Functional analysis of the propeptides of subtilisin E and aqualysin I as intramolecular chaperones (Q43806037)

27 November 2017

title

Functional analysis of the propeptides of subtilisin E and aqualysin I as intramolecular chaperones (English)

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27 November 2017

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Takagi H

1

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27 November 2017

Koga M

2

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27 November 2017

Katsurada S

3

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Yabuta Y

4

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27 November 2017

Shinde U

5

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Inouye M

6

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27 November 2017

Nakamori S

7

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27 November 2017

language of work or name

English

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publication date

1 November 2001

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27 November 2017

number of pages

5

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based on heuristic

inferred from page(s)

published in

FEBS Letters

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27 November 2017

volume

508

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27 November 2017

issue

2

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page(s)

210-214

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Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process.

27 November 2017

cites work

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Protein memory through altered folding mediated by intramolecular chaperones.

21 January 2018

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Substrate-induced activation of a trapped IMC-mediated protein folding intermediate

21 January 2018

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The alpha-lytic protease pro-region does not require a physical linkage to activate the protease domain in vivo

21 January 2018

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A protein-folding reaction under kinetic control

21 January 2018

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Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity

21 January 2018

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The prosequence of thermolysin acts as an intramolecular chaperone when expressed in trans with the mature sequence in Escherichia coli.

21 January 2018

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Intramolecular chaperones: polypeptide extensions that modulate protein folding.

21 January 2018

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The structural and functional organization of intramolecular chaperones: the N-terminal propeptides which mediate protein folding

21 January 2018

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Subtilisin--an enzyme designed to be engineered

21 January 2018

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Protein engineering on subtilisin

21 January 2018

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Subtilases: the superfamily of subtilisin-like serine proteases

21 January 2018

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Folding pathway mediated by an intramolecular chaperone

21 January 2018

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Folding mediated by an intramolecular chaperone: autoprocessing pathway of the precursor resolved via a substrate assisted catalysis mechanism

21 January 2018

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Intramolecular chaperones and protein folding

21 January 2018

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Catalysis of a protein folding reaction: thermodynamic and kinetic analysis of subtilisin BPN' interactions with its propeptide fragment.

21 January 2018

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Pro-sequence-assisted protein folding

21 January 2018

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Folding pathway mediated by an intramolecular chaperone: the structural and functional characterization of the aqualysin I propeptide

21 January 2018

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Purification and characterization of aqualysin I (a thermophilic alkaline serine protease) produced by Thermus aquaticus YT-1.

21 January 2018

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The crystal structure of an autoprocessed Ser221Cys-subtilisin E-propeptide complex at 2.0 A resolution

21 January 2018

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Functional analysis of the propeptide of subtilisin E as an intramolecular chaperone for protein folding. Refolding and inhibitory abilities of propeptide mutants.

21 January 2018

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Determination of the positions of the disulfide bonds in aqualysin I (a thermophilic alkaline serine protease) of Thermus aquaticus YT-1.

21 January 2018

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Engineering subtilisin E for enhanced stability and activity in polar organic solvents

21 January 2018

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Substrate Specificity of Aqualysin I, a Bacterial Thermophilic Alkaline Serine Protease from Thermus aquaticus YT-1: Comparison with Proteinase K, Subtilisin BPN' and Subtilisin Carlsberg

21 January 2018

1 reference

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Folding Pathway Mediated by an Intramolecular Chaperone: Characterization of the Structural Changes in Pro-subtilisin E Coincident with Autoprocess ing

21 January 2018

1 reference

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Role of the COOH-terminal pro-sequence of aqualysin I (a heat-stable serine protease) in its extracellular secretion by Thermus thermophilus

21 January 2018

1 reference

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Folding pathway mediated by an intramolecular chaperone. The inhibitory and chaperone functions of the subtilisin propeptide are not obligatorily linked

21 January 2018

1 reference

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10.1016/S0014-5793(01)03053-8

21 January 2018

Identifiers

DOI

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27 November 2017

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