Author

C. Z. Buffalo

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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Cell Biology· 2 Biochemistry· 1 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:host-pathogen & immune response· 2 Assay:structural biology· 2 Research Focus:cell signaling & trafficking· 1 Assay:cryo-EM· 1 Organism:human· 1 Organism:non-human primate· 1 Assay:protein structure· 1

Frequent Co-Authors

X. Ren· 4 shared J. H. Hurley· 3 shared T. G. Flower· 2 shared A. Boecker· 1 shared A. K. Stavoe· 1 shared A. L. Yokom· 1 shared C. Chang· 1 shared C. Sturzel· 1 shared

Activity by Year

2019-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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4 shared papersCell Biology

X. Ren

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Author profile →

4 papers

Recent·Most cited

Structural basis for ATG9A recruitment to the ULK1 complex in mitophagy initiation

X. Ren, T. N. Nguyen, W. K. Lam, C. Z. Buffalo, M. Lazarou, A. L. Yokom, J. H. Hurley

The paper determines the structure of ATG9A's C-terminal tail interacting with the ULK1 complex's ATG13:ATG101 HORMA dimer, revealing how this interaction facilitates mitophagy.

bioRxiv · Jul 12, 2022Cell Biology

Structural Basis for Membrane Recruitment of ATG16L1 by WIPI2 in Autophagy

L. M. Strong, C. Chang, A. Boecker, T. G. Flower, C. Z. Buffalo, X. Ren, A. K. Stavoe, E. L. F. Holzbaur, J. H. Hurley

This study determines the crystal structure of WIPI2 interacting with ATG16L1, revealing the molecular mechanism of ATG16L1 recruitment to the phagophore and its role in autophagy initiation.

bioRxiv · May 14, 2021Cell Biology

Structure of SARS-CoV-2 ORF8, a rapidly evolving coronavirus protein implicated in immune evasion

T. G. Flower, C. Z. Buffalo, R. M. Hooy, M. Allaire, X. Ren, J. H. Hurley

The paper determines the crystal structure of SARS-CoV-2 ORF8, revealing unique dimerization interfaces that may enable immune evasion.

bioRxiv · Aug 27, 2020Biophysics

Structural basis for tetherin antagonism as a barrier to zoonotic lentiviral transmission

C. Z. Buffalo, C. Sturzel, E. Heusinger, D. Kmiec, F. Kirchhoff, J. Hurley, X. Ren

The paper determines the structure of SIV Nef interacting with simian tetherin and AP-2, revealing how Nef bypasses tetherin's antiviral function by refolding AP-2 and creating a binding site for the DIWK motif.

bioRxiv · May 17, 2019Biochemistry