Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Dagan C. Marx"'
Autor:
Alexa Strauss, Alberto J. Gonzalez-Hernandez, Joon Lee, Nohely Abreu, Purushotham Selvakumar, Leslie Salas-Estrada, Melanie Kristt, Anisul Arefin, Kevin Huynh, Dagan C. Marx, Kristen Gilliland, Bruce J. Melancon, Marta Filizola, Joel Meyerson, Joshua Levitz
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-17 (2024)
Abstract The metabotropic glutamate receptors (mGluRs) are neuromodulatory family C G protein coupled receptors which assemble as dimers and allosterically couple extracellular ligand binding domains (LBDs) to transmembrane domains (TMDs) to drive in
Externí odkaz:
https://doaj.org/article/6e48d6960b5240c69e16e202a52f5256
Autor:
Taylor Devlin, Dagan C. Marx, Michaela A. Roskopf, Quenton R. Bubb, Ashlee M. Plummer, Karen G. Fleming
Publikováno v:
Protein Science. 32
Autor:
Taylor A. Devlin, Dagan C. Marx, Michaela A. Roskopf, Quenton R. Bubb, Ashlee M. Plummer, Karen G. Fleming
Outer membrane protein (OMP) biogenesis in gram-negative bacteria is managed by a network of periplasmic chaperones that includes SurA, Skp, and FkpA. These chaperones bind unfolded OMPs (uOMPs) in dynamic conformational ensembles to suppress uOMP ag
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::231d4177a2e3cf3de2d72d2a0d5b1d19
https://doi.org/10.1101/2022.11.01.514694
https://doi.org/10.1101/2022.11.01.514694
Autor:
Dagan C. Marx, Karen G. Fleming
Publikováno v:
J Am Chem Soc
Through the insertion of nonpolar side chains into the bilayer, the hydrophobic effect has long been accepted as a driving force for membrane protein folding. However, how the changing chemical composition of the bilayer affects the magnitude side ch
Autor:
Taylor Devlin, Dagan C. Marx, Michaela A. Roskopf, Quenton R. Bubb, Ashlee M. Plummer, Karen G. Fleming
Publikováno v:
Biophysical Journal. 122:152a
Autor:
Mathis J. Leblanc, Patrick J. Fleming, Anneliese M. Faustino, Henry J. Lessen, Susan Krueger, Barbara T. Amann, Stephen D. Fried, Dagan C. Marx, Ashlee M. Plummer, Taylor Devlin, Michaela A. Roskopf, Karen G. Fleming
Publikováno v:
Proc Natl Acad Sci U S A
The periplasmic chaperone network ensures the biogenesis of bacterial outer membrane proteins (OMPs) and has recently been identified as a promising target for antibiotics. SurA is the most important member of this network, both due to its genetic in
Publikováno v:
Protein Sci
SurA is thought to be the most important periplasmic chaperone for outer membrane protein biogenesis. Its structure is composed of a core region and two peptidylprolyl isomerase domains, termed P1 and P2, connected by flexible linkers. As such these
Autor:
Karen G. Fleming, G. Nasir Khan, Cameron M. Chow, Binyong Liang, Vicki H. Wysocki, Stacey Gerben, David Baker, Anastassia A. Vorobieva, David J. Brockwell, Dagan C. Marx, Alyssa Q. Stiving, Sheena E. Radford, Jim E. Horne, Sophie R. Harvey, Alex Kang, Sinduja Marx, Asim K. Bera, Paul White, Lukas K. Tamm
Publikováno v:
Science
Building a barrel Computational design offers the possibility of making proteins with customized structures and functions. The range of accessible protein scaffolds has expanded with the design of increasingly complex cytoplasmic proteins and, recent
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2168
The thermodynamic stabilities of membrane proteins are of fundamental interest to provide a biophysical description of their structure-function relationships because energy determines conformational populations. In addition, structure-energy relation
Autor:
Dagan C. Marx, Karen G. Fleming
Publikováno v:
Curr Opin Struct Biol
Membrane proteins have historically been recalcitrant to biophysical folding studies. However, recent adaptations of methods from the soluble protein folding field have found success in their applications to transmembrane proteins composed of both α