核糖体蛋白。XXVII. 来自两种抗壮观霉素的大肠杆菌突变体的蛋白S5中氨基酸交换的定位。 - Suppr

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超能文献

Ribosomal proteins. XXVII. Localization of the amino acid exchanges in protein S5 from two Escherichia coli mutants resistant to spectinomycin.

作者信息

Funatsu G, Schiltz E, Wittmann H G

出版信息

Mol Gen Genet. 1972;114(2):106-11. doi: 10.1007/BF00332781.

DOI:10.1007/BF00332781

PMID:4553095

Abstract

摘要

相似文献

Ribosomal proteins. XXVII. Localization of the amino acid exchanges in protein S5 from two Escherichia coli mutants resistant to spectinomycin.核糖体蛋白。XXVII. 来自两种抗壮观霉素的大肠杆菌突变体的蛋白S5中氨基酸交换的定位。

Mol Gen Genet. 1972;114(2):106-11. doi: 10.1007/BF00332781.

Ribosomal proteins. XXII. Studies on the altered protein S5 from a spectinomycin-resistant mutant of Escherichia coli.核糖体蛋白。二十二。对来自大肠杆菌壮观霉素抗性突变体的改变的蛋白S5的研究。

J Mol Biol. 1972 Feb 28;64(1):201-9. doi: 10.1016/0022-2836(72)90329-4.

Localization of the amino-acid exchange in protein S5 from an Escherichia coli mutant resistant to spectinomycin.来自一株对壮观霉素耐药的大肠杆菌突变体中蛋白质S5氨基酸交换的定位。

Mol Gen Genet. 1973 Dec 31;127(3):273-6. doi: 10.1007/BF00333767.

Genetic studies of the ribosomal proteins in Escherichia coli. I. Mutants and strains having 30s ribosomal subunit with altered protein components.大肠杆菌核糖体蛋白的遗传学研究。I. 具有蛋白质成分改变的30S核糖体亚基的突变体和菌株。

Mol Gen Genet. 1969 Oct 13;105(2):113-21. doi: 10.1007/BF00445680.

Ribosomal proteins. XXI. Amino acid composition of the tryptic peptides isolated from proteins S4, S18 and S20 of Escherichia coli ribosomes.核糖体蛋白质。 XXI. 从大肠杆菌核糖体的蛋白质S4、S18和S20中分离出的胰蛋白酶肽段的氨基酸组成。

Hoppe Seylers Z Physiol Chem. 1971 Dec;352(12):1705-14. doi: 10.1515/bchm2.1971.352.2.1705.

Interaction of the cytoplasmic membrane and ribosomes in Escherichia coli; altered ribosomal proteins in sucrose-dependent spectinomycin-resistant mutants.大肠杆菌中细胞质膜与核糖体的相互作用；蔗糖依赖性壮观霉素抗性突变体中核糖体蛋白的改变

Mol Gen Genet. 1977 Sep 21;155(1):53-60. doi: 10.1007/BF00268560.

[Identification of the substitution amino acid responsible for resistance to spectinomycin in a mutant of Escherichia coli].[大肠杆菌突变体中对壮观霉素耐药的替代氨基酸的鉴定]

Arch Int Physiol Biochim. 1973 May;81(2):369.

Ribosomal proteins. XX. Isolation and analyses of the tryptic peptides of proteins S5 from strain K and B of Escherichia coli.核糖体蛋白。XX。大肠杆菌K株和B株中S5蛋白胰蛋白酶肽段的分离与分析。

Biochim Biophys Acta. 1971 Oct;251(1):44-53. doi: 10.1016/0005-2795(71)90057-2.

Amino acid replacement in the protein S5 from a spectinomycin resistant mutant of Bacillus subtilis.来自枯草芽孢杆菌壮观霉素抗性突变体的蛋白质S5中的氨基酸替换

Mol Gen Genet. 1976 Feb 27;144(1):39-42. doi: 10.1007/BF00277301.

Genetic studies of the ribosomal proteins in Escherichia coli. IV. Pattern of the alteration of ribosomal protein components in mutants resistant to spectinomycin or erythromycin in different strains of Escherichia coli.大肠杆菌核糖体蛋白的遗传学研究。IV. 不同大肠杆菌菌株中对壮观霉素或红霉素耐药的突变体核糖体蛋白成分的改变模式。

Mol Gen Genet. 1970;107(1):39-49. doi: 10.1007/BF00433222.

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The molecular basis for rRNA-dependent spectinomycin resistance in Nicotiana chloroplasts.rRNA 依赖性壮观霉素抗性在烟草叶绿体中的分子基础。

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Mutations conferring aminoglycoside and spectinomycin resistance in Borrelia burgdorferi.在伯氏疏螺旋体中赋予氨基糖苷类和壮观霉素抗性的突变

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Single ribosomal protein mutations in antibiotic-resistant bacteria analyzed by mass spectrometry.通过质谱分析抗生素抗性细菌中的单个核糖体蛋白突变。

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本文引用的文献

Ribosomal Protein Conferring Sensitivity to the Antibiotic Spectinomycin in Escherichia coli.赋予大肠杆菌对抗生素壮观霉素敏感性的核糖体蛋白

Science. 1969 Jul 4;165(3888):85-6. doi: 10.1126/science.165.3888.85.

Characterization of an amino-acid substitution leading to spectinomycin resistance in Escherichia coli.

FEBS Lett. 1971 Sep 15;17(1):21-22. doi: 10.1016/0014-5793(71)80553-7.

Protein chemical studies of two RNA viruses and their mutants.两种RNA病毒及其突变体的蛋白质化学研究。

Cold Spring Harb Symp Quant Biol. 1966;31:163-72. doi: 10.1101/sqb.1966.031.01.024.

Correlation of 30S ribosomal proteins of Escherichia coli isolated in different laboratories.不同实验室分离的大肠杆菌30S核糖体蛋白的相关性

Mol Gen Genet. 1971;111(4):327-33. doi: 10.1007/BF00569784.

Biochim Biophys Acta. 1971 Oct;251(1):44-53. doi: 10.1016/0005-2795(71)90057-2.

J Mol Biol. 1972 Feb 28;64(1):201-9. doi: 10.1016/0022-2836(72)90329-4.

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