J
J. Christopher Fromme
Researcher at Cornell University
Publications - 62
Citations - 3260
J. Christopher Fromme is an academic researcher from Cornell University. The author has contributed to research in topics: GTPase & Golgi apparatus. The author has an hindex of 22, co-authored 53 publications receiving 2545 citations. Previous affiliations of J. Christopher Fromme include Harvard University & University of California, Berkeley.
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Journal ArticleDOI
Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase
TL;DR: The use of disulphide crosslinking is reported to obtain high-resolution crystal structures of MutY–DNA lesion-recognition complexes that reveal the basis for recognizing both lesions in the A·oxoG pair and for catalysing removal of the adenine base.
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Cranio-lenticulo-sutural dysplasia is caused by a SEC23A mutation leading to abnormal endoplasmic-reticulum-to-Golgi trafficking
Simeon A. Boyadjiev,Simeon A. Boyadjiev,J. Christopher Fromme,Jin Ben,Samuel S. Chong,Christopher Nauta,David J. Hur,George Q. Zhang,Susan Hamamoto,Randy Schekman,Mariella Ravazzola,Lelio Orci,Wafaa Eyaid +12 more
TL;DR: The observations suggest that disrupted endoplasmic reticulum export of the secretory proteins required for normal morphogenesis accounts for CLSD.
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Computed structures of core eukaryotic protein complexes.
Ian R. Humphreys,Jimin Pei,Minkyung Baek,Aditya Krishnakumar,Ivan Anishchenko,Sergey Ovchinnikov,Jing Zhang,Travis J. Ness,Sudeep Banjade,Saket R. Bagde,Viktoriya G. Stancheva,Xiao-Han Li,Kaixian Liu,Zhi Zheng,Zhi Zheng,Daniel J. Barrero,Upasana Roy,Jochen Kuper,Israel S. Fernández,Barnabas Szakal,Dana Branzei,Josep Rizo,Caroline Kisker,Eric C. Greene,Sue Biggins,Scott Keeney,Scott Keeney,Elizabeth A. Miller,J. Christopher Fromme,Tamara L. Hendrickson,Qian Cong,David Baker +31 more
TL;DR: The structures of many eukaryotic protein complexes are unknown, and there are likely many protein-protein interactions not yet identified as mentioned in this paper, but these structures play critical roles in biology.
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DNA glycosylase recognition and catalysis
TL;DR: The basis of the recognition of the oxidative lesion 8-oxoguanine by two structurally unrelated DNA glycosylases is now understood and has been revealed to involve surprisingly similar strategies.
Journal ArticleDOI
Structure of a trapped endonuclease III-DNA covalent intermediate.
TL;DR: The crystal structure of a trapped intermediate that represents EndoIII frozen in the act of repairing DNA is determined and suggests a rationale for the frequent occurrence in certain human cancers of a specific mutation in the related DNA repair protein MYH.