M
Michel Streuli
Researcher at Harvard University
Publications - 69
Citations - 9260
Michel Streuli is an academic researcher from Harvard University. The author has contributed to research in topics: Protein tyrosine phosphatase & Peptide sequence. The author has an hindex of 45, co-authored 69 publications receiving 9004 citations. Previous affiliations of Michel Streuli include University of Zurich & Radboud University Nijmegen.
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Journal ArticleDOI
TIA-1 is a translational silencer that selectively regulates the expression of TNF-α
Monica Piecyk,Stephen Wax,Andreas Beck,Nancy Kedersha,Mita Gupta,Beatrice Maritim,Samantha Chen,Cyril Gueydan,Véronique Kruys,Michel Streuli,Paul A. Anderson +10 more
TL;DR: Mice lacking TIA‐1 are hypersensitive to the toxic effects of LPS, indicating that this translational control pathway may regulate the organismal response to microbial stress.
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The Multidomain Protein Trio Binds the LAR Transmembrane Tyrosine Phosphatase, Contains a Protein Kinase Domain, and Has Separate Rac-Specific and Rho-Specific Guanine Nucleotide Exchange Factor Domains
Anne Debant,Carles Serra-Pagès,Katja Seipel,Stephen J. O'Brien,May Tang,Sang-Ho Park,Michel Streuli +6 more
TL;DR: As the LAR PTPase localizes to the ends of focal adhesions, it is proposed that LAR and the Trio GEF/PSK may orchestrate cell-matrix and cytoskeletal rearrangements necessary for cell migration.
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Synthesis in E. coli of a polypeptide with human leukocyte interferon activity
Shigekazu Nagata,Hideharu Taira,Alan Hall,Lorraine Johnsrud,Michel Streuli,Josef Ecsödi,Werner Boll,Kari Cantell,Charles Weissmann +8 more
TL;DR: Double-stranded cDNA prepared from the 12S fraction of poly (A) RNA from interferon (IF)-producing human leukocytes was cloned in Escherichia coli using the pBR322 vector and one of the resulting clones had a 910-base pair insert which could hybridise to IF mRNA and was responsible for the production of a polypeptide with biological IF activity.
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Structural diversity and evolution of human receptor-like protein tyrosine phosphatases.
TL;DR: The structural diversity of receptor‐like PTPases was examined by isolated human cDNA clones that cross‐hybridized to a Drosophila PTPase cDNA clone, DPTP12, under non‐stringent hybridization conditions and found partial sequences of HPTP gamma and zeta indicate that they are highly homologous and contain two P TPase‐like domains.
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The 193-Kd Vault Protein, Vparp, Is a Novel Poly(Adp-Ribose) Polymerase
Valerie A. Kickhoefer,Amara C. Siva,Nancy Kedersha,Elisabeth M. Inman,Cristina T. Ruland,Michel Streuli,Leonard H. Rome +6 more
TL;DR: The 193-kD vault protein is identified by its interaction with the MVP in a yeast two-hybrid screen and confirmed its identity by peptide sequence analysis, and it is shown that one substrate for this vault-associated PARP activity is the MVP.