Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Jeanine A. Ursitti"'
Autor:
Anicca D. Harriot, Tessa Altair Morris, Camilo Vanegas, Jacob Kallenbach, Kaylie Pinto, Humberto C. Joca, Marie-Jo Moutin, Guoli Shi, Jeanine A. Ursitti, Anna Grosberg, Christopher W. Ward
Publikováno v:
Frontiers in Cell and Developmental Biology, Vol 11 (2023)
Altered myofibrillar structure is a consequence of dystrophic pathology that impairs skeletal muscle contractile function and increases susceptibility to contraction injury. In murine Duchenne muscular dystrophy (mdx), myofibrillar alterations are ab
Externí odkaz:
https://doaj.org/article/a51700562a7c4ab8a3cb96c40aeb52a0
Publikováno v:
Pflugers Archiv : European journal of physiology. 473(4)
Alternative splicing of exon 24 (E24) of the myosin phosphatase regulatory subunit (Mypt1) tunes smooth muscle sensitivity to NO/cGMP-mediated vasorelaxation and thereby controls blood pressure (BP) in otherwise normal mice. This occurs via the toggl
Publikováno v:
European Heart Journal. 40
Background Despite the many drugs for treatment of hypertension, it remains inadequately treated in >50% of patients and the number one contributor to cardiovascular mortality world-wide. Thus new targets and treatment strategies are badly needed. My
Publikováno v:
Hypertension. 70
Myosin Phosphatase (MP) is the primary effector of vascular smooth muscle (VSM) relaxation and a key end target of signaling pathways that regulate vessel tone. Regulated splicing of alternative Exon24 (E24) of Myosin Phosphatase Regulatory/ Targetin
Autor:
Brian G. Petrich, Xin Ye, William R. Randall, Pervis C. Lee, Wendy G. Resneck, Yibin Wang, Robert J. Bloch, Jeanine A. Ursitti, Jay Yang
Publikováno v:
Journal of Molecular and Cellular Cardiology. 42:572-581
Decreases in the expression of connexin 43 and the integrity of gap junctions in cardiac muscle, induced by the constitutive activation of the c-Jun N-terminal kinase (JNK) signaling pathway, have been linked to conduction defects and sudden cardiac
Autor:
Dawn H. Catino, Robert J. Bloch, Jeanine A. Ursitti, Christian Antolik, Wendy G. Resneck, Andrea O'Neill
Publikováno v:
Neuroscience. 145:56-65
Formation of the neuromuscular junction requires the release of agrin from the presynaptic terminal of motor neurons. Clustering of acetylcholine receptors (AChRs) on the postsynaptic sarcolemma is initiated by agrin-dependent activation of the muscl
Publikováno v:
Current Protocols in Protein Science
Transferring proteins from polyacrylamide gels onto retentive membranes is now primarily used for immunoblotting. A second application that was quite common up to about a decade ago was electroblotting of proteins for N-terminal and internal sequenci
Autor:
Michele R. Stone, Jeanine A. Ursitti, Andrea O'Neill, Wendy G. Resneck, Robert J. Bloch, Minda M. McNally, Pervis C. Lee, Amber L. Bowman
Publikováno v:
Journal of Biological Chemistry. 279:41830-41838
We used degenerate primers for the amino- and carboxyl-terminal ends of the rod domains of intermediate filament proteins in reverse transcriptase-PCR experiments to identify and clone cytokeratins 8 and 19 (K8 and K19) from cardiac muscle of the adu
Autor:
Keith W. Dilly, Yibin Wang, Meizi Zheng, Jader S. Cruz, Yusu Gu, Jonathan W. Lederer, Manxiang Li, Kenneth R. Chien, Ju Chen, John Ross, Jeanine A. Ursitti
Publikováno v:
American Journal of Physiology-Heart and Circulatory Physiology. 286:H424-H433
The small G protein Ras-mediated signaling pathway has been implicated in the development of hypertrophy and diastolic dysfunction in the heart. Earlier cellular studies have suggested that the Ras pathway is responsible for reduced L-type calcium ch
Autor:
L. A. Martin, Robert J. Bloch, Tessa Chaney, Wendy G. Resneck, Bradley E. Alger, Jeanine A. Ursitti, Carol L. Zielke
Publikováno v:
Developmental Brain Research. 129:81-93
We studied the spectrins in developing hippocampal tissue in vivo and in vitro to learn how they contribute to the organization of synaptic and extrasynaptic regions of the neuronal plasma membrane. beta-Spectrin, but not beta-fodrin or alpha-fodrin,