P
Pranitha Reddy
Researcher at University of North Carolina at Chapel Hill
Publications - 3
Citations - 5012
Pranitha Reddy is an academic researcher from University of North Carolina at Chapel Hill. The author has contributed to research in topics: ADAM17 Protein & ADAM15. The author has an hindex of 3, co-authored 3 publications receiving 4809 citations.
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Journal ArticleDOI
A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells
Roy A. Black,Charles Rauch,Carl J. Kozlosky,Jacques J. Peschon,Jennifer L. Slack,Martin F. Wolfson,Beverly J. Castner,Kim L. Stocking,Pranitha Reddy,Subhashini Srinivasan,Nicole Nelson,Norman Boiani,Kenneth A. Schooley,Mary Gerhart,Raymond Davis,Jeffrey N. Fitzner,Richard S. Johnson,Raymond J. Paxton,Carl J. March,Douglas P. Cerretti +19 more
TL;DR: The results should facilitate the development of therapeutically useful inhibitors of TNF-α release, and they indicate that an important function of adamalysins may be to shed cell-surface proteins.
Journal ArticleDOI
An Essential Role for Ectodomain Shedding in Mammalian Development
Jacques J. Peschon,Jennifer L. Slack,Pranitha Reddy,Kim L. Stocking,Susan W. Sunnarborg,David C. Lee,William E. Russell,Beverly J. Castner,Richard S. Johnson,Jeffrey N. Fitzner,Rogely W. Boyce,Nicole Nelson,Carl J. Kozlosky,Martin F. Wolfson,Charles Rauch,Douglas P. Cerretti,Raymond J. Paxton,Carl J. March,Roy A. Black +18 more
TL;DR: The phenotype of mice lacking TACE suggests an essential role for soluble TGFalpha in normal development and emphasizes the importance of protein ectodomain shedding in vivo.
Journal ArticleDOI
Crystal structure of the catalytic domain of human tumor necrosis factor-alpha-converting enzyme.
Klaus Maskos,Carlos Fernandez-Catalan,Robert Huber,Gleb Bourenkov,Hans D. Bartunik,George A. Ellestad,Pranitha Reddy,Martin F. Wolfson,Charles Rauch,Beverly J. Castner,Raymond J. Davis,Howard R. G. Clarke,Melissa Petersen,Jeffrey N. Fitzner,Douglas P. Cerretti,Carl J. March,Raymond J. Paxton,Roy A. Black,Wolfram Bode +18 more
TL;DR: The structure of TACE opens a different approach toward the design of specific synthetic TACE inhibitors, which could act as effective therapeutic agents in vivo to modulate TNFalpha-induced pathophysiological effects, and might also help to control related shedding processes.