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Literature DB >> 14015715

Suppressor gene alteration of protein primary structure.

S BRODY, C YANOFSKY.

Abstract

Keywords: ESCHERICHIA COLI; LIGASES; TRYPTOPHAN

Mesh：

Substances：
Tryptophan
Ligases

Year: 1963 PMID： 14015715 PMCID： PMC300646 DOI： 10.1073/pnas.50.1.9

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

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14 in total

1. Peptide pattern studies on the wild-type A protein of the tryptophan synthetase of Escherichia coli.

Authors: D R HELINSKI; C YANOFSKY
Journal: Biochim Biophys Acta Date: 1962-09-10

2. Correspondence between genetic data and the position of amino acid alteration in a proein.

Authors: D R HELINSKI; C YANOFSKY
Journal: Proc Natl Acad Sci U S A Date: 1962-02 Impact factor: 11.205

3. An alteration in the primary structure of a protein predicted on the basis of genetic recombination data.

Authors: U HENNING; C YANOFSKY
Journal: Proc Natl Acad Sci U S A Date: 1962-02 Impact factor: 11.205

4. The A protein of the tryptophan synthetase of Escherichia coli. Purification, crystallization, and composition studies.

Authors: U HENNING; D R HELINSKI; F C CHAO; C YANOFSKY
Journal: J Biol Chem Date: 1962-05 Impact factor: 5.157

5. Identification of the triose phosphate formed in the tryptophan synthetase reaction.

Authors: I P CRAWFORD
Journal: Biochim Biophys Acta Date: 1960-12-04

6. The properties of altered proteins from mutants bearing one or two lesions in the same gene.

Authors: B D MALING; C YANOFSKY
Journal: Proc Natl Acad Sci U S A Date: 1961-04-15 Impact factor: 11.205

7. Transduction of linked genetic characters of the host by bacteriophage P1.

Authors: E S LENNOX
Journal: Virology Date: 1955-07 Impact factor: 3.616

8. THE FORMATION OF A NEW ENZYMATICALLY ACTIVE PROTEIN AS A RESULT OF SUPPRESSION.

Authors: I P Crawford; C Yanofsky
Journal: Proc Natl Acad Sci U S A Date: 1959-08 Impact factor: 11.205

9. AMBIVALENT rII MUTANTS OF PHAGE T4.

Authors: S Benzer; S P Champe
Journal: Proc Natl Acad Sci U S A Date: 1961-07 Impact factor: 11.205

10. Studies on a Series of Tryptophan-Independent Strains Derived from a Tryptophan-Requiring Mutant of Escherichia Coli.

Authors: J Stadler; C Yanofsky
Journal: Genetics Date: 1959-01 Impact factor: 4.562

34 in total

Suppressor gene alteration of protein primary structure.

1. Peptide pattern studies on the wild-type A protein of the tryptophan synthetase of Escherichia coli.

2. Correspondence between genetic data and the position of amino acid alteration in a proein.

3. An alteration in the primary structure of a protein predicted on the basis of genetic recombination data.

4. The A protein of the tryptophan synthetase of Escherichia coli. Purification, crystallization, and composition studies.

5. Identification of the triose phosphate formed in the tryptophan synthetase reaction.

6. The properties of altered proteins from mutants bearing one or two lesions in the same gene.

7. Transduction of linked genetic characters of the host by bacteriophage P1.

8. THE FORMATION OF A NEW ENZYMATICALLY ACTIVE PROTEIN AS A RESULT OF SUPPRESSION.

9. AMBIVALENT rII MUTANTS OF PHAGE T4.

10. Studies on a Series of Tryptophan-Independent Strains Derived from a Tryptophan-Requiring Mutant of Escherichia Coli.

1. INTERACTION OF STREPTOMYCIN AND A SUPPRESSOR FOR GALACTOSE FERMENTATION IN E. COLI K-12.

2. STREPTOMYCIN-INDUCED OVERSUPPRESSION IN E. COLI.

3. STREPTOMYCIN, SUPPRESSION, AND THE CODE.

4. NUCLEASE ACTIVITY IN DEFECTIVE LYSOGENS OF PHAGE MU. II. A HYPERACTIVE MUTANT.

5. LACK OF FIDELITY IN THE TRANSLATION OF SYNTHETIC POLYRIBONUCLEOTIDES.

6. [EFFECT OF SUPRESSOR GENE MUTATION AND INTERGENIC REVERSION OF THE MUTATION FORM OF OO TYPE].

7. Amber mutants of bacteriophage T4D: their isolation and genetic characterization.

Review 8. Suppression and the code: beyond codons and anticodons.

9. Restoration of enzyme activity by recessive missense suppressors in the fungus Coprinus.

10. Altered protein formation as a result of suppression in Neurospora crassa.