Christopher L. Colbert
North Dakota State University
32 Papers
118 Citations
Christopher L. Colbert is an academic researcher from North Dakota State University. The author has contributed to research in topics: Protein structure & Chemistry. The author has an hindex of 14, co-authored 26 publications. Previous affiliations of Christopher L. Colbert include University of Texas Southwestern Medical Center & Purdue University.
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Papers
Evidence for a strong sulfur–aromatic interaction derived from crystallographic data
TL;DR: This study confirms observations based on statistics of interaction of amino acids in protein crystal structures and identifies a preferred geometry of interaction between the divalent sulfur moiety and the aromatic ring that differs significantly from that found by other approaches.
170
Molecular basis of the regulation of Beclin 1-dependent autophagy by the γ-herpesvirus 68 Bcl-2 homolog M11
TL;DR: The results suggest that M11 inhibits autophagy through a mechanism that involves the binding of the Beclin 1 BH3 domain in the M11 hydrophobic surface groove.
A Cluster Exposed: Structure of the Rieske Ferredoxin from Biphenyl Dioxygenase and the Redox Properties of Rieske Fe-S Proteins
Christopher L. Colbert,Manon M.-J. Couture,Lindsay D. Eltis,Lindsay D. Eltis,Jeffrey T. Bolin +4 more
TL;DR: The crystal structure of BphF, the Rieske-type ferredoxin associated with biphenyl dioxygenase, has structural features consistent with a minimal and perhaps archetypical Rieskes protein.
104
Intrinsically Disordered Regions in Autophagy Proteins
TL;DR: This rigorous bioinformatic analysis shows that the majority of key human autophagy proteins include intrinsically disordered regions (IDRs), which are sequences lacking stable secondary and tertiary structure; suggesting that IDRs play an important, yet hitherto uninvestigated, role inAutophagy.
78
Crystal structure of Spot 14, a modulator of fatty acid synthesis
Christopher L. Colbert,Chai Wan Kim,Young Ah Moon,Lisa Henry,Lisa Henry,Maya Palnitkar,Maya Palnitkar,William B. McKean,Kevin Fitzgerald,Johann Deisenhofer,Jay D. Horton,Hyock Joo Kwon +11 more
TL;DR: The structure of S14 suggests a mechanism whereby heterodimer formation with MIG12 attenuates the ability of MIG 12 to activate ACC, and biochemical data showing that S14 can form heterodimers with M IG12 are presented.