Výsledky vyhledávání - "Moira B. Glaccum"

TNF Receptor-Deficient Mice Reveal Divergent Roles for p55 and p75 in Several Models of Inflammation

Autor: Jacques J. Peschon, Dauphine S. Torrance, Kim L. Stocking, Moira B. Glaccum, Carol Otten, Cynthia R. Willis, Keith Charrier, Philip J. Morrissey, Carol B. Ware, Kendall M. Mohler

Publikováno v: The Journal of Immunology. 160:943-952

The pleiotropic activities of the potent proinflammatory cytokine TNF are mediated by two structurally related, but functionally distinct, receptors, p55 and p75, that are coexpressed on most cell types. The majority of biologic responses classically

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::bb6f71c8b610a603a86ab4382bb25a68
https://doi.org/10.4049/jimmunol.160.2.943

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Isolation and Mapping of Human T-Cell Protein Tyrosine Phosphatase Sequences: Localization of Genes and Pseudogenes Discriminated Using Fluorescence Hybridization with Genomic versus cDNA Probes

Autor: D. E. Cool, Jeanne B. Lawrence, Arthur M. Bruskin, Nancy R. Green, David E. Hill, Moira B. Glaccum, Edmond H. Fischer, Carol V. Johnson

Publikováno v: Genomics. 16:619-629

This work reports the isolation, partial characterization, and chromosomal mapping of several human T-cell protein tyrosine phosphatase (PTPase) sequences and provides a direct comparison of the specificity of cDNA versus genomic probes in discrimina

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9a6209eb2aa23c7a7a2b355f77a0ddb
https://doi.org/10.1006/geno.1993.1239

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Characterization of the in vivo function of TNF-alpha-related apoptosis-inducing ligand, TRAIL/Apo2L, using TRAIL/Apo2L gene-deficient mice

Autor: Lisa M, Sedger, Moira B, Glaccum, JoAnn C L, Schuh, Suzanne T, Kanaly, Eilidh, Williamson, Nobuhiko, Kayagaki, Theordore, Yun, Pam, Smolak, Tiep, Le, Ray, Goodwin, Brian, Gliniak

Publikováno v: European journal of immunology. 32(8)

To define the normal physiological role for the TRAIL/Apo2L in vivo, we generated TRAIL/Apo2L gene-targeted mice. These mice develop normally and show no defects in lymphoid or myeloid cell homeostasis or function. Although TRAIL/Apo2L kills transfor

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f846517250c436d2ccabe3d95c38f527
https://pubmed.ncbi.nlm.nih.gov/12209637

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Isolation of the cDNA encoding rat skeletal muscle myosin light chain kinase. Sequence and tissue distribution

Autor: E G Krebs, John D. Scott, C L Roush, Peter J. Kennelly, David M. Helfman, Moira B. Glaccum

Publikováno v: Journal of Biological Chemistry. 263:10510-10516

A cDNA clone encoding skeletal muscle myosin light chain kinase (MLCK) was isolated from a rat skeletal muscle library using oligonucleotide probes. The total length of the rat skeletal muscle MLCK cDNA was 2823 base pairs with an open reading frame

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::3f4ae1753e909dae569b11262d8b59ec
https://doi.org/10.1016/s0021-9258(19)81545-4

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Primary-structure requirements for inhibition by the heat-stable inhibitor of the cAMP-dependent protein kinase

Autor: Moira B. Glaccum, Edmond H. Fischer, John D. Scott, Edwin G. Krebs

Publikováno v: Proceedings of the National Academy of Sciences. 83:1613-1616

The amino acid sequence of the heat-stable inhibitor of the cAMP-dependent protein kinase (PKI) was determined recently [Scott, J. D., Fischer, E. H., Takio, K., Demaille, J. G. & Krebs, E. G. (1985) Proc. Natl. Acad. Sci. USA 82, 5732-5736]. An earl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71a68411a117b83a39dd83ade2925363
https://doi.org/10.1073/pnas.83.6.1613

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ORGANIZATION OF MYOSIN LIGHT CHAIN KINASE FROM RABBIT SKELETAL MUSCLE

Autor: Peter J. Kennelly, Koji Takio, Donald K. Blumenthal, Arthur M. Edelman, Moira B. Glaccum, Rachel E. Klevit, Christine L. Roush, John D. Scott, Koiti Titani, Kenneth A. Walsh, Edwin G. Krebs

Publisher Summary This chapter elaborates the organization of myosin light chain kinase from rabbit skeletal muscle. The myosin light chain kinases comprise a family of tissue-specific isozymes whose function is to phosphorylate one of the light chai

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::fbb067f0b8a9a5dd0ff0e1d4a454fcce
https://doi.org/10.1016/b978-0-12-521040-9.50091-7

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The molecular cloning of a type II regulatory subunit of the cAMP-dependent protein kinase from rat skeletal muscle and mouse brain

Autor: Michael D. Uhler, E G Krebs, Moira B. Glaccum, G S McKnight, Mark J. Zoller, David M. Helfman, John D. Scott

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America. 84(15)

A cDNA clone for a type II regulatory (R) subunit of the cAMP-dependent protein kinase (ATP:protein phosphotransferase, EC 2.7.1.37) was isolated from a rat skeletal muscle library using a specific 47-base oligonucleotide probe. The rat cDNA was 1.2

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb332fed6c290acfbc324289c70d2fbc
https://pubmed.ncbi.nlm.nih.gov/3037538

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