John D. Huck
Hauptman-Woodward Medical Research Institute
6 Papers
John D. Huck is an academic researcher from Hauptman-Woodward Medical Research Institute. The author has contributed to research in topics: Nucleotide excision repair & Replication protein A. The author has an hindex of 5, co-authored 6 publications. Previous affiliations of John D. Huck include University at Buffalo.
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Papers
Thrombin contributes to cancer immune evasion via proteolysis of platelet-bound GARP to activate LTGF-β
Alessandra Metelli,Bill X. Wu,Brian Riesenberg,Silvia Guglietta,John D. Huck,Catherine M. Mills,Anqi Li,Saleh Rachidi,Carsten Krieg,Mark P. Rubinstein,Daniel T. Gewirth,Shaoli Sun,Michael B. Lilly,Amy H. Wahlquist,David P. Carbone,Yiping Yang,Bei Liu,Zihai Li,Zihai Li +18 more
TL;DR: A direct link between thrombin catalytic activity and release of mature TGF-β1 from platelets is shown and it is proposed that blockade of GARP cleavage is a valuable therapeutic strategy to overcome cancer’s resistance to immunotherapy.
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Structural and Functional Analysis of GRP94 in the Closed State Reveals an Essential Role for the Pre-N Domain and a Potential Client-Binding Site.
TL;DR: It is shown that the GRP94 pre-N domain is essential for client maturation, and it is identified as an important regulator of ATPase rates and dimer closure and the results provide structural insight into the ATP-dependent client maturation process of GRP 94.
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Dynamic DNA binding licenses a repair factor to bypass roadblocks in search of DNA lesions.
Maxwell W. Brown,Yoori Kim,Gregory M. Williams,John D. Huck,Jennifer A. Surtees,Ilya J. Finkelstein +5 more
TL;DR: This work uses DNA curtains and single-molecule fluorescence imaging to investigate how Msh2–Msh3, a eukaryotic mismatch repair complex, navigates on crowded DNA and suggests how MSh2– Msh3 locates DNA lesions outside of replication-coupled repair.
Structures of Hsp90 alpha and Hsp90 beta bound to a purine-scaffold inhibitor reveal an exploitable residue for drug selectivity.
John D. Huck,John D. Huck,Nanette L.S. Que,Sahil Sharma,Tony Taldone,Gabriela Chiosis,Daniel T. Gewirth,Daniel T. Gewirth +7 more
TL;DR: The results provide a structural explanation for the binding preference of PU inhibitors for Hsp90α and demonstrate that the single nonconserved residue in the ATP-binding pocket may be exploited for α/β selectivity.
9
Exploring the Functional Complementation between Grp94 and Hsp90.
Kevin A. Maharaj,Kevin A. Maharaj,Nanette L.S. Que,Feng Hong,John D. Huck,John D. Huck,Sabrina K. Gill,Shuang Wu,Zihai Li,Daniel T. Gewirth,Daniel T. Gewirth +10 more
TL;DR: It is shown that the N-terminal domain or the combination of the second lobe of the Middle domain plus the C-terminale domain of Grp94 can functionally substitute for their yeast Hsp90 counterparts but that the equivalent HSp90 domains cannot functionally replace their counterparts in Grp 94.