Author

M. D. Flores

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

Biology Disciplines

Click to filter author papers

Biochemistry· 3

Signature Assays, Organisms & Methods

Click to filter · or open tag

Organism:human· 3 Approach:experimental assay· 2 Research Focus:protein structure prediction· 2 Assay:cryo-EM· 1 Approach:deep learning· 1 Assay:electronic health records· 1 Organism:mouse· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

J. A. Rodriguez· 3 shared M. R. Sawaya· 3 shared C.-T. Zee· 2 shared S. Zink· 2 shared A. Saucedo· 1 shared C. Glynn· 1 shared C. Millan· 1 shared D. R. Boyer· 1 shared

Activity by Year

2021-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersBiochemistry

J. A. Rodriguez

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

BiochemistrybioRxivFeb 8, 2023

Cryo-EM Structure of a Human LECT2 Amyloid Fibril Reveals a Network of Polar Ladders at its Core

L. S. Richards, M. D. Flores, S. Zink…·J. A. Rodriguez

This paper determines the cryo-EM structure of human LECT2 amyloid fibrils, revealing a tightly packed core stabilized by polar residues and hydrophobic contacts.

DOI 10.1016/j.str.2023.08.007

humancryo-EM

𝕏 PostBluesky

BiochemistrybioRxivPreprintDec 7, 2022

Structure of a reversible amyloid fibril formed by the CPEB3 prion-like domain reveals a core sequence involved in translational regulation

M. D. Flores, M. R. Sawaya, D. R. Boyer…·J. A. Rodriguez

This study identifies an amyloidogenic segment in CPEB3's prion domain that is critical for its function in translational regulation and long-term memory.

DOI 10.1101/2022.12.07.519389

humanprotein structure

𝕏 PostBluesky

BiochemistrybioRxivSep 13, 2021

Fragment-based ab initio phasing of peptidic nanocrystals by MicroED

L. Richards, M. D. Flores, C. Millan…·J. A. Rodriguez

This paper introduces a fragment-based method for de novo structure determination of peptidic nanocrystals using MicroED, enabling the solution of previously intractable structures.

DOI 10.1021/acsbiomedchemau.2c00082

humanyeast

𝕏 PostBluesky