Focus on metals

In this issue - pv

doi:10.1038/nchembio0308-v

Full Text - In this issue | PDF (158 KB) - In this issue

Focus on metals

Metals in chemical biology - p143

doi:10.1038/nchembio0308-143

As scientists move towards a more comprehensive understanding of the role of metals in biology, bioinorganic chemistry will be an increasingly important component of chemical biology.

Full Text - Metals in chemical biology | PDF (220 KB) - Metals in chemical biology

Focus on metals

Assembling the pieces - pp145 - 147

Dennis J Thiele & Jonathan D Gitlin

doi:10.1038/nchembio0308-145

Abstract - Assembling the pieces | Full Text - Assembling the pieces | PDF (260 KB) - Assembling the pieces

Focus on metals

A place for thioether chemistry in cellular copper ion recognition and trafficking - pp148 - 151

Anna V Davis & Thomas V O'Halloran

doi:10.1038/nchembio0308-148

Abstract - A place for thioether chemistry in cellular copper ion recognition and trafficking | Full Text - A place for thioether chemistry in cellular copper ion recognition and trafficking | PDF (525 KB) - A place for thioether chemistry in cellular copper ion recognition and trafficking

Focus on metals

Expanding chemical biology of 2-oxoglutarate oxygenases - pp152 - 156

Christoph Loenarz & Christopher J Schofield

doi:10.1038/nchembio0308-152

Abstract - Expanding chemical biology of 2-oxoglutarate oxygenases | Full Text - Expanding chemical biology of 2-oxoglutarate oxygenases | PDF (478 KB) - Expanding chemical biology of 2-oxoglutarate oxygenases

Focus on metals

Ivano Bertini - p157

Joanne Kotz

doi:10.1038/nchembio0308-157

Building on his contributions to NMR methodologies for studying metalloproteins, Bertini has been instrumental in bringing together inorganic chemists and biologists interested in metals in biology.

Full Text - Ivano Bertini | PDF (90 KB) - Ivano Bertini

Delivery of tailor-made cobalamin to methylmalonyl-CoA mutase - pp158 - 159

Vahe Bandarian

doi:10.1038/nchembio0308-158

Methylmalonyl coenzyme A mutase (MCM) catalyzes the adenosylcobalamin-dependent isomerization of methylmalonyl-CoA to succinyl-CoA. Adenosyltransferase, an enzyme that carries out the final step in biosynthesis of adenosylcobalamin, is shown to be involved in delivery of the cofactor to MCM.

Full Text - Delivery of tailor-made cobalamin to methylmalonyl-CoA mutase | PDF (219 KB) - Delivery of tailor-made cobalamin to methylmalonyl-CoA mutase

See also: Brief Communication by Padovani et al.

Aggregator compounds confound amyloid fibrillization assay - pp159 - 160

Gilbert M Rishton

doi:10.1038/nchembio0308-159

The highly sensitive and artificial biochemical assays that enable high-throughput screening are vulnerable to artifact-generating compounds that occur in drug screening collections. An investigation of known aggregator compounds and amyloid fibrillization inhibitors suggests that such inhibitors operate via a nonspecific mechanism in a well-used assay of amyloid fibrillization.

Full Text - Aggregator compounds confound amyloid fibrillization assay | PDF (272 KB) - Aggregator compounds confound amyloid fibrillization assay

See also: Brief Communication by Feng et al.

Arresting malaria parasite egress from infected red blood cells - pp161 - 162

Marcus C S Lee & David A Fidock

doi:10.1038/nchembio0308-161

The escape of mature malaria parasites from the confines of their host red blood cells is an essential yet poorly understood process. Recent studies now highlight a key role for parasite proteases that trigger the degradation of parasite and host membranes, leading to the egress of infectious parasite forms.

Full Text - Arresting malaria parasite egress from infected red blood cells | PDF (980 KB) - Arresting malaria parasite egress from infected red blood cells

See also: Article by Arastu-Kapur et al.

It's a mod mod tRNA world - pp162 - 164

Richard J Maraia, Nathan H Blewett & Mark A Bayfield

doi:10.1038/nchembio0308-162

Postsynthetic modifications are widespread in genetic regulation. Trm9-mediated modification of the anticodon wobble base of specific tRNAs modulates expression of DNA damage response mRNAs in which cognate codons are unusually overrepresented. Thus, modification-dependent tRNA decoding activity is keyed to codon use in a genetic program.

Full Text - It's a mod mod tRNA world | PDF (958 KB) - It's a mod mod tRNA world

Looking at membrane lipids from the inside of the cell - pp164 - 165

J Antoinette Killian

doi:10.1038/nchembio0308-164

A novel biosensor developed to visualize phosphatidylserine in intact cells suggests a new role for the anionic lipid in specifying intracellular membranes involved in signaling events.

Full Text - Looking at membrane lipids from the inside of the cell | PDF (562 KB) - Looking at membrane lipids from the inside of the cell

Research highlights - p167

doi:10.1038/nchembio0308-167

Full Text - Research highlights | PDF (147 KB) - Research highlights

Focus on metals

Synthetic fluorescent sensors for studying the cell biology of metals - pp168 - 175

Dylan W Domaille, Emily L Que & Christopher J Chang

doi:10.1038/nchembio.69

Abstract - Synthetic fluorescent sensors for studying the cell biology of metals | Full Text - Synthetic fluorescent sensors for studying the cell biology of metals | PDF (635 KB) - Synthetic fluorescent sensors for studying the cell biology of metals

Focus on metals

Mechanisms for copper acquisition, distribution and regulation - pp176 - 185

Byung-Eun Kim, Tracy Nevitt & Dennis J Thiele

doi:10.1038/nchembio.72

Abstract - Mechanisms for copper acquisition, distribution and regulation | Full Text - Mechanisms for copper acquisition, distribution and regulation | PDF (6,022 KB) - Mechanisms for copper acquisition, distribution and regulation

Focus on metals

Versatility of biological non-heme Fe(II) centers in oxygen activation reactions - pp186 - 193

Elena G Kovaleva & John D Lipscomb

doi:10.1038/nchembio.71

Abstract - Versatility of biological non-heme Fe(II) centers in oxygen activation reactions | Full Text - Versatility of biological non-heme Fe(II) centers in oxygen activation reactions | PDF (637 KB) - Versatility of biological non-heme Fe(II) centers in oxygen activation reactions