Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Saraswathi Ponnam"'
Autor:
Thomas Kampourakis, Saraswathi Ponnam, Kenneth S. Campbell, Austin Wellette-Hunsucker, Daniel Koch
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-15 (2024)
Abstract Phosphorylation of cardiac myosin binding protein-C (cMyBP-C) is a determinant of cardiac myofilament function. Although cMyBP-C phosphorylation by various protein kinases has been extensively studied, the influence of protein phosphatases o
Externí odkaz:
https://doaj.org/article/7a23efe4b40e463b8186edcb27c59c8c
Autor:
Priyanka Parijat, Saraswathi Ponnam, Seetharamaiah Attili, Kenneth S. Campbell, Mohammed El-Mezgueldi, Mark Pfuhl, Thomas Kampourakis
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-13 (2023)
Abstract The large unmet demand for new heart failure therapeutics is widely acknowledged. Over the last decades the contractile myofilaments themselves have emerged as an attractive target for the development of new therapeutics for both systolic an
Externí odkaz:
https://doaj.org/article/426170449f754cb48a52dcf44aedf251
Publikováno v:
bioRxiv : the preprint server for biology
Phosphorylation of cardiac myosin binding protein-C (cMyBP-C) is a crucial determinant of cardiac myofilament function. Although cMyBP-C phosphorylation by various protein kinases has been extensively studied, the influence of protein phosphatases on
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df5265bab5a9e079dd022e305c256e82
https://hdl.handle.net/21.11116/0000-000C-FCD2-B21.11116/0000-000C-FCD4-9
https://hdl.handle.net/21.11116/0000-000C-FCD2-B21.11116/0000-000C-FCD4-9
Autor:
Ivanka R. Sevrieva, Saraswathi Ponnam, Ziqian Yan, Malcolm Irving, Thomas Kampourakis, Yin-Biao Sun
Publikováno v:
The Journal of biological chemistry.
Protein kinase A (PKA)-mediated phosphorylation of sarcomeric proteins enhances heart muscle performance in response to β-adrenergic stimulation and is associated with accelerated relaxation and increased cardiac output for a given preload. At the c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d665c8e53ab404d1e6ebf0965e83566
https://pubmed.ncbi.nlm.nih.gov/36470422
https://pubmed.ncbi.nlm.nih.gov/36470422
Autor:
Yin-Biao Sun, Birgit Brandmeier, Saraswathi Ponnam, Thomas Kampourakis, Kenneth S. Campbell, Malcolm Irving, Mathias Gautel, Ivanka Sevrieva
Publikováno v:
The Journal of Biological Chemistry
Heart muscle contractility and performance are controlled by posttranslational modifications of sarcomeric proteins. Although myosin regulatory light chain (RLC) phosphorylation has been studied extensively in vitro and in vivo, the precise role of c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29d5de9dd591591d13112109a754ccad
http://europepmc.org/articles/PMC7135997
http://europepmc.org/articles/PMC7135997
Autor:
Thomas Kampourakis, Saraswathi Ponnam
Publikováno v:
The Journal of Biological Chemistry
The cardiac isoform of myosin-binding protein C (cMyBP-C) is a key regulatory protein found in cardiac myofilaments that can control the activation state of both the actin-containing thin and myosin-containing thick filaments. However, in contrast to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7cef65eda5396fba4700cacbee677366
https://pubmed.ncbi.nlm.nih.gov/34915024
https://pubmed.ncbi.nlm.nih.gov/34915024
Publikováno v:
The Journal of biological chemistry. 293(37)
Myosin-binding protein-C (cMyBP-C) is a key regulator of contractility in heart muscle, and its regulatory function is controlled in turn by phosphorylation of multiple serines in its m-domain. The structural and functional effects of m-domain phosph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4f50d0b24717f13a06764d72947c4600
https://pubmed.ncbi.nlm.nih.gov/30082313
https://pubmed.ncbi.nlm.nih.gov/30082313
Publikováno v:
Journal of Molecular and Cellular Cardiology
Hypertrophic cardiomyopathy (HCM) is frequently linked to mutations in the protein components of the myosin-containing thick filaments leading to contractile dysfunction and ultimately heart failure. However, the molecular structure-function relation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::46f61750a99b7d63ef0e96f0ed8363c8
https://pubmed.ncbi.nlm.nih.gov/29452157
https://pubmed.ncbi.nlm.nih.gov/29452157