Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Laxma G. Reddy"'
Autor:
Jody L. Lutterman, Sean M. Mcgurran, Laxma G. Reddy, Kevin S. Gorski, Calin D. Dumitru, Elaine A. Egging, Kenneth E. Lipson, Melissa M. Piri, Gary W. Gullikson, Dave D. Johnson, Felicia R. Cochran, Mark A. Tomai, Mary A. Antonysamy, Joel Proksch
Publikováno v:
Cancer Immunology, Immunotherapy. 58:575-587
Innate immune stimulation with Toll-like receptor (TLR) agonists is a proposed modality for immunotherapy of melanoma. Here, a TLR7/8 agonist, 3M-011, was used effectively as a single systemic agent against disseminated mouse B16-F10 melanoma. The in
Defining the Molecular Components of Calcium Transport Regulation in a Reconstituted Membrane System
Publikováno v:
Biochemistry. 42:4585-4592
Using a chemically defined reconstitution system, we performed a systematic study of key factors in the regulation of the Ca-ATPase by phospholamban (PLB). We varied both the lipid/protein and PLB/Ca-ATPase ratios, determined the effects of PLB phosp
Publikováno v:
Biophysical Journal. 76:2587-2599
We have developed a method using fluorescence energy transfer (FET) to analyze protein oligomeric structure. Two populations of a protein are labeled with fluorescent donor and acceptor, respectively, then mixed at a defined donor/acceptor ratio. A t
Publikováno v:
Biochemistry. 38:3954-3962
Phospholamban (PLB), a 52-amino acid protein, regulates the Ca-ATPase (calcium pump) in cardiac sarcoplasmic reticulum (SR) through PLB phosphorylation mediated by beta-adrenergic stimulation. The mobility of PLB on SDS-PAGE indicates a homopentamer,
Publikováno v:
Annals of the New York Academy of Sciences. 853:103-115
Significant advances have recently been made in understanding the regulation of Ca(2+)-ATPase by phospholamban and in modeling their structures. However, these insights would be furthered by determining the 3-D structure of both proteins within the m
Publikováno v:
Biochemistry. 34:4448-4456
We have studied the secondary structure of native phospholamban (PLB), a 52-residue integral membrane protein that regulates calcium uptake into the cardiac sarcoplasmic reticulum, as well as its 27-residue carboxy-terminal transmembrane segment (PLB
Autor:
Jeffrey J. O'Brian, Suren A. Tatulian, Larry R. Jones, Laxma G. Reddy, David L. Stokes, Steven E. Cala
Publikováno v:
Journal of Biological Chemistry. 270:9390-9397
Phospholamban (PLB) is a small, transmembrane protein that resides in the cardiac sarcoplasmic reticulum (SR) and regulates the activity of Ca(2+)-ATPase in response to beta-adrenergic stimulation. We have used the baculovirus expression system in Sf
Publikováno v:
The Journal of biological chemistry. 281(49)
Toll-like receptors (TLRs) TLR1, TLR2, TLR4, and TLR6 are evolutionarily conserved, highly homologous, and localized to plasma membranes of host cells and recognize pathogen-associated molecular patterns (PAMPs) derived from bacterial membranes. Thes
Autor:
Gregory W. Hunter, Laxma G. Reddy, David D. Thomas, Yvonne M. Angell, Christine B. Karim, George Barany
Publikováno v:
Peptides for the New Millennium ISBN: 0792364457
Calcium transport into the sarcoplasmic reticulum of cardiac muscle is catalyzed by the Ca pump and regulated by phospholamban (PLB), a 52-amino acid integral membrane peptide that inhibits the pump [1]. PLB is predominantly a homopentamer on electro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c3213c240034a0e3971821dcb4056ca9
https://doi.org/10.1007/0-306-46881-6_153
https://doi.org/10.1007/0-306-46881-6_153
Autor:
George Barany, M. Germana Paterlini, Laxma G. Reddy, David D. Thomas, Gregory W. Hunter, Christine B. Karim
Publikováno v:
The Journal of biological chemistry. 276(42)
To study the structural and functional roles of the cysteine residues at positions 36, 41, and 46 in the transmembrane domain of phospholamban (PLB), we have used Fmoc (N-(9-fluorenyl)methoxycarbonyl) solid-phase peptide synthesis to prepare alpha-am