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Mary Gerhart

Researcher at Amgen

Publications -  14
Citations -  5518

Mary Gerhart is an academic researcher from Amgen. The author has contributed to research in topics: Growth hormone receptor & Glycosylation. The author has an hindex of 12, co-authored 14 publications receiving 5331 citations.

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A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells

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.
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Trail-r2: a novel apoptosis-mediating receptor for trail

TL;DR: The identification of a distinct receptor for TRAIL, TRAIL‐R2, by ligand‐based affinity purification and subsequent molecular cloning suggests an unexpected complexity to TRAIL biology, reminiscent of dual receptors for TNF, the canonical member of this family.
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Tumor necrosis factor-alpha converting enzyme (TACE) regulates epidermal growth factor receptor ligand availability.

TL;DR: A broad role for TACE in the regulated shedding of EGFR ligands is supported, showing that cells lacking TACE activity shed dramatically less TGF-α as compared with wild-type cultures and that T GF-α cleavage was partially restored by infection of Tace-deficient cells with TACE-encoding adenovirus.
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T1/ST2 Signaling Establishes It as a Member of an Expanding Interleukin-1 Receptor Family

TL;DR: Comparisons between new proteins that share homology with the signaling domain of the type I interleukin-1 receptor and known IL-1RI homologous proteins revealed six clusters of amino acid similarity, indicating that the sequence homology between IL- 1RI and T1/ST2 indicates a functional homology as well.
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Poxvirus Genomes Encode a Secreted, Soluble Protein That Preferentially Inhibits β Chemokine Activity yet Lacks Sequence Homology to Known Chemokine Receptors☆

TL;DR: This work shows the "35K" virulence gene in variola and cowpox viruses, whose vaccinia and Shope fibroma virus equivalents are strongly conserved in sequence, actually encodes a secreted soluble protein with high-affinity binding to virtually all known beta chemokines, but only weak or no affinity to the alpha and gamma classes.