Targeting mycobacterial proteolytic complexes with natural products

Tanya Parish

doi:10.1016/j.chembiol.2014.04.002

Targeting mycobacterial proteolytic complexes with natural products

Tanya Parish

Infectious Disease Research Institute

Research output: Contribution to journal › Short survey › peer-review

12 Citations (Scopus)

Abstract

Controlled proteolysis is key to bacterial viability. In this issue of Chemistry & Biology, Gavrish and colleagues characterize a natural product, lassomycin, targeting the Mycobacterium tuberculosis caseinolytic (Clp) protease. Unusually, lassomycin activates ClpC1, inducing ATPase activity and decoupling it from proteolysis.

Original language	English
Pages (from-to)	437-438
Number of pages	2
Journal	Chemistry and Biology
Volume	21
Issue number	4
DOIs	https://doi.org/10.1016/j.chembiol.2014.04.002
Publication status	Published - 24 Apr 2014
Externally published	Yes

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

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10.1016/j.chembiol.2014.04.002

Cite this

@article{0c029894c6714074b3daa633d058e00c,

title = "Targeting mycobacterial proteolytic complexes with natural products",

abstract = "Controlled proteolysis is key to bacterial viability. In this issue of Chemistry \& Biology, Gavrish and colleagues characterize a natural product, lassomycin, targeting the Mycobacterium tuberculosis caseinolytic (Clp) protease. Unusually, lassomycin activates ClpC1, inducing ATPase activity and decoupling it from proteolysis.",

author = "Tanya Parish",

year = "2014",

month = apr,

day = "24",

doi = "10.1016/j.chembiol.2014.04.002",

language = "English",

volume = "21",

pages = "437--438",

journal = "Chemistry and Biology",

issn = "1074-5521",

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number = "4",

}

TY - JOUR

T1 - Targeting mycobacterial proteolytic complexes with natural products

AU - Parish, Tanya

PY - 2014/4/24

Y1 - 2014/4/24

N2 - Controlled proteolysis is key to bacterial viability. In this issue of Chemistry & Biology, Gavrish and colleagues characterize a natural product, lassomycin, targeting the Mycobacterium tuberculosis caseinolytic (Clp) protease. Unusually, lassomycin activates ClpC1, inducing ATPase activity and decoupling it from proteolysis.

AB - Controlled proteolysis is key to bacterial viability. In this issue of Chemistry & Biology, Gavrish and colleagues characterize a natural product, lassomycin, targeting the Mycobacterium tuberculosis caseinolytic (Clp) protease. Unusually, lassomycin activates ClpC1, inducing ATPase activity and decoupling it from proteolysis.

U2 - 10.1016/j.chembiol.2014.04.002

DO - 10.1016/j.chembiol.2014.04.002

M3 - Short survey

C2 - 24766844

AN - SCOPUS:84899574943

SN - 1074-5521

VL - 21

SP - 437

EP - 438

JO - Chemistry and Biology

JF - Chemistry and Biology

IS - 4

ER -

Targeting mycobacterial proteolytic complexes with natural products

Abstract

UN SDGs

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