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Mycobacterium tuberculosis ClpP1 and ClpP2 function together in protein degradation and are required for viability in vitro and during infection

PLoS pathogens, 2012-02, Vol.8 (2), p.e1002511-e1002511

2012

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Pyrazinamide triggers degradation of its target aspartate decarboxylase

Nature communications, 2020-04, Vol.11 (1), p.1661-1661, Article 1661

2020

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The cyclic peptide ecumicin targeting ClpC1 is active against Mycobacterium tuberculosis in vivo

Antimicrobial agents and chemotherapy, 2015-02, Vol.59 (2), p.880-889

2015

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Development of high throughput screening methods for inhibitors of ClpC1P1P2 from Mycobacteria tuberculosis

Analytical biochemistry, 2019-02, Vol.567, p.30-37

2019

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Targeted protein degradation in mycobacteria uncovers antibacterial effects and potentiates antibiotic efficacy

Nature communications, 2024-05, Vol.15 (1), p.4065-4065, Article 4065

2024

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Proteasome Active Sites Allosterically Regulate Each Other, Suggesting a Cyclical Bite-Chew Mechanism for Protein Breakdown

Molecular cell, 1999-09, Vol.4 (3), p.395-402

1999

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Two Distinct Proteolytic Processes in the Generation of a Major Histocompatibility Complex Class I-Presented Peptide

Proceedings of the National Academy of Sciences - PNAS, 1997-09, Vol.94 (20), p.10850-10855

1997

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Lassomycin, a ribosomally synthesized cyclic peptide, kills mycobacterium tuberculosis by targeting the ATP-dependent protease ClpC1P1P2

Chemistry & biology, 2014-04, Vol.21 (4), p.509-518

2014

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Major Histocompatibility Complex Class I-presented Antigenic Peptides Are Degraded in Cytosolic Extracts Primarily by Thimet Oligopeptidase

The Journal of biological chemistry, 2001-09, Vol.276 (39), p.36474-36481

2001

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Correction: Structure of the drug target ClpC1 unfoldase in action provides insights on antibiotic mechanism of action

The Journal of biological chemistry, 2023-07, Vol.299 (7), p.104926-104926, Article 104926

2023

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Structure of the drug target ClpC1 unfoldase in action provides insights on antibiotic mechanism of action

The Journal of biological chemistry, 2022-11, Vol.298 (11), p.102553-102553, Article 102553

2022

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Range of Sizes of Peptide Products Generated during Degradation of Different Proteins by Archaeal Proteasomes

The Journal of biological chemistry, 1998-01, Vol.273 (4), p.1982-1989

1998

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The active ClpP protease from M. tuberculosis is a complex composed of a heptameric ClpP1 and a ClpP2 ring

The EMBO journal, 2012-03, Vol.31 (6), p.1529-1541

2012

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Acyldepsipeptide antibiotics kill mycobacteria by preventing the physiological functions of the ClpP1P2 protease

Molecular microbiology, 2016-07, Vol.101 (2), p.194-209

2016

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Processive Degradation of Proteins and Other Catalytic Properties of the Proteasome from Thermoplasma acidophilum

The Journal of biological chemistry, 1997-01, Vol.272 (3), p.1791-1798

1997

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Structure and Functional Properties of the Active Form of the Proteolytic Complex, ClpP1P2, from Mycobacterium tuberculosis

The Journal of biological chemistry, 2016-04, Vol.291 (14), p.7465-7476

2016

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An Antibacterial β‐Lactone Kills Mycobacterium tuberculosis by Disrupting Mycolic Acid Biosynthesis

Angewandte Chemie International Edition, 2018-01, Vol.57 (1), p.348-353

2018

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ClpX Is Essential and Activated by Single-Strand DNA Binding Protein in Mycobacteria

Journal of bacteriology, 2021-01, Vol.203 (4), p.1

2021

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A novel approach to identifying β-secretase inhibitors: Bis-statine peptide mimetics discovered using structure and spot synthesis

Peptides (New York, N.Y. : 1980), 2006-07, Vol.27 (7), p.1877-1885

2006

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Cleavage Specificity of Mycobacterium tuberculosis ClpP1P2 Protease and Identification of Novel Peptide Substrates and Boronate Inhibitors with Anti-bacterial Activity

The Journal of biological chemistry, 2015-04, Vol.290 (17), p.11008-11020

2015

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The sizes of peptides generated from protein by mammalian 26 and 20 S proteasomes. Implications for understanding the degradative mechanism and antigen presentation

The Journal of biological chemistry, 1999-02, Vol.274 (6), p.3363-3371

1999

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An Antibacterial [beta]-Lactone Kills Mycobacterium tuberculosis by Disrupting Mycolic Acid Biosynthesis

Angewandte Chemie International Edition, 2018-01, Vol.57 (1), p.348

International ed. in English, 2018

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An antibacterial β-lactone kills Mycobacterium tuberculosis by infiltrating mycolic acid biosynthesis

Angewandte Chemie International Edition, 2017-12, Vol.57 (1), p.348-353

2017

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Ein antibakterielles β‐Lacton bekämpft Mycobacterium tuberculosis durch Infiltration der Mykolsäurebiosynthese

Angewandte Chemie, 2018-01, Vol.130 (1), p.354-359

2018

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Structure-Based Design of Estrogen Receptor-β Selective Ligands

Journal of the American Chemical Society, 2004-11, Vol.126 (46), p.15106-15119

2004

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Mycobacterium tuberculosis ClpP1 and ClpP2 function together in protein degradation and are required for viability in vitro and during infection

Pyrazinamide triggers degradation of its target aspartate decarboxylase

The cyclic peptide ecumicin targeting ClpC1 is active against Mycobacterium tuberculosis in vivo

Development of high throughput screening methods for inhibitors of ClpC1P1P2 from Mycobacteria tuberculosis

Targeted protein degradation in mycobacteria uncovers antibacterial effects and potentiates antibiotic efficacy

Proteasome Active Sites Allosterically Regulate Each Other, Suggesting a Cyclical Bite-Chew Mechanism for Protein Breakdown

Two Distinct Proteolytic Processes in the Generation of a Major Histocompatibility Complex Class I-Presented Peptide

Lassomycin, a ribosomally synthesized cyclic peptide, kills mycobacterium tuberculosis by targeting the ATP-dependent protease ClpC1P1P2

Major Histocompatibility Complex Class I-presented Antigenic Peptides Are Degraded in Cytosolic Extracts Primarily by Thimet Oligopeptidase

Correction: Structure of the drug target ClpC1 unfoldase in action provides insights on antibiotic mechanism of action

Structure of the drug target ClpC1 unfoldase in action provides insights on antibiotic mechanism of action

Range of Sizes of Peptide Products Generated during Degradation of Different Proteins by Archaeal Proteasomes

The active ClpP protease from M. tuberculosis is a complex composed of a heptameric ClpP1 and a ClpP2 ring

Acyldepsipeptide antibiotics kill mycobacteria by preventing the physiological functions of the ClpP1P2 protease

Processive Degradation of Proteins and Other Catalytic Properties of the Proteasome from Thermoplasma acidophilum

Structure and Functional Properties of the Active Form of the Proteolytic Complex, ClpP1P2, from Mycobacterium tuberculosis

An Antibacterial β‐Lactone Kills Mycobacterium tuberculosis by Disrupting Mycolic Acid Biosynthesis

ClpX Is Essential and Activated by Single-Strand DNA Binding Protein in Mycobacteria

A novel approach to identifying β-secretase inhibitors: Bis-statine peptide mimetics discovered using structure and spot synthesis

Cleavage Specificity of Mycobacterium tuberculosis ClpP1P2 Protease and Identification of Novel Peptide Substrates and Boronate Inhibitors with Anti-bacterial Activity

The sizes of peptides generated from protein by mammalian 26 and 20 S proteasomes. Implications for understanding the degradative mechanism and antigen presentation

An Antibacterial [beta]-Lactone Kills Mycobacterium tuberculosis by Disrupting Mycolic Acid Biosynthesis

An antibacterial β-lactone kills Mycobacterium tuberculosis by infiltrating mycolic acid biosynthesis

Ein antibakterielles β‐Lacton bekämpft Mycobacterium tuberculosis durch Infiltration der Mykolsäurebiosynthese

Structure-Based Design of Estrogen Receptor-β Selective Ligands

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