Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Sarah E. Lang"'
Publikováno v:
Earth and Space Science, Vol 10, Iss 7, Pp n/a-n/a (2023)
Abstract Understanding and attributing changes to water quality is essential to the study and management of coastal ecosystems and the ecological functions they sustain (e.g., primary productivity, predation, and submerged aquatic vegetation growth).
Externí odkaz:
https://doaj.org/article/03405f74fcf5422583343db2292cf14d
Autor:
Sarah E. Lang, Tamara K. Stevenson, Tabea M. Schatz, Brandon J. Biesiadecki, Margaret V. Westfall
Publikováno v:
Data in Brief, Vol 15, Iss , Pp 562-566 (2017)
Secondary phosphorylation develops in myocytes expressing phospho-mimetic cardiac troponin I (cTnI) but it is not known whether multiple substitutions (e.g. cTnISDTD and cTnIS4D) cause preferential phosphorylation of the remaining endogenous or the p
Externí odkaz:
https://doaj.org/article/a4e1837e11024f5d9df365da743af645
Autor:
Tabea M. Schatz, Brandon J. Biesiadecki, Margaret V. Westfall, Sarah E. Lang, Tamara K. Stevenson
Publikováno v:
Data in Brief, Vol 15, Iss, Pp 562-566 (2017)
Data in Brief
Data in Brief
Secondary phosphorylation develops in myocytes expressing phospho-mimetic cardiac troponin I (cTnI) but it is not known whether multiple substitutions (e.g. cTnISDTD and cTnIS4D) cause preferential phosphorylation of the remaining endogenous or the p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79d55c9c4e103d37fca353486bb71ff9
https://doi.org/10.1016/j.dib.2017.09.066
https://doi.org/10.1016/j.dib.2017.09.066
Publikováno v:
Archives of Biochemistry and Biophysics. 601:42-47
A phospho-null Ala substitution at protein kinase C (PKC)-targeted cardiac troponin I (cTnI) S43/45 reduces myocyte and cardiac contractile function. The goal of the current study was to test whether cTnIS43/45N is an alternative, functionally conser
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3f93951a926f324e7d0daf7e154fb43
https://doi.org/10.1016/j.abb.2016.02.002
https://doi.org/10.1016/j.abb.2016.02.002
Autor:
Sarah E. Lang, Tabea M. Schatz, Margaret V. Westfall, Brandon J. Biesiadecki, Tamara K. Stevenson
Increased protein kinase C (PKC) activity is associated with heart failure, and can target multiple cardiac troponin I (cTnI) residues in myocytes, including S23/24, S43/45 and T144. In earlier studies, cTnI-S43D and/or -S45D augmented S23/24 and T14
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e9d78c08703abb952eea8ce56498cd0
https://europepmc.org/articles/PMC5555030/
https://europepmc.org/articles/PMC5555030/
Autor:
Helen C. Wu, Todd J. Herron, Dustin Robinson, Sarah E. Lang, Margaret V. Westfall, Philip A. Wahr
Publikováno v:
Archives of Biochemistry and Biophysics. 535:49-55
Phosphorylation of cardiac troponin I serines 43/45 (cTnISer43/45) by protein kinase C (PKC) is associated with cardiac dysfunction and yet there is disagreement about the role this cluster plays in modulating contractile performance. The present stu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8049710c7649f6149775418d41388865
https://doi.org/10.1016/j.abb.2012.12.021
https://doi.org/10.1016/j.abb.2012.12.021
Autor:
Margaret V. Westfall, Sarah E. Lang
Publikováno v:
Methods in Molecular Biology ISBN: 9781493925711
Traditional methods for DNA transfection are often inefficient and toxic for terminally differentiated cells, such as cardiac myocytes. Vector-based gene transfer is an efficient approach for introducing exogenous cDNA into these types of primary cel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85af38715d547bcc6453f3cc75b05af0
https://doi.org/10.1007/978-1-4939-2572-8_15
https://doi.org/10.1007/978-1-4939-2572-8_15
Publikováno v:
Journal of molecular and cellular cardiology. 79
Protein kinase C (PKC) targets cardiac troponin I (cTnI) S43/45 for phosphorylation in addition to other residues. During heart failure, cTnI S43/45 phosphorylation is elevated, and yet there is ongoing debate about its functional role due, in part,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a17283f19f49e99e4c0330d78ac99456
https://pubmed.ncbi.nlm.nih.gov/25481661
https://pubmed.ncbi.nlm.nih.gov/25481661
Autor:
Sarah E. Lang, Hyosook Hwang, Sakthivel Sadayappan, Julie B. Rogers, Margaret V. Westfall, Tamara K. Stevenson, Dustin Robinson, Sharlene M. Day, Sivaraj Sivaramakrishnan
Publikováno v:
Scientific Reports
Elevated protein kinase C βII (PKCβII) expression develops during heart failure and yet the role of this isoform in modulating contractile function remains controversial. The present study examines the impact of agonist-induced PKCβII activation o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b03b2cd73f8fe62515e424905e69893
https://doi.org/10.1038/srep01971
https://doi.org/10.1038/srep01971
Autor:
Sarah E. Lang, Margaret V. Westfall
Publikováno v:
Biophysical Journal. 106:775a
Protein kinase C phosphorylation of S43/45 on cardiac troponin I (cTnI) increases during periods of cardiac stress to modulate cardiac myocyte contractile performance, but the functional impact of this phosphorylation remains controversial. Adenovira
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::857ca21a7b2bea8e30fc200649e895af
https://doi.org/10.1016/j.bpj.2013.11.4252
https://doi.org/10.1016/j.bpj.2013.11.4252