Front Cover: An Integrated Proteomic Approach Uncovers Novel Substrates and Functions of the Lon Protease in  Escherichia coli | Zendy

Arends Jan | Zendy; Griego Marcena | Zendy; Thomanek Nikolas | Zendy; Lindemann Claudia | Zendy; Kutscher Blanka | Zendy; Meyer Helmut E. | Zendy; Narberhaus Franz | Zendy

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Front Cover: An Integrated Proteomic Approach Uncovers Novel Substrates and Functions of the Lon Protease in Escherichia coli

Author(s) -

Arends Jan,

Griego Marcena,

Thomanek Nikolas,

Lindemann Claudia,

Kutscher Blanka,

Meyer Helmut E.,

Narberhaus Franz

Publication year - 2018

Publication title -

proteomics

Language(s) - English

Resource type - Reports

SCImago Journal Rank - 1.26

H-Index - 167

eISSN - 1615-9861

pISSN - 1615-9853

DOI - 10.1002/pmic.201870111

Subject(s) - protease , proteolysis , escherichia coli , proteome , proteomics , biology , biochemistry , proteases , computational biology , substrate specificity , chemistry , microbiology and biotechnology , enzyme , gene

DOI: 10.1002/pmic.201800080 Regulated proteolysis of active and natively folded proteins is a universal strategy to shape the cellular proteome. In article number 1800080 , Arends et al. use a combination of quantitative comparative proteomics and trapping experiments with a proteolytically inactive protease variant to investigate the substrate repertoire of the Lon protease from Escherichia coli . By these approaches, several new physiological functions of the Lon protease are identified.

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