The Ionic and hydrophobic interactions are required for the auto activation of cysteine proteases of Plasmodium falciparum (Q28484433)

1

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Deepak Singh

2

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Ajay K Saxena

3

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Kapil Vashisht

4

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Puran S Sijwali

5

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Kailash C Pandey

Creative Commons Attribution 4.0 International

7

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language of work or name

English

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publication date

2012

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published in

PLOS One

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volume

7

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issue

10

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page(s)

e47227

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copyright license

start time

16 October 2012

1 reference

April 2022 Public Data File from Crossref

copyright status

copyrighted

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cites work

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Falstatin, a cysteine protease inhibitor of Plasmodium falciparum, facilitates erythrocyte invasion

23 March 2017

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Expression and characterization of the Plasmodium falciparum haemoglobinase falcipain-3

23 March 2017

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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

23 March 2017

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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

23 March 2017

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

23 March 2017

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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

23 March 2017

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Site-directed mutagenesis by overlap extension using the polymerase chain reaction

23 March 2017

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Structural basis for unique mechanisms of folding and hemoglobin binding by a malarial protease

23 March 2017

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Statistical potential for assessment and prediction of protein structures

23 March 2017

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Modeling of loops in protein structures

7 April 2017

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Structure-function of falcipains: malarial cysteine proteases

7 April 2017

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Regulatory elements within the prodomain of Falcipain-2, a cysteine protease of the malaria parasite Plasmodium falciparum

29 September 2017

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Hemoglobin cleavage site-specificity of the Plasmodium falciparum cysteine proteases falcipain-2 and falcipain-3.

29 September 2017

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How well can the accuracy of comparative protein structure models be predicted?

29 September 2017

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Processing of human cathepsin D is independent of its catalytic function and auto-activation: involvement of cathepsins L and B.

29 September 2017

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The Plasmodium falciparum cysteine protease falcipain-2 captures its substrate, hemoglobin, via a unique motif

29 September 2017

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Cysteine proteases of malaria parasites

29 September 2017

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Gene disruption confirms a critical role for the cysteine protease falcipain-2 in hemoglobin hydrolysis by Plasmodium falciparum

29 September 2017

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Biosynthesis, localization, and processing of falcipain cysteine proteases of Plasmodium falciparum

29 September 2017

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Characterization of native and recombinant falcipain-2, a principal trophozoite cysteine protease and essential hemoglobinase of Plasmodium falciparum

2 June 2018

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Autocatalytic processing of recombinant human procathepsin B is a bimolecular process.

2 June 2018

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2 June 2018

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2 June 2018

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Falcipain cysteine proteases require bipartite motifs for trafficking to the Plasmodium falciparum food vacuole

27 November 2018

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Gene disruptions demonstrate independent roles for the four falcipain cysteine proteases of Plasmodium falciparum

27 November 2018

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Independent intramolecular mediators of folding, activity, and inhibition for the Plasmodium falciparum cysteine protease falcipain-2.

27 November 2018

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Folding of the Plasmodium falciparum cysteine protease falcipain-2 is mediated by a chaperone-like peptide and not the prodomain

27 November 2018

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pH-induced conformational transitions of the propeptide of human cathepsin L. A role for a molten globule state in zymogen activation

27 November 2018

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Potent slow-binding inhibition of cathepsin B by its propeptide

27 November 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/23077573

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Biosyntheses and processing of lysosomal cysteine proteinases in rat macrophages

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/23077573

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Structural basis for specificity of papain-like cysteine protease proregions toward their cognate enzymes

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/23077573

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1371/JOURNAL.PONE.0047227

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2103457

ADS bibcode

2012PLoSO...747227S

0 references

OpenCitations bibliographic resource ID

2103457

1 reference