Amino acid changes in the peptide binding site have structural consequences at the surface of class I glycoproteins

Autor: L R Pease, R M Horton, J K Pullen, H D Hunt, T J Yun, E M Rohren, J L Prescott, S M Jobe, K S Allen

Publikováno v: The Journal of Immunology. 150:3375-3381

Structural changes on the surface of the class I Ag binding domain resulting from point mutations localized inside the Ag binding cleft of the H-2Kb and Kf glycoproteins were revealed using mAb. Both the loss and gain of antibody binding sites found

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8a16d0015bdfcee99f27adb2b3dd62c1
https://doi.org/10.4049/jimmunol.150.8.3375

Peptide interactions with the Kb antigen recognition site

Autor: J K Pullen, H D Hunt, L R Pease

Publikováno v: The Journal of Immunology. 146:2145-2151

The ability of OVA-specific H-2Kb-restricted CTL to recognize the defined OVA258-276 peptide in the context of the Kbm mutants and variants of these mutants was examined to determine how specific variations in the Ag recognition site-influenced pepti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c50d67ad5774d93c30f9bcf024697741
https://doi.org/10.4049/jimmunol.146.7.2145

Systematic Analysis of the Effect of Genomic Knock-Out of Non-Essential Promiscuous HAD-Like Phosphatases YcsE, YitU and YwtE on Flavin and Adenylate Content in Bacillus Subtilis.

Autor: Scharf A; Hamburg School of Food Science, Institute of Food Chemistry, University of Hamburg, Grindelallee 117, 20146, Hamburg, Germany., La-Rostami F; Hamburg School of Food Science, Institute of Food Chemistry, University of Hamburg, Grindelallee 117, 20146, Hamburg, Germany., Illarionov BA; Hamburg School of Food Science, Institute of Food Chemistry, University of Hamburg, Grindelallee 117, 20146, Hamburg, Germany., Nemes V; Hamburg School of Food Science, Institute of Food Chemistry, University of Hamburg, Grindelallee 117, 20146, Hamburg, Germany., Feldmann AM; Hamburg School of Food Science, Institute of Food Chemistry, University of Hamburg, Grindelallee 117, 20146, Hamburg, Germany., Höft LS; Hamburg School of Food Science, Institute of Food Chemistry, University of Hamburg, Grindelallee 117, 20146, Hamburg, Germany., Lösel H; Hamburg School of Food Science, Institute of Food Chemistry, University of Hamburg, Grindelallee 117, 20146, Hamburg, Germany., Bacher A; TUM School of Natural Sciences, Technical University of Munich, 85748, Garching, Germany., Fischer M; Hamburg School of Food Science, Institute of Food Chemistry, University of Hamburg, Grindelallee 117, 20146, Hamburg, Germany.

Publikováno v: Chembiochem : a European journal of chemical biology [Chembiochem] 2024 Jun 17; Vol. 25 (12), pp. e202400165. Date of Electronic Publication: 2024 May 24.

Recognition of a single amino acid change on the surface of a major transplantation antigen is in the context of self peptide

Autor: J K, Pullen, M D, Tallquist, R W, Melvold, L R, Pease

Publikováno v: Journal of immunology (Baltimore, Md. : 1950). 152(7)

The transcripts encoding two strongly alloantigenic class I mutant molecules, Kdm4 and Kdm5, were characterized and found to encode products that differ from the parental Kd glycoprotein by single amino acid substitutions. The Kdm4 molecule has an am

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2a69b3c37960450075984d8617ca8d39
https://pubmed.ncbi.nlm.nih.gov/8144927

Structure and diversity of class I antigen presenting molecules in the mouse

Autor: L R, Pease, R M, Horton, J K, Pullen, Z L, Cai

Publikováno v: Critical reviews in immunology. 11(1)

Sequence comparisons among class I genes provide insight into the nature and origins of diversity in the human and mouse MHC. The profiles of diversity among alleles and between different loci indicate that genetic interactions among class I genes ge

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2cc3dd7fa580656fa2c36d7ad14e2f81
https://pubmed.ncbi.nlm.nih.gov/1883507