been shown to vary in mouse models of cardiac hypertrophy. Little is known about the in vivo role of Tm phosphorylation. This study examines the consequences of Tm dephosphorylation in the murine heart. Transge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01fc234909cc67c98c82124938f2fdc8
https://europepmc.org/articles/PMC3531761/
https://europepmc.org/articles/PMC3531761/
Ischemia and heart failure are associated with protein kinase C (PKC) dependent phosphorylation of cardiac troponin I (cTnI). We investigated the effect of phosphorylation of cTnI PKC sites S43, S45 and T144 under normal (pH 7.0) and acidic (pH 6.5)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3860f09ca2cd87364e8339e00d0dab5b
https://europepmc.org/articles/PMC2716429/
https://europepmc.org/articles/PMC2716429/
Autor:
Agnieszka Galinska-Rakoczy, Roger Craig, Chen Xu, Larry S. Tobacman, Hyun Suk Jung, William Lehman, Patti L. Engel
Publikováno v:
Journal of molecular biology. 379(5)
The molecular switching mechanism governing skeletal and cardiac muscle contraction couples the binding of Ca2+ on troponin to the movement of tropomyosin on actin filaments. Despite years of investigation, this mechanism remains unclear because it h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5204449043a0ae513fb39f302d7e8efa
https://pubmed.ncbi.nlm.nih.gov/18514658
https://pubmed.ncbi.nlm.nih.gov/18514658