(Q47851086)

6 February 2018

title

Autocatalytic processing of recombinant human procathepsin B is a bimolecular process (English)

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6 February 2018

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Rozman J

1

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6 February 2018

Stojan J

2

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6 February 2018

Kuhelj R

3

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6 February 2018

Turk V

4

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6 February 2018

Turk B

5

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6 February 2018

language of work or name

English

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publication date

1 October 1999

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6 February 2018

number of pages

5

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based on heuristic

inferred from page(s)

published in

FEBS Letters

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6 February 2018

volume

459

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6 February 2018

issue

3

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6 February 2018

page(s)

358-362

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6 February 2018

Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain

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Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs

21 January 2018

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The proregion of cathepsin L is required for proper folding, stability, and ER exit

21 January 2018

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Activation of procathepsin B in human hepatoma cells: the conversion into the mature enzyme relies on the action of cathepsin B itself

21 January 2018

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Autocatalytic activation of human cathepsin K.

21 January 2018

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Autocatalytic processing of recombinant human procathepsin L. Contribution of both intermolecular and unimolecular events in the processing of procathepsin L in vitro

21 January 2018

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Crystal structures of human procathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide

21 January 2018

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Crystal structure of the wild-type human procathepsin B at 2.5 A resolution reveals the native active site of a papain-like cysteine protease zymogen

21 January 2018

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https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901302-2

Structure of rat procathepsin B: model for inhibition of cysteine protease activity by the proregion

21 January 2018

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The crystal structure of human procathepsin K

21 January 2018

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https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2901302-2

Crystal structure of wild-type human procathepsin K

21 January 2018

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The preparation of catalytically active human cathepsin B from its precursor expressed in Escherichia coli in the form of inclusion bodies.

21 January 2018

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How to measure and predict the molar absorption coefficient of a protein

21 January 2018

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Surface activation of pro-cathepsin L

21 January 2018

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High-affinity binding of two molecules of cysteine proteinases to low-molecular-weight kininogen.

21 January 2018

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

21 January 2018

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Kinetics of activation and autoactivation of human factor XII.

21 January 2018

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The identification of the major excreted protein (MEP) from a transformed mouse fibroblast cell line as a catalytically active precursor form of cathepsin L

21 January 2018

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Autocatalytic processing of pro-papaya proteinase IV is prevented by crowding of the active-site cleft

21 January 2018

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Procathepsin L degrades extracellular matrix proteins in the presence of glycosaminoglycans in vitro

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Extracellular presence of the lysosomal proteinase cathepsin B in rheumatoid synovium and its activity at neutral pH

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Identification of latent procathepsins B and L in microsomal lumen: characterization of enzymatic activation and proteolytic processing in vitro

7 January 2021

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Biosyntheses and processing of lysosomal cysteine proteinases in rat macrophages

7 January 2021

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Potent slow-binding inhibition of cathepsin B by its propeptide

7 January 2021

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Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment

7 January 2021

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Kinetics of the pH-induced inactivation of human cathepsin L

7 January 2021

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pH-induced Conformational Transitions of the Propeptide of Human Cathepsin L

7 January 2021

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Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases

7 January 2021

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The inhibition of cathepsin S by its propeptide--specificity and mechanism of action

7 January 2021

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10.1016/S0014-5793(99)01302-2

7 January 2021

Identifiers

DOI

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6 February 2018

PubMed ID

10526165

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6 February 2018