P
Philip A. Pemberton
Researcher at Icahn School of Medicine at Mount Sinai
Publications - 30
Citations - 2550
Philip A. Pemberton is an academic researcher from Icahn School of Medicine at Mount Sinai. The author has contributed to research in topics: Serpin & Protease. The author has an hindex of 16, co-authored 30 publications receiving 2482 citations.
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The serpins are an expanding superfamily of structurally similar but functionally diverse proteins - Evolution, mechanism of inhibition, novel functions, and a revised nomenclature
Gary A. Silverman,Phillip I. Bird,Robin W. Carrell,Frank C. Church,Paul Bernard Coughlin,Peter G.W. Gettins,James A. Irving,David A. Lomas,Cliff J. Luke,Richard W. Moyer,Philip A. Pemberton,Eileen Remold-O'Donnell,Guy S. Salvesen,James Travis,James C. Whisstock +14 more
TL;DR: This work aims to provide a systematic literature review and meta-analyses of the determinants of blood clotting disorders and their Kessler’s disease progression as well as some of the mechanisms behind these reactions.
Journal ArticleDOI
Cross-Class Inhibition of the Cysteine Proteinases Cathepsins K, L, and S by the Serpin Squamous Cell Carcinoma Antigen 1: A Kinetic Analysis†
Charles Schick,Philip A. Pemberton,Guo-Ping Shi,Yoshiro Kamachi,Sule Cataltepe,Allison J. Bartuski,Eric R. Gornstein,Dieter Brömme,Harold A. Chapman,Gary A. Silverman +9 more
TL;DR: The data suggest that mammalian serpins, in general, utilize their dynamic tertiary structure to trap proteinases from more than one mechanistic class and that SCCA1, in particular, may be involved in a novel inhibitory pathway aimed at regulating a powerful array of lysosomal cysteine proteinases.
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Squamous Cell Carcinoma Antigen 2 Is a Novel Serpin That Inhibits the Chymotrypsin-like Proteinases Cathepsin G and Mast Cell Chymase
Charles Schick,Yoshiro Kamachi,Allison J. Bartuski,Sule Cataltepe,Norman M. Schechter,Philip A. Pemberton,Gary A. Silverman +6 more
TL;DR: Recombinant SCCA2 was most effective against two chymotrypsin-like proteinases from inflammatory cells, but was ineffective against papain-like cysteine proteinases.
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Maspin Is an Intracellular Serpin That Partitions into Secretory Vesicles and Is Present at the Cell Surface
Philip A. Pemberton,A. Rene Tipton,Nadine Pavloff,Jason Smith,James R. Erickson,Zahi M. Mouchabeck,Michael C. Kiefer +6 more
TL;DR: The tissue distribution and subcellular localization studies indicate that soluble intracellular and vesicle-associated maspin probably play an important role in controlling the invasion, motility, and proliferation of cells expressing it, whereas extracellular maspIn may also regulate these processes in adjacent cells.
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The Tumor Suppressor Maspin Does Not Undergo the Stressed to Relaxed Transition or Inhibit Trypsin-like Serine Proteases. EVIDENCE THAT MASPIN IS NOT A PROTEASE INHIBITORY SERPIN
Philip A. Pemberton,Daniel T. Wong,Helen L. Gibson,Kiefer Michael C,Paul A. Fitzpatrick,Ruth Sager,Philip J. Oakland Barr +6 more
TL;DR: The role of tumor suppressor proteins in the development of malignancy has made the understanding of their molecular mechanisms of action of great importance as mentioned in this paper, but the molecular mechanism of maspin is currently unknown.