Relevant bibliographies by topics / High temperature requirement A (HtrA) protease

Contents

  1. Journal articles
  2. Dissertations / Theses

Academic literature on the topic 'High temperature requirement A (HtrA) protease'

Author: Grafiati
Published: 6 September 2023
Last updated: 31 July 2025

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'High temperature requirement A (HtrA) protease.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "High temperature requirement A (HtrA) protease"

1

NIE, Gui-Ying, Anne HAMPTON, Ying LI, Jock K. FINDLAY, and Lois A. SALAMONSEN. "Identification and cloning of two isoforms of human high-temperature requirement factor A3 (HtrA3), characterization of its genomic structure and comparison of its tissue distribution with HtrA1 and HtrA2." Biochemical Journal 371, no. 1 (2003): 39–48. http://dx.doi.org/10.1042/bj20021569.

Full text
Abstract:
In the present study, we identified an additional member of the human high-temperature requirement factor A (HtrA) protein family, called pregnancy-related serine protease or HtrA3, which was most highly expressed in the heart and placenta. We cloned the full-length sequences of two forms (long and short) of human HtrA3 mRNA, located the gene on chromosome 4p16.1, determined its genomic structure and revealed how the two mRNA variants are produced through alternative splicing. The alternative splicing was also verified by Northern blotting. Four distinct domains were found for the long form Ht
APA, Harvard, Vancouver, ISO, and other styles
2

Bowden, M. A., L. A. Di Nezza, T. Jobling, L. A. Salamonsen, and G. Nie. "284.Expression of HtrA1, 2 and 3 in human endometrial cancer." Reproduction, Fertility and Development 16, no. 9 (2004): 284. http://dx.doi.org/10.1071/srb04abs284.

Full text
Abstract:
The mammalian HtrA family consists of serine proteases with distinct domains homologous to the bacterial high temperature requirement factor (HtrA). Three human HtrA members have been reported: HtrA1 (PRSS11 or L56), HtrA2 (OMI) and HtrA3 (PRSP). The function of HtrA1 is not well characterised, but it has been shown to be downregulated in malignant tissues (1–3) indicating that the downregulation of HtrA1 is associated with cancer progression. HtrA2 regulates apoptosis by interacting with X-linked inhibitors of apoptosis (XIAP) thus preventing the caspase-inhibitory function of XIAP (4). The f
APA, Harvard, Vancouver, ISO, and other styles
3

Bæk, Kristoffer T., Christina S. Vegge, Joanna Skórko-Glonek, and Lone Brøndsted. "Different Contributions of HtrA Protease and Chaperone Activities toCampylobacter jejuniStress Tolerance and Physiology." Applied and Environmental Microbiology 77, no. 1 (2010): 57–66. http://dx.doi.org/10.1128/aem.01603-10.

Full text
Abstract:
ABSTRACTThe microaerophilic bacteriumCampylobacter jejuniis the most common cause of bacterial food-borne infections in the developed world. Tolerance to environmental stress relies on proteases and chaperones in the cell envelope, such as HtrA and SurA. HtrA displays both chaperone and protease activities, but little is known about how each of these activities contributes to stress tolerance in bacteria.In vitroexperiments showed temperature-dependent protease and chaperone activities ofC. jejuniHtrA. AC. jejunimutant lacking only the protease activity of HtrA was used to show that the HtrA c
APA, Harvard, Vancouver, ISO, and other styles
4

Singh, Khundrakpam Herojit, Savita Yadav, Deepak Kumar, and Bichitra Kumar Biswal. "The crystal structure of an essential high-temperature requirement protein HtrA1 (Rv1223) from Mycobacterium tuberculosis reveals its unique features." Acta Crystallographica Section D Structural Biology 74, no. 9 (2018): 906–21. http://dx.doi.org/10.1107/s205979831800952x.

Full text
Abstract:
High-temperature requirement A (HtrA) proteins, which are members of the heat-shock-induced serine protease family, are involved in extracytoplasmic protein quality control and bacterial survival strategies under stress conditions, and are associated with the virulence of several pathogens; they are therefore major drug targets. Mycobacterium tuberculosis possesses three putative HtrAs: HtrA1 (Rv1223), HtrA2 (Rv0983) and HtrA3 (Rv0125). Each has a cytoplasmic region, a transmembrane helix and a periplasmic region. Here, the crystal structure of the periplasmic region consisting of a protease d
APA, Harvard, Vancouver, ISO, and other styles
5

Bernegger, Sabine, Evelyn Hutterer, Urszula Zarzecka, et al. "E-Cadherin Orthologues as Substrates for the Serine Protease High Temperature Requirement A (HtrA)." Biomolecules 12, no. 3 (2022): 356. http://dx.doi.org/10.3390/biom12030356.

Full text
Abstract:
Helicobacter pylori (H. pylori) expresses the serine protease and chaperone High temperature requirement A (HtrA) that is involved in periplasmic unfolded protein stress response. Additionally, H. pylori-secreted HtrA directly cleaves the human cell adhesion molecule E-cadherin leading to a local disruption of intercellular adhesions during pathogenesis. HtrA-mediated E-cadherin cleavage has been observed in response to a broad range of pathogens, implying that it is a prevalent mechanism in humans. However, less is known whether E-cadherin orthologues serve as substrates for bacterial HtrA. H
APA, Harvard, Vancouver, ISO, and other styles
6

Padmanabhan, Nirmala, Lars Fichtner, Achim Dickmanns, Ralf Ficner, Jörg B. Schulz, and Gerhard H. Braus. "The Yeast HtrA Orthologue Ynm3 Is a Protease with Chaperone Activity that Aids Survival Under Heat Stress." Molecular Biology of the Cell 20, no. 1 (2009): 68–77. http://dx.doi.org/10.1091/mbc.e08-02-0178.

Full text
Abstract:
Ynm3 is the only budding yeast protein possessing a combination of serine protease and postsynaptic density 95/disc-large/zona occludens domains, a defining feature of the high temperature requirement A (HtrA) protein family. The bacterial HtrA/DegP is involved in protective stress response to aid survival at higher temperatures. The role of mammalian mitochondrial HtrA2/Omi in protein quality control is unclear, although loss of its protease activity results in susceptibility toward Parkinson's disease, in which mitochondrial dysfunction and impairment of protein folding and degradation are k
APA, Harvard, Vancouver, ISO, and other styles
7

Gupta, Arvind Kumar, Debashree Behera, and Balasubramanian Gopal. "The crystal structure of Mycobacterium tuberculosis high-temperature requirement A protein reveals an autoregulatory mechanism." Acta Crystallographica Section F Structural Biology Communications 74, no. 12 (2018): 803–9. http://dx.doi.org/10.1107/s2053230x18016217.

Full text
Abstract:
The crystal structure of Mycobacterium tuberculosis high-temperature requirement A (HtrA) protein was determined at 1.83 Å resolution. This membrane-associated protease is essential for the survival of M. tuberculosis. The crystal structure reveals that interactions between the PDZ domain and the catalytic domain in HtrA lead to an inactive conformation. This finding is consistent with its proposed role as a regulatory protease that is conditionally activated upon appropriate environmental triggers. The structure provides a basis for directed studies to evaluate the role of this essential prot
APA, Harvard, Vancouver, ISO, and other styles
8

Ye, Meiping, Kavita Sharma, Meghna Thakur, et al. "HtrA, a Temperature- and Stationary Phase-Activated Protease Involved in Maturation of a Key Microbial Virulence Determinant, Facilitates Borrelia burgdorferi Infection in Mammalian Hosts." Infection and Immunity 84, no. 8 (2016): 2372–81. http://dx.doi.org/10.1128/iai.00360-16.

Full text
Abstract:
High-temperature requirement protease A (HtrA) represents a family of serine proteases that play important roles in microbial biology. Unlike the genomes of most organisms, that ofBorrelia burgdorferinotably encodes a single HtrA gene product, termed BbHtrA. Previous studies identified a few substrates of BbHtrA; however, their physiological relevance could not be ascertained, as targeted deletion of the gene has not been successful. Here we show that BbhtrAtranscripts are induced during spirochete growth either in the stationary phase or at elevated temperature. Successful generation of a Bbh
APA, Harvard, Vancouver, ISO, and other styles
9

Kummari, Raghupathi, Shubhankar Dutta, Lalith K. Chaganti, and Kakoli Bose. "Discerning the mechanism of action of HtrA4: a serine protease implicated in the cell death pathway." Biochemical Journal 476, no. 10 (2019): 1445–63. http://dx.doi.org/10.1042/bcj20190224.

Full text
Abstract:
Abstract High-temperature requirement protease A4 (HtrA4) is a secretary serine protease whose expression is up-regulated in pre-eclampsia (PE) and hence is a possible biomarker of PE. It has also been altered in cancers such as glioblastoma, breast carcinoma, and prostate cancer making it an emerging therapeutic target. Among the human HtrAs, HtrA4 is the least characterized protease pertaining to both structure and its functions. Although the members of human HtrA family share a significant structural and functional conservation, subtle structural changes have been associated with certain di
APA, Harvard, Vancouver, ISO, and other styles
10

Wang, Yao, and Guiying Nie. "Overview of Human HtrA Family Proteases and Their Distinctive Physiological Roles and Unique Involvement in Diseases, Especially Cancer and Pregnancy Complications." International Journal of Molecular Sciences 22, no. 19 (2021): 10756. http://dx.doi.org/10.3390/ijms221910756.

Full text
Abstract:
The mammalian high temperature requirement A (HtrA) proteins are a family of evolutionarily conserved serine proteases, consisting of four homologs (HtrA1-4) that are involved in many cellular processes such as growth, unfolded protein stress response and programmed cell death. In humans, while HtrA1, 2 and 3 are widely expressed in multiple tissues with variable levels, HtrA4 expression is largely restricted to the placenta with the protein released into maternal circulation during pregnancy. This limited expression sets HtrA4 apart from the rest of the family. All four HtrAs are active prote
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "High temperature requirement A (HtrA) protease"

1

Marsh, James W. "In silico and functional characterisation of the high temperature requirement a (HtrA) protease from Chlamydia trachomatis." Thesis, Queensland University of Technology, 2015. https://eprints.qut.edu.au/83818/1/James_Marsh_Thesis.pdf.

Full text
Abstract:
This project used modelling, biochemical, and genetic approaches to investigate the physiological function of the HtrA protease in C. trachomatis. This organism is responsible for several human diseases, however our understanding of how it causes these diseases is limited. By focusing on a single C. trachomatis protein, HtrA, we were able to demonstrate the protein is a unique protease/chaperone which is important for the replicative phase of the organism. This project has identified HtrA as one of the key components for the pathogenesis of C. trachomatis and will guide the generation of new t
APA, Harvard, Vancouver, ISO, and other styles
2

Prinz, Alexander Dietrich [Verfasser], and Andreas [Akademischer Betreuer] Fischer. "Der Einfluss der Serin-Protease High Temperature Requirement Protein A1 auf glatte Gefäßmuskelzellen / Alexander Dietrich Prinz ; Betreuer: Andreas Fischer." Heidelberg : Universitätsbibliothek Heidelberg, 2020. http://d-nb.info/1220698199/34.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Prinz, Alexander [Verfasser], and Andreas [Akademischer Betreuer] Fischer. "Der Einfluss der Serin-Protease High Temperature Requirement Protein A1 auf glatte Gefäßmuskelzellen / Alexander Dietrich Prinz ; Betreuer: Andreas Fischer." Heidelberg : Universitätsbibliothek Heidelberg, 2020. http://d-nb.info/1220698199/34.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Gupta, Arvind Kumar. "Understanding intramolecular signal transduction in regulated proteases of the High Temperature Requirement A family." Thesis, 2020. https://etd.iisc.ac.in/handle/2005/4507.

Full text
Abstract:
Protein homeostasis in all organisms is a complex process involving regulatory mechanisms that govern protein synthesis, post-translational events and degradation. The protein degradation mechanism serves multiple functions ranging from maturation of cellular proteins, protein recycling and intracellular signal transduction. This mechanism, therefore, has a major role in diverse cellular and developmental contexts. In prokaryotes, the protein degradation mechanism has been shown to influence the cellular response to environmental stimuli and thus pathogenesis and virulence. The prokaryotic pro
APA, Harvard, Vancouver, ISO, and other styles
5

Chen, Yao-Yu, and 陳瑤瑜. "Functional antagonism between high-temperature requirement protein A (HtrA) family members regulates trophoblast cell invasion." Thesis, 2014. http://ndltd.ncl.edu.tw/handle/24441564364973180189.

Full text
Abstract:
碩士<br>國立臺灣大學<br>生化科學研究所<br>102<br>Human trophoblast invasion of decidualized endometrium is essential for placentation and is tightly regulated and involves decidua-trophoblastic interaction. High-temperature requirement A4 (HtrA4) is a secreted serine protease highly expressed in the invasive extravillous trophoblasts and promotes decidua-trophoblastic interaction. In contrast, both HtrA1 and HtrA3 have been shown to inhibit placental cell invasion. Here we provide evidence that decidua-secreted HtrA1 and HtrA3 antagonize HtrA4-mediated placental cell invasion. We demonstrated that HtrA1 and
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'High temperature requirement A (HtrA) protease' for particular source types:
Journal articles
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography