(Q56384751)

1

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Ah Ram Wi

2

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Byoung Wook Jeon

3

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Seung Chul Shin

5

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Hyun Park

6

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Sung-Jong Jeon

https://scigraph.springernature.com/pub.10.1007/s10529-015-1860-y

7

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language of work or name

English

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publication date

September 2015

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published in

Biotechnology Letters

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volume

37

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issue

9

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page(s)

1887-93

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exact match

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cites work

Biotechnological uses of enzymes from psychrophiles

1 reference

https://api.crossref.org/works/10.1007%2FS10529-015-1860-Y

ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL Chaperonin

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS10529-015-1860-Y

Chaperones GroEL/GroES accelerate the refolding of a multidomain protein through modulating on-pathway intermediates

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS10529-015-1860-Y

Psychrophilic microorganisms: challenges for life

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS10529-015-1860-Y

Sequence of a lipase gene from the antarctic psychrotroph Moraxella TA144.

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS10529-015-1860-Y

Chaperonins govern growth of Escherichia coli at low temperatures.

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS10529-015-1860-Y

GroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain Folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS10529-015-1860-Y

GroEL (Hsp60) of Clostridium difficile is involved in cell adherence.

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS10529-015-1860-Y

One-step sequence- and ligation-independent cloning as a rapid and versatile cloning method for functional genomics studies

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS10529-015-1860-Y

Genome sequence of a novel member of the genus Psychrobacter isolated from Antarctic soil

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS10529-015-1860-Y

Crystal structure of a symmetric football-shaped GroEL:GroES2-ATP14 complex determined at 3.8Å reveals rearrangement between two GroEL rings

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS10529-015-1860-Y

Use of folding modulators to improve heterologous protein production in Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS10529-015-1860-Y

Versatile roles of the chaperonin GroEL in microorganism-insect interactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS10529-015-1860-Y

Hydrophilic residues 526 KNDAAD 531 in the flexible C-terminal region of the chaperonin GroEL are critical for substrate protein folding within the central cavity.

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS10529-015-1860-Y

A nonconserved carboxy-terminal segment of GroEL contributes to reaction temperature

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS10529-015-1860-Y

GroEL/GroES cycling: ATP binds to an open ring before substrate protein favoring protein binding and production of the native state

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS10529-015-1860-Y

GroEL dependency affects codon usage--support for a critical role of misfolding in gene evolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS10529-015-1860-Y

Functional understanding of solvent structure in GroEL cavity through dipole field analysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS10529-015-1860-Y

The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS10529-015-1860-Y

Coexpression of chaperonin GroEL/GroES markedly enhanced soluble and functional expression of recombinant human interferon-gamma in Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS10529-015-1860-Y

Molecular chaperones facilitate the soluble expression of N-acyl-D-amino acid amidohydrolases in Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS10529-015-1860-Y

Expression, purification, and characterization of formaldehyde dehydrogenase from Pseudomonas aeruginosa

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS10529-015-1860-Y