Pub Date : 2004-01-01DOI: 10.1016/S0065-3233(04)67006-9
Anthony N Imbalzano, Hengyi Xiao
{"title":"Functional properties of ATP-dependent chromatin remodeling enzymes.","authors":"Anthony N Imbalzano, Hengyi Xiao","doi":"10.1016/S0065-3233(04)67006-9","DOIUrl":"https://doi.org/10.1016/S0065-3233(04)67006-9","url":null,"abstract":"","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"67 ","pages":"157-79"},"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)67006-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24399201","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)69012-7
E. Friedberg
{"title":"Advances in Protein Chemistry: Preface","authors":"E. Friedberg","doi":"10.1016/S0065-3233(04)69012-7","DOIUrl":"https://doi.org/10.1016/S0065-3233(04)69012-7","url":null,"abstract":"","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"69 1","pages":""},"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)69012-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"55906237","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)67008-2
Adam Wood, Ali Shilatifard
{"title":"Posttranslational modifications of histones by methylation.","authors":"Adam Wood, Ali Shilatifard","doi":"10.1016/S0065-3233(04)67008-2","DOIUrl":"https://doi.org/10.1016/S0065-3233(04)67008-2","url":null,"abstract":"","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"67 ","pages":"201-22"},"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)67008-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24399203","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)68003-X
William A Barton, Juha-Pekka Himanen, Alexander Antipenko, Dimitar B Nikolov
{"title":"Structures of axon guidance molecules and their neuronal receptors.","authors":"William A Barton, Juha-Pekka Himanen, Alexander Antipenko, Dimitar B Nikolov","doi":"10.1016/S0065-3233(04)68003-X","DOIUrl":"https://doi.org/10.1016/S0065-3233(04)68003-X","url":null,"abstract":"","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"68 ","pages":"65-106"},"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)68003-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24777337","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)69007-3
Alexandra Vaisman, Alan R Lehmann, Roger Woodgate
{"title":"DNA polymerases eta and iota.","authors":"Alexandra Vaisman, Alan R Lehmann, Roger Woodgate","doi":"10.1016/S0065-3233(04)69007-3","DOIUrl":"https://doi.org/10.1016/S0065-3233(04)69007-3","url":null,"abstract":"","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"69 ","pages":"205-28"},"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)69007-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24853544","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)67004-5
Robyn D Moir, Ian M Willis
{"title":"Tetratricopeptide repeats of Tfc4 and a limiting step in the assembly of the initiation factor TFIIIB.","authors":"Robyn D Moir, Ian M Willis","doi":"10.1016/S0065-3233(04)67004-5","DOIUrl":"https://doi.org/10.1016/S0065-3233(04)67004-5","url":null,"abstract":"","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"67 ","pages":"93-121"},"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)67004-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24399199","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)68010-7
Elaine K Lau, Samantha Allen, Andro R Hsu, Tracy M Handel
A key feature of the immune system is the migration of leukocytes throughout the organism in an effort to patrol for infectious pathogens, tissue damage, and other physiological insults. This remarkable surveillance system is controlled by a family of proteins called chemokines (chemoattractant cytokines), and their respective receptors. Originally discovered because of their role in cell recruitment during inflammation, it is now well recognized that chemokines are also involved in other diverse processes including lymphocyte development and homing, organogenesis, and neuronal communication. While chemokines have evolved largely for host protection, their ability to induce cell damage and inappropriate cell recruitment, can lead to disease. Thus, there is considerable interest in developing antagonists. In this review we emphasize what is known about the structural biology of chemokines, chemokine receptors, and interactions with cell surface glycosaminoglycans. We also briefly describe their role in certain diseases and strategies for interfering with chemokine function that have emerged from mechanistic and structural understanding of their function. Finally we discuss viral mechanisms for sabotaging or manipulating the chemokine system, in part to illustrate the level of molecular mimicry that viruses have achieved and the evolutionary pressure imposed on the immune system by these pathogens.
{"title":"Chemokine-receptor interactions: GPCRs, glycosaminoglycans and viral chemokine binding proteins.","authors":"Elaine K Lau, Samantha Allen, Andro R Hsu, Tracy M Handel","doi":"10.1016/S0065-3233(04)68010-7","DOIUrl":"https://doi.org/10.1016/S0065-3233(04)68010-7","url":null,"abstract":"<p><p>A key feature of the immune system is the migration of leukocytes throughout the organism in an effort to patrol for infectious pathogens, tissue damage, and other physiological insults. This remarkable surveillance system is controlled by a family of proteins called chemokines (chemoattractant cytokines), and their respective receptors. Originally discovered because of their role in cell recruitment during inflammation, it is now well recognized that chemokines are also involved in other diverse processes including lymphocyte development and homing, organogenesis, and neuronal communication. While chemokines have evolved largely for host protection, their ability to induce cell damage and inappropriate cell recruitment, can lead to disease. Thus, there is considerable interest in developing antagonists. In this review we emphasize what is known about the structural biology of chemokines, chemokine receptors, and interactions with cell surface glycosaminoglycans. We also briefly describe their role in certain diseases and strategies for interfering with chemokine function that have emerged from mechanistic and structural understanding of their function. Finally we discuss viral mechanisms for sabotaging or manipulating the chemokine system, in part to illustrate the level of molecular mimicry that viruses have achieved and the evolutionary pressure imposed on the immune system by these pathogens.</p>","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"68 ","pages":"351-91"},"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)68010-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24776750","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)68002-8
Timothy A Springer, Jia-Huai Wang
Integrins are a structurally elaborate family of adhesion molecules that transmit signals bidirectionally across the plasma membrane by undergoing large-scale structural rearrangements. By regulating cell-cell and cell-matrix contacts, integrins participate in a wide-range of biological interactions including development, tissue repair, angiogenesis, inflammation and hemostasis. From a therapeutic standpoint, integrins are probably the most important class of cell adhesion receptors. Structural investigations on integrin-ligand interactions reveal remarkable features in molecular detail. These details include the atomic basis for divalent cation-dependent ligand binding and how conformational signals are propagated long distances from one domain to another between the cytoplasm and the extracellular ligand binding site that regulate affinity for ligand, and conversely, cytosolic signaling pathways.
{"title":"The three-dimensional structure of integrins and their ligands, and conformational regulation of cell adhesion.","authors":"Timothy A Springer, Jia-Huai Wang","doi":"10.1016/S0065-3233(04)68002-8","DOIUrl":"https://doi.org/10.1016/S0065-3233(04)68002-8","url":null,"abstract":"<p><p>Integrins are a structurally elaborate family of adhesion molecules that transmit signals bidirectionally across the plasma membrane by undergoing large-scale structural rearrangements. By regulating cell-cell and cell-matrix contacts, integrins participate in a wide-range of biological interactions including development, tissue repair, angiogenesis, inflammation and hemostasis. From a therapeutic standpoint, integrins are probably the most important class of cell adhesion receptors. Structural investigations on integrin-ligand interactions reveal remarkable features in molecular detail. These details include the atomic basis for divalent cation-dependent ligand binding and how conformational signals are propagated long distances from one domain to another between the cytoplasm and the extracellular ligand binding site that regulate affinity for ligand, and conversely, cytosolic signaling pathways.</p>","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"68 ","pages":"29-63"},"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)68002-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24777336","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)68006-5
Mark R Walter
{"title":"Structural analysis of IL-10 and Type I interferon family members and their complexes with receptor.","authors":"Mark R Walter","doi":"10.1016/S0065-3233(04)68006-5","DOIUrl":"https://doi.org/10.1016/S0065-3233(04)68006-5","url":null,"abstract":"","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"68 ","pages":"171-223"},"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)68006-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24777340","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)69003-6
Aziz Sancar
{"title":"Photolyase and cryptochrome blue-light photoreceptors.","authors":"Aziz Sancar","doi":"10.1016/S0065-3233(04)69003-6","DOIUrl":"https://doi.org/10.1016/S0065-3233(04)69003-6","url":null,"abstract":"","PeriodicalId":51216,"journal":{"name":"Advances in Protein Chemistry","volume":"69 ","pages":"73-100"},"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)69003-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"24853540","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}
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