Pub Date : 2015-11-19DOI: 10.1016/j.chembiol.2015.09.015
Devin K. Schweppe, C. Harding, J. Chavez, Xia Wu, Elizabeth R. Ramage, Pradeep K. Singh, C. Manoil, J. Bruce
{"title":"Host-Microbe Protein Interactions during Bacterial Infection.","authors":"Devin K. Schweppe, C. Harding, J. Chavez, Xia Wu, Elizabeth R. Ramage, Pradeep K. Singh, C. Manoil, J. Bruce","doi":"10.1016/j.chembiol.2015.09.015","DOIUrl":"https://doi.org/10.1016/j.chembiol.2015.09.015","url":null,"abstract":"","PeriodicalId":9772,"journal":{"name":"Chemistry & biology","volume":"26 1","pages":"1521-1530"},"PeriodicalIF":0.0,"publicationDate":"2015-11-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73101353","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 : 2015-11-19DOI: 10.1016/j.chembiol.2015.09.011
N. Petronikolou, S. Nair
{"title":"Biochemical Studies of Mycobacterial Fatty Acid Methyltransferase: A Catalyst for the Enzymatic Production of Biodiesel.","authors":"N. Petronikolou, S. Nair","doi":"10.1016/j.chembiol.2015.09.011","DOIUrl":"https://doi.org/10.1016/j.chembiol.2015.09.011","url":null,"abstract":"","PeriodicalId":9772,"journal":{"name":"Chemistry & biology","volume":"25 1","pages":"1480-1490"},"PeriodicalIF":0.0,"publicationDate":"2015-11-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78205156","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 : 2015-11-19DOI: 10.1016/j.chembiol.2015.10.005
Romila D. Gopalan, M. D. Del Borgo, A. Mechler, P. Perlmutter, M. Aguilar
{"title":"Geometrically Precise Building Blocks: the Self-Assembly of β-Peptides.","authors":"Romila D. Gopalan, M. D. Del Borgo, A. Mechler, P. Perlmutter, M. Aguilar","doi":"10.1016/j.chembiol.2015.10.005","DOIUrl":"https://doi.org/10.1016/j.chembiol.2015.10.005","url":null,"abstract":"","PeriodicalId":9772,"journal":{"name":"Chemistry & biology","volume":"58 1","pages":"1417-1423"},"PeriodicalIF":0.0,"publicationDate":"2015-11-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82315308","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 : 2015-11-19DOI: 10.1016/j.chembiol.2015.09.018
Ahmed M. Ali, Ahmed M. Ali, J. Reis, Yan Xia, A. Rashid, Valentina Mercaldo, B. Walters, Katherine E. Brechun, V. Borisenko, S. Josselyn, J. Karanicolas, G. Woolley
{"title":"Optogenetic Inhibitor of the Transcription Factor CREB.","authors":"Ahmed M. Ali, Ahmed M. Ali, J. Reis, Yan Xia, A. Rashid, Valentina Mercaldo, B. Walters, Katherine E. Brechun, V. Borisenko, S. Josselyn, J. Karanicolas, G. Woolley","doi":"10.1016/j.chembiol.2015.09.018","DOIUrl":"https://doi.org/10.1016/j.chembiol.2015.09.018","url":null,"abstract":"","PeriodicalId":9772,"journal":{"name":"Chemistry & biology","volume":"78 1","pages":"1531-1539"},"PeriodicalIF":0.0,"publicationDate":"2015-11-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82493619","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 : 2015-11-19DOI: 10.1016/j.chembiol.2015.09.014
Minyoung Park, Bjørn B. Sivertsen, Sylvia Els‐Heindl, T. Huber, B. Holst, A. Beck‐Sickinger, T. Schwartz, T. Sakmar
{"title":"Bioorthogonal Labeling of Ghrelin Receptor to Facilitate Studies of Ligand-Dependent Conformational Dynamics.","authors":"Minyoung Park, Bjørn B. Sivertsen, Sylvia Els‐Heindl, T. Huber, B. Holst, A. Beck‐Sickinger, T. Schwartz, T. Sakmar","doi":"10.1016/j.chembiol.2015.09.014","DOIUrl":"https://doi.org/10.1016/j.chembiol.2015.09.014","url":null,"abstract":"","PeriodicalId":9772,"journal":{"name":"Chemistry & biology","volume":"22 1","pages":"1431-1436"},"PeriodicalIF":0.0,"publicationDate":"2015-11-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72743083","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 : 2015-11-19DOI: 10.1016/j.chembiol.2015.09.017
C. Olea, J. Weidmann, P. Dawson, G. F. Joyce
{"title":"An L-RNA Aptamer that Binds and Inhibits RNase.","authors":"C. Olea, J. Weidmann, P. Dawson, G. F. Joyce","doi":"10.1016/j.chembiol.2015.09.017","DOIUrl":"https://doi.org/10.1016/j.chembiol.2015.09.017","url":null,"abstract":"","PeriodicalId":9772,"journal":{"name":"Chemistry & biology","volume":"55 1","pages":"1437-1441"},"PeriodicalIF":0.0,"publicationDate":"2015-11-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89078438","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 : 2015-11-19DOI: 10.1016/j.chembiol.2015.09.013
Carole Urbach, N. Gordon, I. Strickland, D. Lowne, C. Joberty-Candotti, R. May, A. Herath, D. Hijnen, J. Thijs, C. Bruijnzeel-Koomen, R. Minter, F. Hollfelder, L. Jermutus
{"title":"Combinatorial Screening Identifies Novel Promiscuous Matrix Metalloproteinase Activities that Lead to Inhibition of the Therapeutic Target IL-13.","authors":"Carole Urbach, N. Gordon, I. Strickland, D. Lowne, C. Joberty-Candotti, R. May, A. Herath, D. Hijnen, J. Thijs, C. Bruijnzeel-Koomen, R. Minter, F. Hollfelder, L. Jermutus","doi":"10.1016/j.chembiol.2015.09.013","DOIUrl":"https://doi.org/10.1016/j.chembiol.2015.09.013","url":null,"abstract":"","PeriodicalId":9772,"journal":{"name":"Chemistry & biology","volume":"64 1","pages":"1442-1452"},"PeriodicalIF":0.0,"publicationDate":"2015-11-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89083499","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 : 2015-10-22Epub Date: 2015-10-01DOI: 10.1016/j.chembiol.2015.08.012
Elwira Sieniawska
Tuberculosis (TB) is a recurring threat to contemporary civilization. It affects not only those within developing countries, but has also appeared again in places where it was once considered eradicated. TB co-infection in patients infected by HIV is, at the time of writing, the most common cause of death. In the field of searching for new antimycobacterial drug leads, compounds of natural origin still remain a promising source. The review is intended to gather information about natural products (metabolites of plants, fungi, bacteria, and marine sponges) that show activity against mycobacterial enzymes. Here, natural metabolites are presented as being inhibitors/activators of the mycobacterial enzymes involved in mycobacterial growth in vitro (ClpC1, ClpP, MurE ligase, mycothiol S-conjugate amidase, β-ketoacyl-ACP synthase, InhA) and in vivo, as regards the host cell (PtpB). Each enzyme is briefly described so as to generate an understanding of its role in mycobacterial growth and engender a perception of the mechanism of action of the studied natural compounds. Furthermore, after the introduction of the enzyme, its inhibitors are listed and exactly characterized.
{"title":"RETRACTED: Targeting Mycobacterial Enzymes with Natural Products.","authors":"Elwira Sieniawska","doi":"10.1016/j.chembiol.2015.08.012","DOIUrl":"https://doi.org/10.1016/j.chembiol.2015.08.012","url":null,"abstract":"<p><p>Tuberculosis (TB) is a recurring threat to contemporary civilization. It affects not only those within developing countries, but has also appeared again in places where it was once considered eradicated. TB co-infection in patients infected by HIV is, at the time of writing, the most common cause of death. In the field of searching for new antimycobacterial drug leads, compounds of natural origin still remain a promising source. The review is intended to gather information about natural products (metabolites of plants, fungi, bacteria, and marine sponges) that show activity against mycobacterial enzymes. Here, natural metabolites are presented as being inhibitors/activators of the mycobacterial enzymes involved in mycobacterial growth in vitro (ClpC1, ClpP, MurE ligase, mycothiol S-conjugate amidase, β-ketoacyl-ACP synthase, InhA) and in vivo, as regards the host cell (PtpB). Each enzyme is briefly described so as to generate an understanding of its role in mycobacterial growth and engender a perception of the mechanism of action of the studied natural compounds. Furthermore, after the introduction of the enzyme, its inhibitors are listed and exactly characterized.</p>","PeriodicalId":9772,"journal":{"name":"Chemistry & biology","volume":"22 10","pages":"1288-300"},"PeriodicalIF":0.0,"publicationDate":"2015-10-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.chembiol.2015.08.012","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"34235990","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 : 2015-10-22DOI: 10.1016/j.chembiol.2015.09.007
Jeung-Hoi Ha, Joshua M Karchin, Nancy Walker-Kopp, Carlos A Castañeda, Stewart N Loh
Domain swapping occurs when identical proteins exchange segments in reciprocal fashion. Natural swapping mechanisms remain poorly understood, and engineered swapping has the potential for creating self-assembling biomaterials that encode for emergent functions. We demonstrate that induced swapping can be used to regulate the function of a target protein. Swapping is triggered by inserting a "lever" protein (ubiquitin) into one of four loops of the ribose binding protein (RBP) target. The lever splits the target, forcing RBP to refold in trans to generate swapped oligomers. Identical RBP-ubiquitin fusions form homo-swapped complexes with the ubiquitin domain acting as the hinge. Surprisingly, some pairs of non-identical fusions swap more efficiently with each other than they do with themselves. Nuclear magnetic resonance experiments reveal that the hinge of these hetero-swapped complexes maps to a region of RBP distant from both ubiquitins. This design is expected to be applicable to other proteins to convert them into functional switches.
{"title":"Engineered Domain Swapping as an On/Off Switch for Protein Function.","authors":"Jeung-Hoi Ha, Joshua M Karchin, Nancy Walker-Kopp, Carlos A Castañeda, Stewart N Loh","doi":"10.1016/j.chembiol.2015.09.007","DOIUrl":"https://doi.org/10.1016/j.chembiol.2015.09.007","url":null,"abstract":"<p><p>Domain swapping occurs when identical proteins exchange segments in reciprocal fashion. Natural swapping mechanisms remain poorly understood, and engineered swapping has the potential for creating self-assembling biomaterials that encode for emergent functions. We demonstrate that induced swapping can be used to regulate the function of a target protein. Swapping is triggered by inserting a \"lever\" protein (ubiquitin) into one of four loops of the ribose binding protein (RBP) target. The lever splits the target, forcing RBP to refold in trans to generate swapped oligomers. Identical RBP-ubiquitin fusions form homo-swapped complexes with the ubiquitin domain acting as the hinge. Surprisingly, some pairs of non-identical fusions swap more efficiently with each other than they do with themselves. Nuclear magnetic resonance experiments reveal that the hinge of these hetero-swapped complexes maps to a region of RBP distant from both ubiquitins. This design is expected to be applicable to other proteins to convert them into functional switches. </p>","PeriodicalId":9772,"journal":{"name":"Chemistry & biology","volume":"22 10","pages":"1384-93"},"PeriodicalIF":0.0,"publicationDate":"2015-10-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.chembiol.2015.09.007","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"34113645","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2015-10-22DOI: 10.1016/j.chembiol.2015.09.008
Daniel Medina-Cleghorn, Leslie A Bateman, Breanna Ford, Ann Heslin, Karl J Fisher, Esha D Dalvie, Daniel K Nomura
We are exposed to a growing number of chemicals in our environment, most of which have not been characterized in terms of their toxicological potential or mechanisms. Here, we employ a chemoproteomic platform to map the cysteine reactivity of environmental chemicals using reactivity-based probes to mine for hyper-reactive hotspots across the proteome. We show that environmental contaminants such as monomethylarsonous acid and widely used pesticides such as chlorothalonil and chloropicrin possess common reactivity with a distinct set of proteins. Many of these proteins are involved in key metabolic processes, suggesting that these targets may be particularly sensitive to environmental electrophiles. We show that the widely used fungicide chlorothalonil specifically inhibits several metabolic enzymes involved in fatty acid metabolism and energetics, leading to dysregulated lipid metabolism in mice. Our results underscore the utility of using reactivity-based chemoproteomic platforms to uncover novel mechanistic insights into the toxicity of environmental chemicals.
{"title":"Mapping Proteome-Wide Targets of Environmental Chemicals Using Reactivity-Based Chemoproteomic Platforms.","authors":"Daniel Medina-Cleghorn, Leslie A Bateman, Breanna Ford, Ann Heslin, Karl J Fisher, Esha D Dalvie, Daniel K Nomura","doi":"10.1016/j.chembiol.2015.09.008","DOIUrl":"https://doi.org/10.1016/j.chembiol.2015.09.008","url":null,"abstract":"<p><p>We are exposed to a growing number of chemicals in our environment, most of which have not been characterized in terms of their toxicological potential or mechanisms. Here, we employ a chemoproteomic platform to map the cysteine reactivity of environmental chemicals using reactivity-based probes to mine for hyper-reactive hotspots across the proteome. We show that environmental contaminants such as monomethylarsonous acid and widely used pesticides such as chlorothalonil and chloropicrin possess common reactivity with a distinct set of proteins. Many of these proteins are involved in key metabolic processes, suggesting that these targets may be particularly sensitive to environmental electrophiles. We show that the widely used fungicide chlorothalonil specifically inhibits several metabolic enzymes involved in fatty acid metabolism and energetics, leading to dysregulated lipid metabolism in mice. Our results underscore the utility of using reactivity-based chemoproteomic platforms to uncover novel mechanistic insights into the toxicity of environmental chemicals. </p>","PeriodicalId":9772,"journal":{"name":"Chemistry & biology","volume":"22 10","pages":"1394-405"},"PeriodicalIF":0.0,"publicationDate":"2015-10-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.chembiol.2015.09.008","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"34113646","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","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