Author

M. Braitbard

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· 2

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 2 Organism:bacteria (other)· 1 Research Focus:cell type annotation· 1 Assay:cryo-EM· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1 Approach:statistical model· 1 Organism:virus· 1

Frequent Co-Authors

D. Schneidman-Duhovny· 2 shared A. Friedman· 1 shared A. Rouvinski· 1 shared B. A. Garcia· 1 shared D. G. Wolf· 1 shared E. Brielle· 1 shared F. Daldal· 1 shared H. J. Kim· 1 shared

Activity by Year

2020-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 25 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

2 shared papersBiochemistry

D. Schneidman-Duhovny

Mutual co-authors in cluster

Author profile →

2 papers

Recent·Most cited

Targeted in situ cross-linking mass spectrometry and integrative modeling reveal the architectures of Nsp1, Nsp2, and Nucleocapsid proteins from SARS-CoV-2

M. Slavin, J. Zamel, K. Zohar, S. Eliyahu, M. Braitbard, E. Brielle, L. Baraz, M. Stolovich-Rain, A. Friedman, D. G. Wolf, A. Rouvinski, M. Linial, D. Schneidman-Duhovny, N. Kalisman

This study uses targeted in situ CLMS and integrative modeling to determine the structures of SARS-CoV-2 Nsp1, Nsp2, and N proteins, revealing key interactions and functional insights.

bioRxiv · Feb 4, 2021Biochemistry

Cryo-EM Structures of Respiratory bc1-cbb3 type CIII2CIV Super-complex and Electronic Communication Between the Complexes

S. Steimle, T. VanEeuwen, Y. Ozturk, H. J. Kim, M. Braitbard, N. Selamoglu, B. A. Garcia, D. Schneidman-Duhovny, K. Murakami, F. Daldal

This paper reports the first cryo-EM structure of a bacterial respiratory bc1-cbb3 super-complex and native CIII2 conformers, revealing structural and electronic communication features between complexes.

bioRxiv · Jun 27, 2020Biochemistry