Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Benjamin F. Maynard"'
Autor:
Megan Leander, Chloe Bass, Kathryn Marchetti, Benjamin F Maynard, Juan Pedro Wulff, Sheila Ons, Ruthann Nichols
Publikováno v:
PLoS ONE, Vol 10, Iss 3, p e0120492 (2015)
Peptidergic signaling regulates cardiac contractility; thus, identifying molecular switches, ligand-receptor contacts, and antagonists aids in exploring the underlying mechanisms to influence health. Myosuppressin (MS), a decapeptide, diminishes card
Externí odkaz:
https://doaj.org/article/842acd85eef845db912f88074f5d4141
Autor:
Benjamin F Maynard, Chloe Bass, Chris Katanski, Kiran Thakur, Beth Manoogian, Megan Leander, Ruthann Nichols
Publikováno v:
PLoS ONE, Vol 8, Iss 9, p e75502 (2013)
FMRF-NH2 peptides which contain a conserved, identical C-terminal tetrapeptide but unique N terminus modulate cardiac contractility; yet, little is known about the mechanisms involved in signaling. Here, the structure-activity relationships (SARs) of
Externí odkaz:
https://doaj.org/article/97c4c4c2ef2e46d39574e9bf87651bbc
Publikováno v:
Peptides. 146:170641
The structural conservation and activity of the myosuppressin cardioinhibitory peptide across species suggests it plays an important role in physiology, yet much remains unknown regarding its signaling. We previously reported Drosophila melanogaster
Autor:
M. Matta, Maria Dolores Setzu, Christopher D. Katanski, E. Mariane, V. Melis, Valentina Capponi, I. Zurro, Benjamin F. Maynard, Chloe Bass, Ruthann Nichols, Patrizia Muroni, Martina Loi
Publikováno v:
Peptides. 53:278-285
Peptides in the RF-NH2 family are grouped together based on an amidated dipeptide C terminus and signal through G-protein coupled receptors (GPCRs) to influence diverse physiological functions. By determining the mechanisms underlying RF-NH2 signalin
Autor:
M. Leander, Juan Pedro Wulff, Ruthann Nichols, Chloe Bass, Kathryn A Marchetti, Benjamin F. Maynard, Sheila Ons
Publikováno v:
PLoS ONE
PLoS ONE, Vol 10, Iss 3, p e0120492 (2015)
SEDICI (UNLP)
Universidad Nacional de La Plata
instacron:UNLP
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
PLoS ONE, Vol 10, Iss 3, p e0120492 (2015)
SEDICI (UNLP)
Universidad Nacional de La Plata
instacron:UNLP
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Peptidergic signaling regulates cardiac contractility; thus, identifying molecular switches, ligand-receptor contacts, and antagonists aids in exploring the underlying mechanisms to influence health. Myosuppressin (MS), a decapeptide, diminishes card
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1e4020f26bb14e30847a301604e6999
http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0120492
http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0120492
Autor:
Ruthann Nichols, Chris Katanski, M. Leander, Benjamin F. Maynard, Beth Manoogian, Kiran T. Thakur, Chloe Bass
Publikováno v:
PLoS ONE
PLoS ONE, Vol 8, Iss 9, p e75502 (2013)
PLoS ONE, Vol 8, Iss 9, p e75502 (2013)
FMRF-NH2 peptides which contain a conserved, identical C-terminal tetrapeptide but unique N terminus modulate cardiac contractility; yet, little is known about the mechanisms involved in signaling. Here, the structure-activity relationships (SARs) of