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Patricia M. Cameron

Researcher at Merck & Co.

Publications -  33
Citations -  3131

Patricia M. Cameron is an academic researcher from Merck & Co.. The author has contributed to research in topics: Peptide sequence & Antigen. The author has an hindex of 22, co-authored 33 publications receiving 3069 citations.

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Mediation by HLA-DM of dissociation of peptides from HLA-DR

TL;DR: Recombinant soluble HLA-DM heterodimers have been purified from culture supernatants of insect cell transformants and induce the dissociation of a subset of peptides bound to Hla-DR, including a nested set of class-II-associated invariant chain peptides (CLIP).
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Identification of a monocyte specific pre-interleukin 1 beta convertase activity

TL;DR: In this paper, the authors showed that only extracts derived from human monocytes and THP.1 cells were capable of cleaving precursor IL-1 beta to authentic mature IL 1 β.
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Stromelysin‐1: Three‐dimensional structure of the inhibited catalytic domain and of the C‐truncated proenzyme

TL;DR: Comparison of the active site of stromelysin with that of thermolysin reveals that most of the residues proposed to play significant roles in the enzymatic mechanism of temperaturesolysin have equivalents in stromlysin, but that three residues implicated in the catalytic mechanism of Thermolysin are not represented in stamelysin.
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Photochemical preparation of a pyridone containing tetracycle: A jak protein kinase inhibitor

TL;DR: The pyridone-containing tetracycle may be prepared from trisubstituted imidazole in high yield by irradiation with >350 nm light and inhibits the phosphorylation of STAT5 (an in vivo substrate of the Jak family) as measured by Western blotting.
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The envA Permeability/Cell Division Gene of Escherichia coli Encodes the Second Enzyme of Lipid A Biosynthesis UDP-3-O-(R-3-HYDROXYMYRISTOYL)-N-ACETYLGLUCOSAMINE DEACETYLASE

TL;DR: The envA gene of Escherichia coli was cloned into an isopropyl-1-thio-β-D-galactopyranoside-inducible T7-based expression system and it was found to be the structural gene for UDP-3-O-acyl-GlcNAc deacetylase, which is the second enzymatic step of lipid A biosynthesis.