Pub Date : 2004-01-01DOI: 10.1016/S0065-3233(04)69001-2
J Christopher Fromme, Gregory L Verdine
{"title":"Base excision repair.","authors":"J Christopher Fromme, Gregory L Verdine","doi":"10.1016/S0065-3233(04)69001-2","DOIUrl":"https://doi.org/10.1016/S0065-3233(04)69001-2","url":null,"abstract":"","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"69 ","pages":"1-41"},"PeriodicalIF":0.0,"publicationDate":"2004-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0065-3233(04)69001-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24853538","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2004-01-01DOI: 10.1016/S0065-3233(04)68001-6
Daniel J Leahy
{"title":"Structure and function of the epidermal growth factor (EGF/ErbB) family of receptors.","authors":"Daniel J Leahy","doi":"10.1016/S0065-3233(04)68001-6","DOIUrl":"https://doi.org/10.1016/S0065-3233(04)68001-6","url":null,"abstract":"","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"68 ","pages":"1-27"},"PeriodicalIF":0.0,"publicationDate":"2004-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0065-3233(04)68001-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24777335","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2004-01-01DOI: 10.1016/S0065-3233(04)69005-X
Katarzyna Bebenek, Thomas A Kunkel
{"title":"Functions of DNA polymerases.","authors":"Katarzyna Bebenek, Thomas A Kunkel","doi":"10.1016/S0065-3233(04)69005-X","DOIUrl":"https://doi.org/10.1016/S0065-3233(04)69005-X","url":null,"abstract":"","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"69 ","pages":"137-65"},"PeriodicalIF":0.0,"publicationDate":"2004-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0065-3233(04)69005-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24853542","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2004-01-01DOI: 10.1016/S0065-3233(04)67003-3
Oranart Matangkasombut, Roy Auty, Stephen Buratowski
{"title":"Structure and function of the TFIID complex.","authors":"Oranart Matangkasombut, Roy Auty, Stephen Buratowski","doi":"10.1016/S0065-3233(04)67003-3","DOIUrl":"https://doi.org/10.1016/S0065-3233(04)67003-3","url":null,"abstract":"","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"67 ","pages":"67-92"},"PeriodicalIF":0.0,"publicationDate":"2004-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0065-3233(04)67003-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24399198","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2004-01-01DOI: 10.1016/S0065-3233(04)67007-0
Michael S Torok, Patrick A Grant
{"title":"Histone acetyltransferase proteins contribute to transcriptional processes at multiple levels.","authors":"Michael S Torok, Patrick A Grant","doi":"10.1016/S0065-3233(04)67007-0","DOIUrl":"https://doi.org/10.1016/S0065-3233(04)67007-0","url":null,"abstract":"","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"67 ","pages":"181-99"},"PeriodicalIF":0.0,"publicationDate":"2004-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0065-3233(04)67007-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24399202","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2004-01-01DOI: 10.1016/S0065-3233(04)67002-1
Stefan Björklund, Claes M Gustafsson
{"title":"The mediator complex.","authors":"Stefan Björklund, Claes M Gustafsson","doi":"10.1016/S0065-3233(04)67002-1","DOIUrl":"https://doi.org/10.1016/S0065-3233(04)67002-1","url":null,"abstract":"","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"67 ","pages":"43-65"},"PeriodicalIF":0.0,"publicationDate":"2004-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0065-3233(04)67002-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24399197","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2004-01-01DOI: 10.1016/S0065-3233(04)68008-9
Roland K Strong, Benjamin J McFarland
NK cells are crucial components of the innate immune system, capable of directly eliminating infected or tumorigenic cells and regulating down-stream adaptive immune responses. Unlike T cells, where the key recognition event driving activation is mediated by the unique T cell receptor (TCR) expressed on a given cell, NK cells express multiple activating and inhibitory cell-surface receptors (NKRs), often with overlapping ligand specificities. NKRs display two ectodomain structural homologies, either immunoglobulin- or C-type lectin-like (CTLD). The CTLD immunoreceptor NKG2D is found on NK cells but is also widely expressed on T cells and other immune system cells, providing stimulatory or co-stimulatory signals. NKG2D drives target cell killing following engagement of diverse, conditionally expressed MHC class I-like protein ligands whose expression can signal cellular distress due to infection or transformation. The symmetric, homodimeric receptor interacts with its asymmetric, monomeric ligands in similar 2:1 complexes, with an equivalent surface on each NKG2D monomer binding extensively and intimately to distinct, structurally divergent surfaces on the ligands. Thus, NKG2D ligand-binding site recognition is highly degenerate, further demonstrated by NKG2D's ability to simultaneously accommodate multiple non-conservative allelic or isoform substitutions in the ligands. In TCRs, "induced-fit" recognition explains cross-reactivity, but structural, computational, thermodynamic and kinetic analyses of multiple NKG2D-ligand pairs show that rather than classical "induced-fit" binding, NKG2D degeneracy is achieved using distinct interaction mechanisms at each rigid interface: recognition degeneracy by "rigid adaptation." While likely forming similar complexes with their ligand (HLA-E), other NKG2x NKR family members do not require such recognition degeneracy.
{"title":"NKG2D and Related Immunoreceptors.","authors":"Roland K Strong, Benjamin J McFarland","doi":"10.1016/S0065-3233(04)68008-9","DOIUrl":"https://doi.org/10.1016/S0065-3233(04)68008-9","url":null,"abstract":"<p><p>NK cells are crucial components of the innate immune system, capable of directly eliminating infected or tumorigenic cells and regulating down-stream adaptive immune responses. Unlike T cells, where the key recognition event driving activation is mediated by the unique T cell receptor (TCR) expressed on a given cell, NK cells express multiple activating and inhibitory cell-surface receptors (NKRs), often with overlapping ligand specificities. NKRs display two ectodomain structural homologies, either immunoglobulin- or C-type lectin-like (CTLD). The CTLD immunoreceptor NKG2D is found on NK cells but is also widely expressed on T cells and other immune system cells, providing stimulatory or co-stimulatory signals. NKG2D drives target cell killing following engagement of diverse, conditionally expressed MHC class I-like protein ligands whose expression can signal cellular distress due to infection or transformation. The symmetric, homodimeric receptor interacts with its asymmetric, monomeric ligands in similar 2:1 complexes, with an equivalent surface on each NKG2D monomer binding extensively and intimately to distinct, structurally divergent surfaces on the ligands. Thus, NKG2D ligand-binding site recognition is highly degenerate, further demonstrated by NKG2D's ability to simultaneously accommodate multiple non-conservative allelic or isoform substitutions in the ligands. In TCRs, \"induced-fit\" recognition explains cross-reactivity, but structural, computational, thermodynamic and kinetic analyses of multiple NKG2D-ligand pairs show that rather than classical \"induced-fit\" binding, NKG2D degeneracy is achieved using distinct interaction mechanisms at each rigid interface: recognition degeneracy by \"rigid adaptation.\" While likely forming similar complexes with their ligand (HLA-E), other NKG2x NKR family members do not require such recognition degeneracy.</p>","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"68 ","pages":"281-312"},"PeriodicalIF":0.0,"publicationDate":"2004-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0065-3233(04)68008-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24776748","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2004-01-01DOI: 10.1016/S0065-3233(04)69009-7
Haruo Ohmori, Eiji Ohashi, Tomoo Ogi
{"title":"Mammalian Pol kappa: regulation of its expression and lesion substrates.","authors":"Haruo Ohmori, Eiji Ohashi, Tomoo Ogi","doi":"10.1016/S0065-3233(04)69009-7","DOIUrl":"https://doi.org/10.1016/S0065-3233(04)69009-7","url":null,"abstract":"","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"69 ","pages":"265-78"},"PeriodicalIF":0.0,"publicationDate":"2004-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0065-3233(04)69009-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24853546","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2004-01-01DOI: 10.1016/S0065-3233(04)69011-5
Brigette Tippin, Phuong Pham, Ronda Bransteitter, Myron F Goodman
{"title":"Somatic hypermutation: a mutational panacea.","authors":"Brigette Tippin, Phuong Pham, Ronda Bransteitter, Myron F Goodman","doi":"10.1016/S0065-3233(04)69011-5","DOIUrl":"https://doi.org/10.1016/S0065-3233(04)69011-5","url":null,"abstract":"","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"69 ","pages":"307-35"},"PeriodicalIF":0.0,"publicationDate":"2004-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0065-3233(04)69011-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24853548","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2004-01-01DOI: 10.1016/S0065-3233(04)67005-7
Lucio Comai
{"title":"Mechanism of RNA polymerase I transcription.","authors":"Lucio Comai","doi":"10.1016/S0065-3233(04)67005-7","DOIUrl":"https://doi.org/10.1016/S0065-3233(04)67005-7","url":null,"abstract":"","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"67 ","pages":"123-55"},"PeriodicalIF":0.0,"publicationDate":"2004-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0065-3233(04)67005-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24399200","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
扫码关注我们
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号