Jeffery W. Kelly
Scripps Research Institute
447 Papers
4.7K Citations
Jeffery W. Kelly is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Transthyretin & Chemistry. The author has an hindex of 108, co-authored 428 publications. Previous affiliations of Jeffery W. Kelly include University of North Carolina at Chapel Hill & Texas A&M University.
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Papers
N-PEGylation of a Reverse Turn is Stabilizing in Multiple Sequence Contexts unlike N-GlcNAcylation
TL;DR: The thermodynamic data are consistent with the hypothesis that PEGylation destabilizes the protein denatured state ensemble via an excluded volume effect, whereas N-glycosylation-associated stabilization results primarily from native state interactions between the N- glycan and the protein.
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Transthyretin Acid Induced Denaturation is Required for Amyloid Fibril Formation in Vitro
Wilfredo Colón,Jeffery W. Kelly +1 more
- 01 Jan 1991
TL;DR: The human plasma protein transthyretin, implicated as the causative agent in Familial Amyloid Polyneuropathy and Senile Systemic Amyloidsosis, was transformed into amyloid fibrils in vitro under conditions that mimic the environment of a lysosome.
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Cys-10 mixed disulfide modifications exacerbate transthyretin familial variant amyloidogenicity: a likely explanation for variable clinical expression of amyloidosis and the lack of pathology in C10S/V30M transgenic mice?
Qinghai Zhang,Jeffery W. Kelly +1 more
TL;DR: In vitro data reveal that the C10S/V30M and V30M TTR homotetramers have identical amyloidogenicity and stability, implying that Cys-10 mixed disulfide formation enhances amyloidsogenesis in V 30M transgenic mice.
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A general strategy for the bacterial expression of amyloidogenic peptides using BCL-XL-1/2 fusions.
TL;DR: It is demonstrated that driving the peptides into inclusion bodies using fusion to BCL‐XL‐1/2 is a general strategy for their expression and isolation, as exemplified by the production of 11 peptides species.
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A Comprehensive Enumeration of the Human Proteostasis Network. 1. Components of Translation, Protein Folding, and Organelle-Specific Systems
Suzanne Elsasser,Lisa P. Elia,Richard I. Morimoto,Evan T. Powers,Daniel Finley,Eric Mockler,Leandro Lima,Steven Finkbeiner,Jason E. Gestwicki,Thomas Stoeger,Kedi Cao,Dan Garza,Jeffery W. Kelly,Miranda P. Collier,T. Kelly Rainbolt,Shuhei Taguwa,Ching Chieh Chou,Ranen Aviner,Natália Barbosa,Fabian Morales-Polanco,Vincent B. Masto,Judith Frydman +21 more
TL;DR: This series of manuscripts aims to operationally define the human proteostasis network by providing a comprehensive, annotated list of its components, including 959 unique genes that comprise the protein synthesis machinery, chaperones, folding enzymes, systems for trafficking proteins into and out of organelles, and organelle-specific degradation systems.