(Q43019148)

12 November 2017

A new way of enhancing the thermostability of proteases (English)

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12 November 2017

Imanaka T

1

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12 November 2017

Shibazaki M

series ordinal

2

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12 November 2017

Takagi M

series ordinal

3

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12 November 2017

language of work or name

English

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publication date

1 December 1986

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12 November 2017

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12 November 2017

324

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12 November 2017

695-697

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12 November 2017

6098

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https://scigraph.springernature.com/pub.10.1038/324695a0

12 November 2017

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cites work

Effect of a single amino acid substitution on stability of conformation of a protein

1 reference

7 January 2021

Enzymatic and nucleotide sequence studies of a kanamycin-inactivating enzyme encoded by a plasmid from thermophilic bacilli in comparison with that encoded by plasmid pUB110

1 reference

7 January 2021

1 reference

7 January 2021

Disulfide bond engineered into T4 lysozyme: stabilization of the protein toward thermal inactivation

1 reference

7 January 2021

Thermal stability and protein structure

1 reference

7 January 2021

Molecular cloning of a thermostable neutral protease gene from Bacillus stearothermophilus in a vector plasmid and its expression in Bacillus stearothermophilus and Bacillus subtilis

1 reference

7 January 2021

Nucleotide sequence and promoter region for the neutral protease gene from Bacillus stearothermophilus

1 reference

7 January 2021

Amino-acid sequence of thermolysin

1 reference

7 January 2021

Three-dimensional structure of thermolysin

1 reference

7 January 2021

Efficient site-directed mutagenesis by simultaneous use of two primers

1 reference

7 January 2021

The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus)

1 reference

7 January 2021

Structure of thermolysin

1 reference

7 January 2021

Identifiers

DOI

10.1038/324695A0

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Dimensions Publication ID

12 November 2017

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