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Presentation of endogenous peptides to MHC class I-restricted cytotoxic T lymphocytes in transport deletion mutant T2 cells

Autor: H J Zweerink, M C Gammon, U Utz, S Y Sauma, T Harrer, J C Hawkins, R P Johnson, A Sirotina, J D Hermes, B D Walker

Publikováno v: The Journal of Immunology. 150:1763-1771

The ability of minigene-encoded viral peptide epitopes to be presented by class I molecules in the absence of MHC-encoded transporters has been evaluated in mutant T2 cells. These cells have a large deletion in the class II MHC region that includes t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9bed18ce94df84489104bf7a55204573
https://doi.org/10.4049/jimmunol.150.5.1763

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Endogenous loading of HLA-A2 molecules with an analog of the influenza virus matrix protein-derived peptide and its inhibition by an exogenous peptide antagonist

Autor: M C Gammon, M A Bednarek, W E Biddison, S S Bondy, J D Hermes, G E Mark, A R Williamson, H J Zweerink

Publikováno v: The Journal of Immunology. 148:7-12

Episomal plasmids (p8901) with minigenes coding for the influenza virus matrix peptide amino acids 57-68 (KGILGFVFTLTV; referred to as M57-68) or coding for a modified peptide were introduced into HLA-A2-positive target cells. The association of thes

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ae6e652db52c91188f46ba35febce5b6
https://doi.org/10.4049/jimmunol.148.1.7

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Tetrapeptide derived inhibitors of complexation of a class II MHC: fully unnatural ligands

Autor: A B, Jones, J J, Acton, A D, Adams, W, Yuen, E A, Nichols, C D, Schwartz, L S, Wicker, J D, Hermes

Publikováno v: Bioorganicmedicinal chemistry letters. 9(14)

Tetrapeptide derived major histocompatability (MHC) II ligands have been developed that contain no unadulterated peptide bonds. These are the 'least peptidic' ligands for any MHC protein yet reported.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7edff2cc3a23f8a68d2fd68669e2f779
https://pubmed.ncbi.nlm.nih.gov/10450992

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Human cytoplasmic 3-hydroxy-3-methylglutaryl coenzyme A synthase: expression, purification, and characterization of recombinant wild-type and Cys129 mutant enzymes

Autor: L. L. Rokosz, P. A. Lachance, Gautam Sanyal, M. A. Cueto, E. A. Butkiewicz, D. A. Boulton, J. D. Hermes

Publikováno v: Archives of biochemistry and biophysics. 312(1)

A cDNA for the human cytoplasmic 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) synthase (EC 4.1.3.5) was subcloned and expressed from a T7-based vector in Escherichia coli. The over-produced enzyme was purified using a three-step protocol that gene

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2fcef01dd17f1b6ac42abed4864f80c
https://pubmed.ncbi.nlm.nih.gov/7913309

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FK-506-binding protein: three-dimensional structure of the complex with the antagonist L-685,818

Autor: J W, Becker, J, Rotonda, B M, McKeever, H K, Chan, A I, Marcy, G, Wiederrecht, J D, Hermes, J P, Springer

Publikováno v: The Journal of biological chemistry. 268(15)

L-685,818 differs only slightly in structure from the immunosuppressive drug FK-506, and both compounds bind with comparable affinity to the 12-kDa FK-506-binding protein (FKBP12), the major intracellular receptor for the drug. Despite these similari

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::daba5ba4c879fa51f3e4c496d5598c8a
https://pubmed.ncbi.nlm.nih.gov/7684380

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Presentation of endogenous peptides to MHC class I-restricted cytotoxic T lymphocytes in transport deletion mutant T2 cells

Autor: H J, Zweerink, M C, Gammon, U, Utz, S Y, Sauma, T, Harrer, J C, Hawkins, R P, Johnson, A, Sirotina, J D, Hermes, B D, Walker

Publikováno v: Journal of immunology (Baltimore, Md. : 1950). 150(5)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ec1a28c9fc5da5c2cc28362aabf3a0bf
https://pubmed.ncbi.nlm.nih.gov/7679694

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Chloroform-soluble nucleotides in Escherichia coli. Role of CDP-diglyceride in the enzymatic cytidylylation of phosphomonoester acceptors

Autor: C. R. H. Raetz, J. D. Hermes, C. E. Bulawa

Publikováno v: Journal of Biological Chemistry. 258:14974-14980

CDP-diglyceride, the precursor of all the phospholipids in Escherichia coli, is cleaved in vitro to phosphatidic acid and CMP by a membrane-bound hydrolase. Since the physiological function of CDP-diglyceride hydrolase is unknown, we have explored th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b94e13e7887713827802600054b5de28
https://doi.org/10.1016/s0021-9258(17)43759-8

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Chloroform-soluble nucleotides in Escherichia coli. Role of CDP-diglyceride in the enzymatic cytidylylation of phosphomonoester acceptors

Autor: C E, Bulawa, J D, Hermes, C R, Raetz

Publikováno v: The Journal of biological chemistry. 258(24)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f3eacbe43f02bff3ad6aea269b361b06
https://pubmed.ncbi.nlm.nih.gov/6361023

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Stability constants of Mg2+ and Cd2+ complexes of adenine nucleotides and thionucleotides and rate constants for formation and dissociation of MgATP and MgADP

Autor: V L, Pecoraro, J D, Hermes, W W, Cleland

Publikováno v: Biochemistry. 23(22)

Stability constants for the Mg2+ and Cd2+ complexes of ATP, ADP, ATP alpha S, ATP beta S, and ADP alpha S have been determined at 30 degrees C and mu = 0.1 M by 31P NMR. Besides being of the utmost importance for determining species distributions for

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4d06b9f7478c2b081917bb3083c8c777
https://pubmed.ncbi.nlm.nih.gov/6334536

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