Characterization of human HtrA2, a novel serine protease involved in the mammalian cellular stress response (Q24290181)

cellular response to heat

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author

Christopher Southan

7

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author name string

C W Gray

1

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R V Ward

2

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E Karran

3

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S Turconi

4

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A Rowles

5

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D Viglienghi

6

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A Barton

8

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K G Fantom

9

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A West

10

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J Savopoulos

11

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N J Hassan

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H Clinkenbeard

13

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C Hanning

14

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B Amegadzie

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J B Davis

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C Dingwall

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G P Livi

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C L Creasy

Evidence for PDZ domains in bacteria, yeast, and plants

19

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language of work or name

English

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publication date

September 2000

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published in

FEBS Journal

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volume

267

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issue

18

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page(s)

5699-710

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cites work

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

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Presenilin-1 is processed into two major cleavage products in neuronal cell lines

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Expression, purification, and functional analysis of the human serine protease HtrA2

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Fluorometric determination of bacterial protease activity using fluorescein isothiocyanate-labeled proteins as substrates

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Maturation of the head of bacteriophage T4. I. DNA packaging events

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Getting started with yeast

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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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7 January 2021

Protease Do is essential for survival of Escherichia coli at high temperatures: its identity with the htrA gene product

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Primary structure of a putative serine protease specific for IGF-binding proteins

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

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A role for presenilin-1 in nuclear accumulation of Ire1 fragments and induction of the mammalian unfolded protein response

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Protein-protein interactions: PDZ domain networks

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The unfolded protein response: an intracellular signalling pathway with many surprising features

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Increased vulnerability of hippocampal neurons to excitotoxic necrosis in presenilin-1 mutant knock-in mice

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Presenilin-1 mutations downregulate the signalling pathway of the unfolded-protein response

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PDZ domain of neuronal nitric oxide synthase recognizes novel C-terminal peptide sequences

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Degradation by proteases Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock; HtrA protease action in vivo and in vitro.

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The HtrA family of serine proteases

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Comparison of the structure of wild-type HtrA heat shock protease and mutant HtrA proteins. A Fourier transform infrared spectroscopic study.

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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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Identification of a novel PSD-95/Dlg/ZO-1 (PDZ)-like protein interacting with the C terminus of presenilin-1

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Characterization of a novel human serine protease that has extensive homology to bacterial heat shock endoprotease HtrA and is regulated by kidney ischemia

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Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei

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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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The mechanism and functions of ATP-dependent proteases in bacterial and animal cells

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Recognition of unique carboxyl-terminal motifs by distinct PDZ domains

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Genome sequence of the nematode C. elegans: a platform for investigating biology

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Candidate gene for the chromosome 1 familial Alzheimer's disease locus

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

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

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Alzheimer's presenilin mutation sensitizes neural cells to apoptosis induced by trophic factor withdrawal and amyloid beta-peptide: involvement of calcium and oxyradicals.

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