Zobrazeno 1 - 10
of 33
pro vyhledávání: '"Ruth F. Sommese"'
Autor:
Shenping Liu, Ruth F. Sommese, Nicole L. Nedoma, Lucy Mae Stevens, Jason K. Dutra, Liying Zhang, David J. Edmonds, Yang Wang, Michelle Garnsey, Michelle F. Clasquin
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-14 (2023)
Abstract Hydroxysteroid 17-beta-dehydrogenase 13 (HSD17B13) is a hepatic lipid droplet-associated enzyme that is upregulated in patients with non-alcoholic fatty liver disease. Recently, there have been several reports that predicted loss of function
Externí odkaz:
https://doaj.org/article/749817982a194a3cbe9e946b62e48e24
Autor:
Shenping Liu, Bethany L. Kormos, John D. Knafels, Parag V. Sahasrabudhe, Amy Rosado, Ruth F. Sommese, Allan R. Reyes, Jessica Ward, Rachel J. Roth Flach, Xiaochun Wang, Leanne M. Buzon, Matthew R. Reese, Samit K. Bhattacharya, Kiyoyuki Omoto, Kevin J. Filipski
Publikováno v:
Journal of Biological Chemistry. 299:102959
Autor:
Carter J Swanson, Ruth F Sommese, Karl J Petersen, Michael Ritt, Joshua Karslake, David D Thomas, Sivaraj Sivaramakrishnan
Publikováno v:
PLoS ONE, Vol 11, Iss 10, p e0162331 (2016)
Protein kinase C α (PKCα) is a nodal regulator in several intracellular signaling networks. PKCα is composed of modular domains that interact with each other to dynamically regulate spatial-temporal function. We find that PKCα specifically, rapid
Externí odkaz:
https://doaj.org/article/cc4b07610da745a192461515a767abe7
Publikováno v:
eLife, Vol 4 (2015)
Myosin V and VI are antagonistic motors that cohabit membrane vesicles in cells. A systematic study of their collective function, however, is lacking and forms the focus of this study. We functionally reconstitute a two-dimensional actin-myosin inter
Externí odkaz:
https://doaj.org/article/40cb831e1bd6418baca7a2b3ad01deaa
Autor:
Ruth F Sommese, Suman Nag, Shirley Sutton, Susan M Miller, James A Spudich, Kathleen M Ruppel
Publikováno v:
PLoS ONE, Vol 8, Iss 12, p e83403 (2013)
Hypertrophic cardiomyopathy (HCM) and dilated cardiomyopathy (DCM) lead to significant cardiovascular morbidity and mortality worldwide. Mutations in the genes encoding the sarcomere, the force-generating unit in the cardiomyocyte, cause familial for
Externí odkaz:
https://doaj.org/article/db8f6c99925847daa80dc994a68711a9
Distinct structural mechanisms determine substrate affinity and kinase activity of protein kinase Cα
Autor:
Sangbae Lee, Manbir Sandhu, Nagarajan Vaidehi, Adrien B. Larsen, Titu Devamani, Hyun Deok Song, Sivaraj Sivaramakrishnan, Ruth F. Sommese, Abhinandan Jain
Publikováno v:
Journal of Biological Chemistry. 292:16300-16309
Protein kinase Cα (PKCα) belongs to the family of AGC kinases that phosphorylate multiple peptide substrates. Although the consensus sequence motif has been identified and used to explain substrate specificity for PKCα, it does not inform the stru
Publikováno v:
Journal of Biological Chemistry. 292:2873-2880
Resolving the conformational dynamics of large multidomain proteins has proven to be a significant challenge. Here we use a variety of techniques to dissect the roles of individual protein kinase Cα (PKCα) regulatory domains in maintaining catalyti
Publikováno v:
Journal of Biological Chemistry. 291:21963-21970
The overlapping network of kinase-substrate interactions provides exquisite specificity in cell signaling pathways, but also presents challenges to our ability to understand the mechanistic basis of biological processes. Efforts to dissect kinase-sub
Autor:
Minghui Liu, Ruth F. Sommese, Sivaraj Sivaramakrishnan, Key-Sun Kim, Matthew J. Tyska, Rizal F. Hariadi
Publikováno v:
Protein Science. 25:2089-2094
DNA nanostructures have become an important and powerful tool for studying protein function over the last 5 years. One of the challenges, though, has been the development of universal methods for patterning protein complexes on DNA nanostructures. He
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1805
Throughout the cell, motor proteins work together to drive numerous molecular processes and functions. For example, ensembles of myosin motors collectively transport vesicles and organelles, maintain membrane homeostasis, and drive muscle contraction