In this issue - pv
doi:10.1038/nchembio0508-v
Table of contents
May 2008, Volume 4 No 5 pp265-321
About the coverTop of page
Editorial
Connecting the dots - p265
doi:10.1038/nchembio0508-265
New tools and rigorous chemical and biological studies will be essential for enhancing our mechanistic understanding of cellular oxidative stress.
Full Text - Connecting the dots | PDF (123 KB) - Connecting the dots
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Book Review
Refocusing redox biochemistry - p267
Matthew J Wood reviews Redox Biochemistry by Ruma Banerjee, Donald Becker, Martin Dickman, Vadim Gladyshev & Stephen Ragsdale
doi:10.1038/nchembio0508-267
Full Text - Refocusing redox biochemistry | PDF (97 KB) - Refocusing redox biochemistry
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News and Views
-Mannoside hydrolysis goes by boat - pp269 - 270
Monica M Palcic
doi:10.1038/nchembio0508-269
Enzymatic hydrolysis of 
-mannosides was predicted to occur via an unusual boat transition state conformation. Structural and biochemical studies on transition state mimics of a retaining -mannosidase now provide evidence for the predicted B2,5 transition state conformation.
Full Text - -Mannoside hydrolysis goes by boat | PDF (226 KB) - -Mannoside hydrolysis goes by boat
See also: Article by Tailford et al.
Engineering protease specificity made simple, but not simpler - pp270 - 271
Enrico Di Cera
doi:10.1038/nchembio0508-270
Engineering protease specificity has been a long sought research goal. New findings on OmpT, an outer membrane protease from Escherichia coli, reveal the remarkable success of a simple strategy.
Full Text - Engineering protease specificity made simple, but not simpler | PDF (297 KB) - Engineering protease specificity made simple, but not simpler
See also: Article by Varadarajan et al.
Encoding synthetic polymers - pp272 - 273
Jan C M van Hest
doi:10.1038/nchembio0508-272
DNA is the blueprint for life; it enables nature to pass on information from one DNA strand to the other, create mRNA with high accuracy and make proteins with absolute control over the sequence of the amino acid building blocks. A new paper now adds another templating function to the list: the programmed construction of synthetic polymers.
Full Text - Encoding synthetic polymers | PDF (280 KB) - Encoding synthetic polymers
Do-it-yourself enzymes - pp273 - 275
Vikas Nanda
doi:10.1038/nchembio0508-273
Enzymes have long captivated biologists and chemists by performing difficult reactions rapidly and selectively in aqueous environments. The designs of enzymes catalyzing a retro-aldol reaction and a Kemp elimination demonstrate that complex, biochemically novel reactions can be achieved using cutting-edge computational methods.
Full Text - Do-it-yourself enzymes | PDF (466 KB) - Do-it-yourself enzymes
Breaking the barriers of translation - pp275 - 276
Scott C Blanchard
doi:10.1038/nchembio0508-275
New data from single-molecule optical trapping methods provide exciting clues as to the underlying mechanism of ribosome translocation along mRNA and a powerful new approach for future investigations of translation regulation.
Full Text - Breaking the barriers of translation | PDF (254 KB) - Breaking the barriers of translation
Research highlights - p277
doi:10.1038/nchembio0508-277
Full Text - Research highlights | PDF (126 KB) - Research highlights
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Review
Reconciling the chemistry and biology of reactive oxygen species - pp278 - 286
Christine C Winterbourn
doi:10.1038/nchembio.85
Abstract - Reconciling the chemistry and biology of reactive oxygen species | Full Text - Reconciling the chemistry and biology of reactive oxygen species | PDF (759 KB) - Reconciling the chemistry and biology of reactive oxygen species
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Brief Communication
Single-molecule analysis of human telomerase monomer - pp287 - 289
David Alves, Haitao Li, Rosalind Codrington, Angel Orte, Xiaojun Ren, David Klenerman & Shankar Balasubramanian
doi:10.1038/nchembio.82
Abstract - Single-molecule analysis of human telomerase monomer | Full Text - Single-molecule analysis of human telomerase monomer | PDF (232 KB) - Single-molecule analysis of human telomerase monomer | Supplementary information
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Structural and biochemical evidence for a boat-like transition state in
Top of pageArticles
Highly active and selective endopeptidases with programmed substrate specificities - pp290 - 294
Navin Varadarajan, Sarah Rodriguez, Bum-Yeol Hwang, George Georgiou & Brent L Iverson
doi:10.1038/nchembio.80
Abstract - Highly active and selective endopeptidases with programmed substrate specificities | Full Text - Highly active and selective endopeptidases with programmed substrate specificities | PDF (263 KB) - Highly active and selective endopeptidases with programmed substrate specificities | Supplementary information
See also: News and Views by Di Cera
Novel targets for Huntington's disease in an mTOR-independent autophagy pathway - pp295 - 305
Andrea Williams, Sovan Sarkar, Paul Cuddon, Evangelia K Ttofi, Shinji Saiki, Farah H Siddiqi, Luca Jahreiss, Angeleen Fleming, Dean Pask, Paul Goldsmith, Cahir J O'Kane, Rodrigo Andres Floto & David C Rubinsztein
doi:10.1038/nchembio.79
Abstract - Novel targets for Huntington's disease in an mTOR-independent autophagy pathway | Full Text - Novel targets for Huntington's disease in an mTOR-independent autophagy pathway | PDF (445 KB) - Novel targets for Huntington's disease in an mTOR-independent autophagy pathway | Supplementary information | Chemical compounds
Structural and biochemical evidence for a boat-like transition state in -mannosidases - pp306 - 312
Louise E Tailford, Wendy A Offen, Nicola L Smith, Claire Dumon, Carl Morland, Julie Gratien, Marie-Pierre Heck, Robert V Stick, Yves Blériot, Andrea Vasella, Harry J Gilbert & Gideon J Davies
doi:10.1038/nchembio.81
Abstract - Structural and biochemical evidence for a boat-like transition state in [beta]-mannosidases | Full Text - Structural and biochemical evidence for a boat-like transition state in -mannosidases | PDF (435 KB) - Structural and biochemical evidence for a boat-like transition state in -mannosidases | Supplementary information | Chemical compounds
See also: News and Views by Palcic
Identification of RIP1 kinase as a specific cellular target of necrostatins - pp313 - 321
Alexei Degterev, Junichi Hitomi, Megan Germscheid, Irene L Ch'en, Olga Korkina, Xin Teng, Derek Abbott, Gregory D Cuny, Chengye Yuan, Gerhard Wagner, Stephen M Hedrick, Scott A Gerber, Alexey Lugovskoy & Junying Yuan
doi:10.1038/nchembio.83
Abstract - Identification of RIP1 kinase as a specific cellular target of necrostatins | Full Text - Identification of RIP1 kinase as a specific cellular target of necrostatins | PDF (531 KB) - Identification of RIP1 kinase as a specific cellular target of necrostatins | Supplementary information | Chemical compounds
