(Q44523621)

English

The N-terminal region of HtrA heat shock protease from Escherichia coli is essential for stabilization of HtrA primary structure and maintaining of its oligomeric structure

scientific article published in July 2003

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scholarly article

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Europe PubMed Central

PubMed publication ID

3 December 2017

The N-terminal region of HtrA heat shock protease from Escherichia coli is essential for stabilization of HtrA primary structure and maintaining of its oligomeric structure (English)

1 reference

Europe PubMed Central

PubMed publication ID

3 December 2017

Escherichia coli

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Joanna Skórko-Glonek

1

object named as

Joanna Skórko-Glonek

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Europe PubMed Central

PubMed publication ID

3 December 2017

object named as

Fabio Tanfani

3

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ORCID Public Data File 2021

author name string

Dorota Zurawa

2

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Europe PubMed Central

PubMed publication ID

3 December 2017

Andrea Scirè

4

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Europe PubMed Central

PubMed publication ID

3 December 2017

Alicja Wawrzynów

5

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Europe PubMed Central

PubMed publication ID

3 December 2017

Joanna Narkiewicz

6

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Europe PubMed Central

PubMed publication ID

3 December 2017

Enrico Bertoli

7

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Europe PubMed Central

PubMed publication ID

3 December 2017

Barbara Lipińska

8

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Europe PubMed Central

PubMed publication ID

3 December 2017

language of work or name

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publication date

1 July 2003

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Europe PubMed Central

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3 December 2017

Biochimica et Biophysica Acta

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Europe PubMed Central

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3 December 2017

1649

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Europe PubMed Central

PubMed publication ID

3 December 2017

2

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Europe PubMed Central

PubMed publication ID

3 December 2017

171-182

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Europe PubMed Central

PubMed publication ID

3 December 2017

Proteases and their targets in Escherichia coli

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The HtrA family of serine proteases

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7 January 2021

based on heuristic

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The HtrA Family of Proteases

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7 January 2021

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Selective degradation of unfolded proteins by the self-compartmentalizing HtrA protease, a periplasmic heat shock protein in Escherichia coli

1 reference

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The DegP and DegQ periplasmic endoproteases of Escherichia coli: specificity for cleavage sites and substrate conformation

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A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein.

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The Escherichia coli heat shock protease HtrA participates in defense against oxidative stress

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Roles of disulfide bonds in bacterial alkaline phosphatase

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Human HtrA, an evolutionarily conserved serine protease identified as a differentially expressed gene product in osteoarthritic cartilage

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Characterization of human HtrA2, a novel serine protease involved in the mammalian cellular stress response

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Mitotic misregulation and human aging

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The HtrA1 serine protease is down-regulated during human melanoma progression and represses growth of metastatic melanoma cells

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Sequence analysis and regulation of the htrA gene of Escherichia coli: a sigma 32-independent mechanism of heat-inducible transcription

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Identification, characterization, and mapping of the Escherichia coli htrA gene, whose product is essential for bacterial growth only at elevated temperatures

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Site-directed mutagenesis of the HtrA (DegP) serine protease, whose proteolytic activity is indispensable for Escherichia coli survival at elevated temperatures.

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Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine

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Replacement of the fip gene of Escherichia coli by an inactive gene cloned on a plasmid.

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A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes

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A pSC101-derived plasmid which shows no sequence homology to other commonly used cloning vectors

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The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase

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

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Chaperone activity with a redox switch

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Kinetics of Protein-Protein Interactions at the Surface of an Optical Biosensor

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Ligand loading at the surface of an optical biosensor and its effect upon the kinetics of protein-protein interactions

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Specific interaction of cytosolic and mitochondrial glyoxalase II with acidic phospholipids in form of liposomes results in the inhibition of the cytosolic enzyme only

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The formation of protein disulphide bonds

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Thiol/disulfide exchange equilibria and disulfide bond stability

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The rpoE gene encoding the sigma E (sigma 24) heat shock sigma factor of Escherichia coli.

1 reference

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PDZ domains determine the native oligomeric structure of the DegP (HtrA) protease

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Identifiers

10.1016/S1570-9639(03)00170-5

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PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

3 December 2017

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