In This Issue - p1
doi:10.1038/nchembio0605-1
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June 2005, Volume 1 No 1 pp1-59
About the coverTop of page
Editorial
A community of chemists and biologists - p3
doi:10.1038/nchembio0605-3
Full Text - A community of chemists and biologists | PDF (71 KB) - A community of chemists and biologists
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News and Views
Ribonucleic general acid - pp5 - 6
Scott A Strobel
doi:10.1038/nchembio0605-5
Ribozymes are enzymes comprised of RNA that fold into three-dimensional structures and that catalyze chemical reactions central to all cells. A new study shows that ribozymes, like proteins, may use general acid catalysis as part of their catalytic toolkit.
Full Text - Ribonucleic general acid | PDF (124 KB) - Ribonucleic general acid
See also: Article by Das & Piccirilli
Pulling NO out of thin air - pp6 - 7
Thomas G Spiro
doi:10.1038/nchembio0605-6
Nitric oxide signaling requires that the heme of soluble guanylate cyclase bind NO preferentially to O2. Engineering of the enzyme's active site reveals a molecular basis for NO binding selectivity.
Full Text - Pulling NO out of thin air | PDF (240 KB) - Pulling NO out of thin air
See also: Article by Boon et al.
Trp modification signals a quorum - pp7 - 8
Richard A Gibbs
doi:10.1038/nchembio0605-7
ComX is a post-translationally modified peptide involved in quorum sensing in Bacillus subtilis. The structure of ComX has now been shown to contain a geranylated tryptophan with an unusual tricyclic architecture.
Full Text - Trp modification signals a quorum | PDF (278 KB) - Trp modification signals a quorum
See also: Brief Communication by Okada et al.
Ending the prolonged life of cancer cells - pp8 - 9
Gerhard Wagner
doi:10.1038/nchembio0605-8
The fate of cells depends on a delicate balance of pro- and anti-apoptotic proteins. Small-molecule inhibitors of anti-apoptotic protein-protein interactions promote apoptosis in cancer cells.
Full Text - Ending the prolonged life of cancer cells | PDF (163 KB) - Ending the prolonged life of cancer cells
Research Highlights - p11
doi:10.1038/nchembio0605-11
Full Text - Research Highlights | PDF (139 KB) - Research Highlights
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Review
Chemistry in living systems - pp13 - 21
Jennifer A Prescher & Carolyn R Bertozzi
doi:10.1038/nchembio0605-13
Abstract - Chemistry in living systems | Full Text - Chemistry in living systems | PDF (772 KB) - Chemistry in living systems
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Brief Communication
Structure of the Bacillus subtilis quorum-sensing peptide pheromone ComX - pp23 - 24
Masahiro Okada, Isao Sato, Soo Jeong Cho, Hidehisa Iwata, Toshihiko Nishio, David Dubnau & Youji Sakagami
doi:10.1038/nchembio709
Abstract - Structure of the : Bacillus subtilis: quorum-sensing peptide pheromone ComX | Full Text - Structure of the Bacillus subtilis quorum-sensing peptide pheromone ComX | PDF (120 KB) - Structure of the Bacillus subtilis quorum-sensing peptide pheromone ComX | Supplementary information | Chemical compounds
See also: News and Views by Gibbs
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Letters
Molecular basis of inverse agonism in a G protein–coupled receptor - pp25 - 28
Jean-Pierre Vilardaga, Ralf Steinmeyer, Greg S Harms & Martin J Lohse
doi:10.1038/nchembio705
First Paragraph - Molecular basis of inverse agonism in a G protein-coupled receptor | Full Text - Molecular basis of inverse agonism in a G protein–coupled receptor | PDF (209 KB) - Molecular basis of inverse agonism in a G protein–coupled receptor | Supplementary information | Chemical compounds
Small-molecule inhibition of siderophore biosynthesis in Mycobacterium tuberculosis and Yersinia pestis - pp29 - 32
Julian A Ferreras, Jae-Sang Ryu, Federico Di Lello, Derek S Tan & Luis E N Quadri
doi:10.1038/nchembio706
First Paragraph - Small-molecule inhibition of siderophore biosynthesis in : Mycobacterium tuberculosis: and : Yersinia pestis | Full Text - Small-molecule inhibition of siderophore biosynthesis in Mycobacterium tuberculosis and Yersinia pestis | PDF (198 KB) - Small-molecule inhibition of siderophore biosynthesis in Mycobacterium tuberculosis and Yersinia pestis | Supplementary information | Chemical compounds
Activity-based probes that target diverse cysteine protease families - pp33 - 38
Daisuke Kato, Kelly M Boatright, Alicia B Berger, Tamim Nazif, Galia Blum, Ciara Ryan, Kareem A H Chehade, Guy S Salvesen & Matthew Bogyo
doi:10.1038/nchembio707
First Paragraph - Activity-based probes that target diverse cysteine protease families | Full Text - Activity-based probes that target diverse cysteine protease families | PDF (344 KB) - Activity-based probes that target diverse cysteine protease families | Supplementary information | Chemical compounds
Small-molecule ligand induces nucleotide flipping in (CAG)n trinucleotide repeats - pp39 - 43
Kazuhiko Nakatani, Shinya Hagihara, Yuki Goto, Akio Kobori, Masaki Hagihara, Gosuke Hayashi, Motoki Kyo, Makoto Nomura, Masaki Mishima & Chojiro Kojima
doi:10.1038/nchembio708
First Paragraph - Small-molecule ligand induces nucleotide flipping in (CAG): n: trinucleotide repeats | Full Text - Small-molecule ligand induces nucleotide flipping in (CAG)n trinucleotide repeats | PDF (499 KB) - Small-molecule ligand induces nucleotide flipping in (CAG)n trinucleotide repeats | Supplementary information | Chemical compounds
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Top of pageArticles
General acid catalysis by the hepatitis delta virus ribozyme - pp45 - 52
Subha R Das & Joseph A Piccirilli
doi:10.1038/nchembio703
Abstract - General acid catalysis by the hepatitis delta virus ribozyme | Full Text - General acid catalysis by the hepatitis delta virus ribozyme | PDF (443 KB) - General acid catalysis by the hepatitis delta virus ribozyme | Supplementary information
See also: News and Views by Strobel
A molecular basis for NO selectivity in soluble guanylate cyclase - pp53 - 59
Elizabeth M Boon, Shirley H Huang & Michael A Marletta
doi:10.1038/nchembio704
Abstract - A molecular basis for NO selectivity in soluble guanylate cyclase | Full Text - A molecular basis for NO selectivity in soluble guanylate cyclase | PDF (399 KB) - A molecular basis for NO selectivity in soluble guanylate cyclase
See also: News and Views by Spiro
