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1. 皮膚筋炎および多発性筋炎における間質性肺疾患：臨床症状および診断 interstitial lung disease in dermatomyositis and polymyositis clinical manifestations and diagnosis

English Journal

Functional assignment of KEOPS/EKC complex subunits in the biosynthesis of the universal t6A tRNA modification.

Perrochia L, Guetta D, Hecker A, Forterre P, Basta T.SourceInstitut de Génétique et Microbiologie, Université Paris-Sud, IFR115, UMR8621-CNRS, 91405 Orsay, France and Université de Lorraine, UMR 1136 INRA/Université de Lorraine Interactions Arbres-Microorganismes, Labex ARBRE, FR EFABA, Faculté des Sciences, 54500 Vandoeuvre, France.
Nucleic acids research.Nucleic Acids Res.2013 Nov 1;41(20):9484-99. doi: 10.1093/nar/gkt720. Epub 2013 Aug 14.
N(6)-threonylcarbamoyladenosine (t(6)A) is a universal tRNA modification essential for normal cell growth and accurate translation. In Archaea and Eukarya, the universal protein Sua5 and the conserved KEOPS/EKC complex together catalyze t(6)A biosynthesis. The KEOPS/EKC complex is composed of Kae1,
PMID 23945934

Structural Basis of the Promiscuous Inhibitor Susceptibility of Escherichia coli LpxC.

Lee CJ, Liang X, Gopalaswamy R, Najeeb J, Ark ED, Toone EJ, Zhou P.SourceDepartment of Biochemistry, Duke University Medical Center , Durham, North Carolina 27710, United States.
ACS chemical biology.ACS Chem Biol.2013 Oct 31. [Epub ahead of print]
The LpxC enzyme in the lipid A biosynthetic pathway is one of the most promising and clinically unexploited antibiotic targets for treatment of multidrug-resistant Gram-negative infections. Progress in medicinal chemistry has led to the discovery of potent LpxC inhibitors with a variety of chemical
PMID 24117400

Synthesis, structure, and antibiotic activity of aryl-substituted LpxC inhibitors.

Liang X, Lee CJ, Zhao J, Toone EJ, Zhou P.SourceDepartment of Chemistry, Duke University , Durham, North Carolina 27708, United States.
Journal of medicinal chemistry.J Med Chem.2013 Sep 12;56(17):6954-66. doi: 10.1021/jm4007774. Epub 2013 Aug 21.
The zinc-dependent deacetylase LpxC catalyzes the committed step of lipid A biosynthesis in Gram-negative bacteria and is a validated target for the development of novel antibiotics to combat multidrug-resistant Gram-negative infections. Many potent LpxC inhibitors contain an essential threonyl-hydr
PMID 23914798

D-Amino Acid Dipeptide Production Utilizing D-Alanine-D-Alanine Ligases with Novel Substrate Specificity(Enzymology, Protein Engineering, and Enzyme Technology)