Chemistry & biology最新文献_第3页

Host-Microbe Protein Interactions during Bacterial Infection. 细菌感染期间宿主-微生物蛋白的相互作用。

Chemistry & biology Pub Date : 2015-11-19 DOI: 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

引用次数: 97

Biochemical Studies of Mycobacterial Fatty Acid Methyltransferase: A Catalyst for the Enzymatic Production of Biodiesel. 分枝杆菌脂肪酸甲基转移酶的生化研究:酶法生产生物柴油的催化剂。

Chemistry & biology Pub Date : 2015-11-19 DOI: 10.1016/j.chembiol.2015.09.011

N. Petronikolou, S. Nair

引用次数: 15

Geometrically Precise Building Blocks: the Self-Assembly of β-Peptides. 几何上精确的构建模块:β-肽的自组装。

Chemistry & biology Pub Date : 2015-11-19 DOI: 10.1016/j.chembiol.2015.10.005

Romila D. Gopalan, M. D. Del Borgo, A. Mechler, P. Perlmutter, M. Aguilar

引用次数: 57

Optogenetic Inhibitor of the Transcription Factor CREB. 转录因子CREB的光遗传抑制剂。

Chemistry & biology Pub Date : 2015-11-19 DOI: 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

引用次数: 35

Bioorthogonal Labeling of Ghrelin Receptor to Facilitate Studies of Ligand-Dependent Conformational Dynamics. Ghrelin受体的生物正交标记促进配体依赖性构象动力学研究。

Chemistry & biology Pub Date : 2015-11-19 DOI: 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

引用次数: 17

An L-RNA Aptamer that Binds and Inhibits RNase. 结合和抑制rna酶的L-RNA适体。

Chemistry & biology Pub Date : 2015-11-19 DOI: 10.1016/j.chembiol.2015.09.017

C. Olea, J. Weidmann, P. Dawson, G. F. Joyce

引用次数: 19

Combinatorial Screening Identifies Novel Promiscuous Matrix Metalloproteinase Activities that Lead to Inhibition of the Therapeutic Target IL-13. 组合筛选鉴定新的混杂基质金属蛋白酶活性，导致抑制治疗靶点IL-13。

Chemistry & biology Pub Date : 2015-11-19 DOI: 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

引用次数: 7

RETRACTED: Targeting Mycobacterial Enzymes with Natural Products. 撤回:用天然产物靶向分枝杆菌酶。

Chemistry & biology Pub Date : 2015-10-22 Epub Date: 2015-10-01 DOI: 10.1016/j.chembiol.2015.08.012

Elwira Sieniawska

{"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":"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.","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}

引用次数: 9

Engineered Domain Swapping as an On/Off Switch for Protein Function. 工程结构域交换作为蛋白质功能的开关。

Chemistry & biology Pub Date : 2015-10-22 DOI: 10.1016/j.chembiol.2015.09.007

Jeung-Hoi Ha, Joshua M Karchin, Nancy Walker-Kopp, Carlos A Castañeda, Stewart N Loh

{"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":"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. ","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}

引用次数: 26

Mapping Proteome-Wide Targets of Environmental Chemicals Using Reactivity-Based Chemoproteomic Platforms. 利用基于反应性的化学蛋白质组学平台绘制环境化学物质的蛋白质组靶标。

Chemistry & biology Pub Date : 2015-10-22 DOI: 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

{"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":"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. ","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}

引用次数: 35