(Q43026871)

12 November 2017

Analysis of thermal stabilizing interactions in mesophilic and thermophilic adenylate kinases from the genus Methanococcus (English)

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12 November 2017

Haney PJ

1

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12 November 2017

Stees M

series ordinal

2

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12 November 2017

Konisky J

series ordinal

3

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12 November 2017

language of work or name

English

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publication date

1 October 1999

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Journal of Biological Chemistry

12 November 2017

6

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based on heuristic

inferred from page(s)

published in

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12 November 2017

274

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12 November 2017

28453-28458

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12 November 2017

40

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Thermal adaptation analyzed by comparison of protein sequences from mesophilic and extremely thermophilic Methanococcus species

12 November 2017

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

Crystal structure of neutral protease from Bacillus cereus refined at 3.0 A resolution and comparison with the homologous but more thermostable enzyme thermolysin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

Protein thermal stability: hydrogen bonds or internal packing?

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

Structural basis for the extreme thermostability of D-glyceraldehyde-3-phosphate dehydrogenase from Thermotoga maritima: analysis based on homology modelling.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

Contribution of the hydrophobic effect to globular protein stability

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

Insights into thermal stability from a comparison of the glutamate dehydrogenases from Pyrococcus furiosus and Thermococcus litoralis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

The mechanisms of irreversible enzyme inactivation at 100C.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

Amino acid preferences for specific locations at the ends of alpha helices

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

Engineering protein thermal stability. Sequence statistics point to residue substitutions in alpha-helices.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

Determinants of protein thermostability observed in the 1.9-A crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

Dominant forces in protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

Conformational stability of globular proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

Deciphering the message in protein sequences: tolerance to amino acid substitutions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

Structural features can be unconserved in proteins with similar folds. An analysis of side-chain to side-chain contacts secondary structure and accessibility.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

The adenylate kinases from a mesophilic and three thermophilic methanogenic members of the Archaea

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

The adenylate kinase genes of M. voltae, M. thermolithotrophicus, M. jannaschii, and M. igneus define a new family of adenylate kinases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

Structural basis for thermostability and identification of potential active site residues for adenylate kinases from the archaeal genus Methanococcus.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

Precise gene fusion by PCR.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

The refined structure of the complex between adenylate kinase from beef heart mitochondrial matrix and its substrate AMP at 1.85 A resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

Refined structure of porcine cytosolic adenylate kinase at 2.1 A resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.40.28453

21 January 2018

Identifiers

DOI

10.1074/JBC.274.40.28453

1 reference

12 November 2017

1 reference