Author

D. C. Marx

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Approach:statistical model· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:protein folding & dynamics· 2 Organism:bacteria (other)· 1 Organism:human· 1 Approach:mechanistic / dynamical model· 1 Assay:proteomics· 1

Frequent Co-Authors

K. G. Fleming· 3 shared A. M. Plummer· 2 shared M. A. Roskopf· 2 shared T. Devlin· 2 shared A. Arefin· 1 shared A. J. Gonzalez-Hernandez· 1 shared A. M. Faustino· 1 shared B. T. Amann· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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3 shared papersBiophysics

K. G. Fleming

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4 papers

Recent·Most cited

Control of G protein-coupled receptor function via membrane-interacting intrinsically disordered C-terminal domains

C. Mancinelli, D. C. Marx, A. J. Gonzalez-Hernandez, K. Huynh, L. Mancinelli, A. Arefin, G. Khelashvili, J. Levitz, D. Eliezer

This paper investigates how C-terminal domains of GPCRs interact with membranes to regulate receptor function, showing that these interactions influence transducer coupling and are modulated by phosphorylation and membrane composition.

bioRxiv · Aug 16, 2023 · PreprintBiophysics

FkpA Enhances Membrane Protein Folding using an Extensive Interaction Surface

T. Devlin, D. C. Marx, M. A. Roskopf, Q. R. Bubb, A. M. Plummer, K. G. Fleming

This study investigates FkpA's role in enhancing outer membrane protein folding and shows it binds clients with an extensive interface, distinct from other chaperones.

bioRxiv · Nov 1, 2022Biophysics

Local Bilayer Hydrophobicity Modulates Membrane Protein Stability

D. C. Marx, K. G. Fleming

The paper determines transfer free energies of nonpolar side chains in membranes using experiments and simulations, revealing a correlation with local water concentration and implications for membrane protein design and disease mutation analysis.

bioRxiv · Sep 1, 2020 · PreprintBiophysics

SurA is a "Groove-y" Chaperone That Expands Unfolded Outer Membrane Proteins

D. C. Marx, A. M. Plummer, A. M. Faustino, M. A. Roskopf, M. J. Leblanc, T. Devlin, H. J. Lessen, B. T. Amann, P. J. Fleming, S. Krueger, S. D. Fried, K. G. Fleming

This paper investigates how SurA, a bacterial chaperone, interacts with unfolded outer membrane proteins (uOMPs) using structural biology techniques, revealing distinct binding modes and a mechanism for uOMP expansion.

bioRxiv · Dec 17, 2019Biophysics