Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Rakhi Bajaj"'
Autor:
M. Teresa Bertran, Stéphane Mouilleron, Yanxiang Zhou, Rakhi Bajaj, Federico Uliana, Ganesan Senthil Kumar, Audrey van Drogen, Rebecca Lee, Jennifer J. Banerjee, Simon Hauri, Nicola O’Reilly, Matthias Gstaiger, Rebecca Page, Wolfgang Peti, Nicolas Tapon
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-19 (2019)
Serine/threonine phosphatases such as PP1 associate with a large array of subunit proteins, such as ASPP (apoptosis-stimulating protein of p53) to achieve selective targeting. Here authors solved the crystal structure of the human ASPP2/PP1 complex a
Externí odkaz:
https://doaj.org/article/6895486193a040a6ada179998498e708
Autor:
Gautam Srivastava, Rakhi Bajaj, Ganesan Senthil Kumar, Antoine Gaudreau-Lapierre, Hannah Nicolas, Delphine Chamousset, Dale Kreitler, Wolfgang Peti, Laura Trinkle-Mulcahy, Rebecca Page
Publikováno v:
Cell Reports. 41:111726
The serine/threonine protein phosphatase 1 (PP1) dephosphorylates hundreds of substrates by associating with200 regulatory proteins to form specific holoenzymes. The major PP1 targeting protein in the nucleolus is RRP1B (ribosomal RNA processing 1B).
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b21a522b3d0b36cab385ccaf9728f566
https://doi.org/10.1016/j.celrep.2022.111726
https://doi.org/10.1016/j.celrep.2022.111726
Publikováno v:
Nucleic Acids Research
In Streptomyces coelicolor, we identified a para-hydroxybenzoate (PHB) hydroxylase, encoded by gene pobA (SCO3084), which is responsible for conversion of PHB into PCA (protocatechuic acid), a substrate of the β-ketoadipate pathway which yields inte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee5b7d6c72bbec451e77eb3712b4f8b1
https://pubmed.ncbi.nlm.nih.gov/29240934
https://pubmed.ncbi.nlm.nih.gov/29240934
Autor:
Pawan Kumar, Rakhi Bajaj
Publikováno v:
International Journal of Business and Globalisation. 23:47
The tremendous growth of internet has accounted for accelerated growth in e tailoring. Online shopping irrespective of its growth marked for small percentage of sale due to perceived risk. The study is designed to examine key components of perceived
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8a295fef33e49b7297c3f0f35ee78c80
https://doi.org/10.1504/ijbg.2019.10022551
https://doi.org/10.1504/ijbg.2019.10022551
Specific interactions between proteins govern essential physiological processes including signaling. Many enzymes, especially the family of serine/threonine phosphatases (PSPs: PP1, PP2A and PP2B/calcineurin/CN), recruit substrates and regulatory pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b5d9c2273bebbad71c8a7695510cffb
https://europepmc.org/articles/PMC5180209/
https://europepmc.org/articles/PMC5180209/
Publikováno v:
Protein Science. 19:2045-2054
Proteins targeted to the mitochondrial matrix are translocated through the outer and the inner mitochondrial membranes by two protein complexes, the translocase of the outer membrane (TOM) and one of the translocases of the inner membrane (TIM23). Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7bd5b04d883ca2e32417f7e07c6aa503
https://doi.org/10.1002/pro.482
https://doi.org/10.1002/pro.482
Publikováno v:
Structure
Structure 22(10), 1501-1511 (2014). doi:10.1016/j.str.2014.07.015
Structure 22(10), 1501-1511 (2014). doi:10.1016/j.str.2014.07.015
Summary The presequence translocase TIM23 is a highly dynamic complex in which its subunits can adopt multiple conformations and undergo association-dissociation to facilitate import of proteins into mitochondria. Despite the importance of protein-pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::620f887dbbedd7e41ad5c3cab66d56bc
https://hdl.handle.net/11858/00-001M-0000-0024-3319-511858/00-001M-0000-0024-3317-911858/00-001M-0000-0024-331B-111858/00-001M-0000-0024-331A-3
https://hdl.handle.net/11858/00-001M-0000-0024-3319-511858/00-001M-0000-0024-3317-911858/00-001M-0000-0024-331B-111858/00-001M-0000-0024-331A-3
Publikováno v:
The journal of biological chemistry 289(50), 34620-34626 (2014). doi:10.1074/jbc.M114.595702
Journal of Biological Chemistry
Journal of Biological Chemistry
Background: Tim23 mediates protein translocation into mitochondria. Results: Tim23 binds to mitochondria-like membranes through a hydrophobic anchor at its N terminus, with cardiolipin enhancing the interaction. Conclusion: The intermembrane space do
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef1f0f3535a304eb827adc90882aa425
https://pub.dzne.de/record/137678
https://pub.dzne.de/record/137678
Publikováno v:
Protein science : a publication of the Protein Society. 19(11)
Proteins targeted to the mitochondrial matrix are translocated through the outer and the inner mitochondrial membranes by two protein complexes, the translocase of the outer membrane (TOM) and one of the translocases of the inner membrane (TIM23). Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e50da0bbbcd3fc82889c095515f2e5b4
https://pubmed.ncbi.nlm.nih.gov/20718036
https://pubmed.ncbi.nlm.nih.gov/20718036