In This Issue - pv
doi:10.1038/nchembio0606-v
doi:10.1038/nchembio0606-283
Full Text - Our paper anniversary | PDF (149 KB) - Our paper anniversary
Ryan Hili & Andrei K Yudin
doi:10.1038/nchembio0606-284
The function of many biologically active molecules requires the presence of carbon-nitrogen bonds in strategic positions. The biosynthetic pathways leading to such bonds can be bypassed through chemical synthesis to synthesize natural products more efficiently and also to generate the molecular diversity unavailable in nature.
Full Text - Making carbon-nitrogen bonds in biological and chemical synthesis | PDF (389 KB) - Making carbon-nitrogen bonds in biological and chemical synthesis
Jennifer J Kohler
doi:10.1038/nchembio0606-288
The field of chemical biology is now hitting its stride. Chemical biologists have developed essential tools that are being used to illuminate complex cellular events. The application of chemical principles to biological phenomena has revealed new opportunities for drug discovery. This report highlights recent progress and exciting new directions in chemical genetics and drug discovery.
Full Text - A century at the chemistry-biology interface | PDF (474 KB) - A century at the chemistry-biology interface
Joanne Kotz
doi:10.1038/nchembio0606-293
From research contributions in understanding the molecular details of enzyme catalysis to involvement in education and university administration, Jeremy Knowles offers a broad perspective on chemistry and chemical biology.
Perry A Frey
doi:10.1038/nchembio0606-294
Identifying the structures of transient intermediates is an essential step in the elucidation of an enzymatic reaction mechanism. Cryocrystallography reveals the structures of three thiamine diphosphate derivatives as intermediates in the action of pyruvate oxidase.
Full Text - Snapshots of three intermediates at the active site of pyruvate oxidase | PDF (116 KB) - Snapshots of three intermediates at the active site of pyruvate oxidase
See also: Letter by Wille et al.
Robert T Abraham
doi:10.1038/nchembio0606-295
When introduced into living cells, drugs frequently evoke unanticipated responses that are due either to off-target effects or to previously unknown interactions between the intended target and other biochemical pathways. The development of a panel of high-resolution sentinel assays for signal-transduction cascades in human cells promises to enhance the power of chemical genetics and increase the efficiency of drug-discovery research.
Full Text - Signalomic signatures enlighten drug profiling | PDF (125 KB) - Signalomic signatures enlighten drug profiling
See also: Article by MacDonald et al.
Ronald Wetzel
doi:10.1038/nchembio0606-297
In diseases linked to protein aggregation, the initiation of aggregation can be a critical point in the disease mechanism. New studies in cells expressing huntingtin exon I suggest that the initiation of polyglutamine aggregation proceeds by a simple nucleation mechanism.
Full Text - Nucleation of huntingtin aggregation in cells | PDF (334 KB) - Nucleation of huntingtin aggregation in cells
See also: Letter by Colby et al.
Daniel L Minor, Jr
doi:10.1038/nchembio0606-298
Because of their transmembrane nature, ion channels are notoriously difficult subjects for high-throughput screening approaches. A new method has been developed that provides a simple, elegant and rapid means for assaying channel function.
Full Text - Wanting contact: how to pick up a channel | PDF (544 KB) - Wanting contact: how to pick up a channel
See also: Letter by Holden et al.
Jay W Heinecke
doi:10.1038/nchembio0606-300
Human C-reactive protein (CRP) has been implicated in the inflammatory responses associated with heart attacks and strokes. A small-molecule inhibitor of CRP limits myocardial infarction in rats and should facilitate mechanistic studies of cardiovascular disease.
Full Text - Chemical knockout of C-reactive protein in cardiovascular disease | PDF (250 KB) - Chemical knockout of C-reactive protein in cardiovascular disease
doi:10.1038/nchembio0606-303
Full Text - Research Highlights | PDF (110 KB) - Research Highlights
Jason W Chin
doi:10.1038/nchembio789

Abstract - Modular approaches to expanding the functions of living matter | Full Text - Modular approaches to expanding the functions of living matter | PDF (309 KB) - Modular approaches to expanding the functions of living matter
Sunil Shaunak, Antony Godwin, Ji-Won Choi, Sibu Balan, Elisa Pedone, Damotharan Vijayarangam, Sibylle Heidelberger, Ian Teo, Mire Zloh & Steve Brocchini
doi:10.1038/nchembio786

Abstract - Site-specific PEGylation of native disulfide bonds in therapeutic proteins | Full Text - Site-specific PEGylation of native disulfide bonds in therapeutic proteins | PDF (168 KB) - Site-specific PEGylation of native disulfide bonds in therapeutic proteins | Supplementary information | Chemical compounds
Matthew A Holden, Lakmal Jayasinghe, Oliver Daltrop, Amy Mason & Hagan Bayley
doi:10.1038/nchembio793

First Paragraph - Direct transfer of membrane proteins from bacteria to planar bilayers for rapid screening by single-channel recording | Full Text - Direct transfer of membrane proteins from bacteria to planar bilayers for rapid screening by single-channel recording | PDF (404 KB) - Direct transfer of membrane proteins from bacteria to planar bilayers for rapid screening by single-channel recording | Supplementary information | Chemical compounds
David W Colby, John P Cassady, Grace C Lin, Vernon M Ingram & K Dane Wittrup
doi:10.1038/nchembio792

First Paragraph - Stochastic kinetics of intracellular huntingtin aggregate formation | Full Text - Stochastic kinetics of intracellular huntingtin aggregate formation | PDF (230 KB) - Stochastic kinetics of intracellular huntingtin aggregate formation | Supplementary information
Georg Wille, Danilo Meyer, Andrea Steinmetz, Erik Hinze, Ralph Golbik & Kai Tittmann
doi:10.1038/nchembio788

First Paragraph - The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography | Full Text - The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography | PDF (516 KB) - The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography | Supplementary information | Chemical compounds
Marnie L MacDonald, Jane Lamerdin, Stephen Owens, Brigitte H Keon, Graham K Bilter, Zhidi Shang, Zhengping Huang, Helen Yu, Jennifer Dias, Tomoe Minami, Stephen W Michnick & John K Westwick
doi:10.1038/nchembio790

Abstract - Identifying off-target effects and hidden phenotypes of drugs in human cells | Full Text - Identifying off-target effects and hidden phenotypes of drugs in human cells | PDF (693 KB) - Identifying off-target effects and hidden phenotypes of drugs in human cells | Supplementary information | Chemical compounds
David Kokel, Yehua Li, Jun Qin & Ding Xue
doi:10.1038/nchembio791

Abstract - The nongenotoxic carcinogens naphthalene and para-dichlorobenzene suppress apoptosis in Caenorhabditis elegans | Full Text - The nongenotoxic carcinogens naphthalene and para-dichlorobenzene suppress apoptosis in Caenorhabditis elegans | PDF (305 KB) - The nongenotoxic carcinogens naphthalene and para-dichlorobenzene suppress apoptosis in Caenorhabditis elegans | Supplementary information | Chemical compounds
Artem Y Lyubimov, Paula I Lario, Ibrahim Moustafa & Alice Vrielink
doi:10.1038/nchembio0606-346a
Full Text - Erratum: Atomic resolution crystallography reveals how changes in pH shape the protein microenvironment | PDF (52 KB) - Erratum: Atomic resolution crystallography reveals how changes in pH shape the protein microenvironment
-synuclein fibrilization - p346Daryl A Bosco, Douglas M Fowler, Qinghai Zhang, Jorge Nieva, Evan T Powers, Paul Wentworth, Jr, Richard A Lerner & Jeffery W Kelly
doi:10.1038/nchembio0606-346b
Full Text - Corrigendum: Elevated levels of oxidized cholesterol metabolites in Lewy body disease brains accelerate
-synuclein fibrilization | PDF (52 KB) - Corrigendum: Elevated levels of oxidized cholesterol metabolites in Lewy body disease brains accelerate
-synuclein fibrilization
Nature Chemical Biology
ISSN: 1552-4450
EISSN: 1548-7105
