In this issue - pv
doi:10.1038/nchembio1208-v

doi:10.1038/nchembio1208-715
How do we select papers for publication in Nature Chemical Biology?
Full Text - Decoding decisions | PDF (122 KB) - Decoding decisions
Matthew B Francis reviews Bioconjugate Techniques, 2nd edition by Greg T Hermanson
doi:10.1038/nchembio1208-717
Full Text - Updating the bioconjugation catalog | PDF (110 KB) - Updating the bioconjugation catalog
Jeffrey T. Borenstein
doi:10.1038/nchembio1208-718
Bacterial infections have long been associated with coagulation, but the mechanism is not well understood. New insights into bacterial spatial localization are shedding light on how bacterial clusters can trigger coagulation in a process known as 'quorum acting'.
Full Text - Acting together, bacterial clusters initiate coagulation | PDF (573 KB) - Acting together, bacterial clusters initiate coagulation
See also: Article by Kastrup et al.
Marco W Fraaije & Andrea Mattevi
doi:10.1038/nchembio1208-719
The berberine bridge enzyme catalyzes the crucial step in the biosynthesis of an important class of alkaloids through a reaction that cannot be carried out using conventional organic chemistry tools. Characterization of the enzyme demonstrates a concerted mechanism that couples two distinct chemical steps—oxidation and proton abstraction—affecting two separate groups of the substrate.
Full Text - Cyclization in concert | PDF (712 KB) - Cyclization in concert
See also: Brief Communication by Winkler et al.
Minoru Fukuda & Xingfeng Bao
doi:10.1038/nchembio1208-721
Cell-surface carbohydrates are synthesized in a step-wise fashion, yielding products with unique capping structures. A recent study has shown that carbohydrates at the cell surface can be further remodeled by an endogenous glycosidase to alter the carbohydrate structure, thus generating a new function.
Full Text - Seeing cellular sialidase transform sugars | PDF (575 KB) - Seeing cellular sialidase transform sugars
See also: Article by Gadhoum & Sackstein
Bing Qi & J Marie Hardwick
doi:10.1038/nchembio1208-722
Small-molecule inhibitors of anti-apoptotic Bcl-2 proteins and BH3 mimetic peptides are promising anticancer agents. A recent study identifies a Nur77-based peptide that converts anti-apoptotic Bcl-2 proteins into pro-apoptotic molecules, providing another potential cancer therapeutic strategy.
Full Text - Bcl-2 turns deadly | PDF (447 KB) - Bcl-2 turns deadly
Matthew D Disney
doi:10.1038/nchembio1208-723
Isoginkgetin has been identified as a general inhibitor of pre-mRNA splicing using an in vivo screening assay. This and related inhibitors will not only be useful as tools to decipher the roles of the individual components of the spliceosome but may also serve as therapeutics.
Full Text - Short-circuiting RNA splicing | PDF (628 KB) - Short-circuiting RNA splicing
David M J Lilley
doi:10.1038/nchembio1208-725
X-ray scattering from clusters of gold atoms provides a sensitive way of measuring long-range distance information in macromolecules and now reveals a surprisingly soft, stretchy character to double-stranded DNA.
doi:10.1038/nchembio1208-727
Full Text - Research highlights | PDF (106 KB) - Research highlights
Monika Fuxreiter, Peter Tompa, István Simon, Vladimir N Uversky, Jeffrey C Hansen & Francisco J Asturias
doi:10.1038/nchembio.127

Abstract - Malleable machines take shape in eukaryotic transcriptional regulation | Full Text - Malleable machines take shape in eukaryotic transcriptional regulation | PDF (747 KB) - Malleable machines take shape in eukaryotic transcriptional regulation
Andreas Winkler,
Andrzej
yskowski,
Sabrina Riedl,
Martin Puhl,
Toni M Kutchan,
Peter Macheroux
&
Karl Gruber
doi:10.1038/nchembio.123

Abstract - A concerted mechanism for berberine bridge enzyme | Full Text - A concerted mechanism for berberine bridge enzyme | PDF (311 KB) - A concerted mechanism for berberine bridge enzyme | Supplementary information | Chemical compounds
See also: News and Views by Fraaije & Mattevi
Christian J Kastrup, James Q Boedicker, Andrei P Pomerantsev, Mahtab Moayeri, Yao Bian, Rebecca R Pompano, Timothy R Kline, Patricia Sylvestre, Feng Shen, Stephen H Leppla, Wei-Jen Tang & Rustem F Ismagilov
doi:10.1038/nchembio.124

Abstract - Spatial localization of bacteria controls coagulation of human blood by 'quorum acting' | Full Text - Spatial localization of bacteria controls coagulation of human blood by 'quorum acting' | PDF (610 KB) - Spatial localization of bacteria controls coagulation of human blood by 'quorum acting' | Supplementary information | Chemical compounds
See also: News and Views by Borenstein
Samah Zeineb Gadhoum & Robert Sackstein
doi:10.1038/nchembio.116

Abstract - CD15 expression in human myeloid cell differentiation is regulated by sialidase activity | Full Text - CD15 expression in human myeloid cell differentiation is regulated by sialidase activity | PDF (339 KB) - CD15 expression in human myeloid cell differentiation is regulated by sialidase activity | Supplementary information | Chemical compounds
See also: News and Views by Fukuda & Bao
Abhishek Chatterjee, Yue Li, Yang Zhang, Tyler L Grove, Michael Lee, Carsten Krebs, Squire J Booker, Tadhg P Begley & Steven E Ealick
doi:10.1038/nchembio.121

Abstract - Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily | Full Text - Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily | PDF (587 KB) - Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily | Supplementary information | Chemical compounds
-Poly-L-lysine dispersity is controlled by a highly unusual nonribosomal peptide synthetase - pp766 - 772Kazuya Yamanaka, Chitose Maruyama, Hiroshi Takagi & Yoshimitsu Hamano
doi:10.1038/nchembio.125

Abstract - [epsi]-Poly-: L: -lysine dispersity is controlled by a highly unusual nonribosomal peptide synthetase | Full Text -
-Poly-L-lysine dispersity is controlled by a highly unusual nonribosomal peptide synthetase | PDF (541 KB) -
-Poly-L-lysine dispersity is controlled by a highly unusual nonribosomal peptide synthetase | Supplementary information | Chemical compounds
Nature Chemical Biology
ISSN: 1552-4450
EISSN: 1548-7105
