다음과 같은 기능을 한번의 로그인으로 사용 할 수 있습니다.
NTIS 바로가기
Journal of molecular biology, v.307 no.1, 2001년, pp.1 - 8
Bieger, Boris (Max-Planck-Institute for Biochemistry, Department of Membrane Biochemistry, Am Klopferspitz 18a, D-82152 Martinsried, Germany) , Essen, Lars-Oliver (Corresponding author)
AI-Helper
AbstractAlkylhydroperoxide reductases (AhpR, EC 1.6.4.∗) are essential for the oxygen tolerance of aerobic organisms by converting otherwise toxic hydroperoxides of lipids or nucleic acids to the corresponding alcohols. The AhpF component belongs to the family of pyridine nucleotide-disulphid...
J. Biol. Chem. Jacobson 264 1488 1989 10.1016/S0021-9258(18)94214-6 An alkylhydroperoxide reductase from Salmonella typhimurium involved in the defense of DNA against oxidative damage
J. Biol. Chem. Tartaglia 265 10535 1990 10.1016/S0021-9258(18)86980-0 Alkyl hydroperoxide reductase from Salmonella typhimurium. Sequence and homology to thioredoxin reductase and other flavoprotein disulfide oxidoreductases
Biochemistry Calzi 36 13357 1997 10.1021/bi9713660 Requirement for the two Ahpf cystine disulfide centers in catalysis of peroxide reduction by alkyl hydroperoxide reductase
Biochemistry Ellis 36 13349 1997 10.1021/bi9713658 Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella Typhimurium
Proc. Natl Acad. Sci. USA Zhang 93 13212 1996 10.1073/pnas.93.23.13212 Molecular basis for the exquisite sensitivity of Mycobacterium tuberculosis to isoniazid
J. Mol. Biol. Dai 264 1044 1996 10.1006/jmbi.1996.0695 Crystal structure of Arabidopsis thaliana NADPH dependent thioredoxin reductase at 2.5 A resolution
Nature Kuriyan 352 172 1991 10.1038/352172a0 Convergent evolution of similar function in two structurally divergent enzymes
J. Mol. Biol. Waksman 236 800 1994 10.1006/jmbi.1994.1190 Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. Implications for a large conformational change during catalysis
Nature Struct. Biol. Ren 5 602 1998 10.1038/862 A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units
Biochemistry Poole 39 6602 2000 10.1021/bi000405w AhpF can be dissected into two functional units
Nature Schulz 273 120 1978 10.1038/273120a0 The structure of the flavoenzyme glutathione reductase
Fold. Des. Huber-Wunderlich 3 161 1998 10.1016/S1359-0278(98)00024-8 A single dipeptide sequence modulates the redox properties of a whole enzyme family
Biochemistry Poole 35 65 1996 10.1021/bi951888k Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 2. Cystine disulfides involved in catalysis of peroxide reduction
Protein Sci. Lennon 8 2366 1999 10.1110/ps.8.11.2366 Crystal structure of reduced thioredoxin reductase from Escherichia coli
Science Lennon 289 1190 2000 10.1126/science.289.5482.1190 Twists in catalysis
Biochemistry Wang 37 16378 1998 10.1021/bi980754e Thioredoxin reductase thioredoxin fusion enzyme from Mycobacterium leprae
Acta Crystallog. sect. D Bieger 56 92 2000 10.1107/S0907444999014146 Crystallization and preliminary X-ray analysis of the catalytic core of the alkylhydroperoxide reductase component AhpF from Escherichia coli
Methods Enzymol. Otwinowski 276 307 1997 10.1016/S0076-6879(97)76066-X Processing of X-ray diffraction data collected in oscillation mode
Acta Crystallog. sect. A Navaza A50 157 1994 10.1107/S0108767393007597 AMoRe
Nature Struct. Biol. Perrakis 6 458 1999 10.1038/8263 Automated protein model building combined with iterative structure refinement
Acta Crystallog. sect. D Brunger 54 905 1998 10.1107/S0907444998003254 Crystallography and NMR System - a new software suite for macromolecular structure determination
Acta Crystallog. sect. D 50 760 1994 10.1107/S0907444994003112 The CCP4 suite
Acta Crystallog. sect. A Engh 47 392 1991 10.1107/S0108767391001071 Accurate bond and angle parameters for X-ray protein-structure refinement
J. Appl. Crystallog. Kraulis 24 946 1991 10.1107/S0021889891004399 MOLSCRIPT
Acta Crystallog. sect. D Merritt 50 869 1994 10.1107/S0907444994006396 Raster3D version 2.0. A program for photorealistic molecular graphics
Nucl. Acids Res. Altschul 25 3389 1997 10.1093/nar/25.17.3389 Gapped BLAST and PSI-BLAST
Proteins: Struct. Funct. Genet. Sali 23 318 1995 10.1002/prot.340230306 Evaluation of comparative protein modeling by MODELLER
J. Appl. Crystallog. Laskowski 26 283 1993 10.1107/S0021889892009944 PROCHECK
*원문 PDF 파일 및 링크정보가 존재하지 않을 경우 KISTI DDS 시스템에서 제공하는 원문복사서비스를 사용할 수 있습니다.
Copyright KISTI. All Rights Reserved.
※ AI-Helper는 부적절한 답변을 할 수 있습니다.