Výsledky vyhledávání - "Ewelina M Krysztofinska"

Akademický článek

The association of BAG6 with SGTA and tail-anchored proteins.

Autor: Pawel Leznicki, Quentin P Roebuck, Lydia Wunderley, Anne Clancy, Ewelina M Krysztofinska, Rivka L Isaacson, Jim Warwicker, Blanche Schwappach, Stephen High

Publikováno v: PLoS ONE, Vol 8, Iss 3, p e59590 (2013)

The BAG6 protein is a subunit of a heterotrimeric complex that binds a range of membrane and secretory protein precursors localized to the cytosol, enforcing quality control and influencing their subsequent fate.BAG6 has an N-terminal ubiquitin-like

Externí odkaz: https://doaj.org/article/64d12d24e67b4b8f877d17a4d74feb1f

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A novel RNA polymerase‐binding protein that interacts with a sigma‐factor docking site

Autor: Ann Hochschild, Caterina Alfano, Ewelina M. Krysztofinska, Rivka L. Isaacson, Cinthia P. Garcia, Anna F. Wang Erickson, Padraig Deighan, Kelsey Barrasso, Santiago Martínez-Lumbreras, Richard Losick, Arjun Thapaliya, Amy H. Camp, Shanshan Chen

Publikováno v: Wang Erickson, A F, Deighan, P, Chen, S, Barrasso, K, Garcia, C P, Martínez-Lumbreras, S, Alfano, C, Krysztofinska, E M, Thapaliya, A, Camp, A H, Isaacson, R L, Hochschild, A & Losick, R 2017, ' A Novel RNA Polymerase-binding Protein that interacts with a Sigma-Factor Docking Site ', Molecular Microbiology . https://doi.org/10.1111/mmi.13724

Sporulation in Bacillus subtilis is governed by a cascade of alternative RNA polymerase sigma factors. We previously identified a small protein Fin that is produced under the control of the sporulation sigma factor σ(F) to create a negative feedback

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82a07e2951497dcbc147b45bdebb8c04
https://doi.org/10.1111/mmi.13724

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Structure and Interactions of the TPR Domain of Sgt2 with Yeast Chaperones and Ybr137wp

Autor: Ewelina M. Krysztofinska, Nicola J. Evans, Arjun Thapaliya, James W. Murray, Rhodri M. L. Morgan, Santiago Martinez-Lumbreras, Rivka L. Isaacson

Publikováno v: Frontiers in Molecular Biosciences, Vol 4 (2017)

Small glutamine-rich tetratricopeptide repeat-containing protein 2 (Sgt2) is a multi-module co-chaperone involved in several protein quality control pathways. The TPR domain of Sgt2 and several other proteins, including SGTA, Hop, and CHIP, is a high

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::1eceb2c9b82ddc1d7ced1f2bc5d841e0

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Structure of the Sgt2/Get5 complex provides insights into GET-mediated targeting of tail-anchored membrane proteins

Autor: Peter Simpson, Stephen High, Rachael M. Goldstone, Aline C. Simon, James W. Murray, Rivka L. Isaacson, Ewelina M. Krysztofinska

Publikováno v: Proceedings of the National Academy of Sciences. 110:1327-1332

Small, glutamine-rich, tetratricopeptide repeat protein 2 (Sgt2) is the first known port of call for many newly synthesized tail-anchored (TA) proteins released from the ribosome and destined for the GET (Guided Entry of TA proteins) pathway. This le

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb9db10d94646c54c9b3b79129670b73
https://doi.org/10.1073/pnas.1207518110

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SGTA interacts with the proteasomal ubiquitin receptor Rpn13 via a carboxylate clamp mechanism

Autor: Santiago Martínez-Lumbreras, Isabelle L. Terry, Nicola J. Evans, Rivka L. Isaacson, Arjun Thapaliya, Ewelina M. Krysztofinska, Yvonne Nyathi, Stephen High

Publikováno v: Thapaliya, A, Nyathi, Y, Martinez Lumbreras, S, Krysztofinska, E, Evans, N, Terry, I L, High, S & Isaacson, R L 2016, ' SGTA interacts with the proteasomal ubiquitin receptor Rpn13 via a carboxylate clamp mechanism ', Scientific Reports, vol. 6, 36622 . https://doi.org/10.1038/srep36622
Scientific Reports

The fate of secretory and membrane proteins that mislocalize to the cytosol is decided by a collaboration between cochaperone SGTA (small, glutamine-rich, tetratricopeptide repeat protein alpha) and the BAG6 complex, whose operation relies on multipl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d9973c1c2a73abba49351a59e4b4e32
https://kclpure.kcl.ac.uk/en/publications/464dc9fe-eeac-4f4d-876a-904299e8849e

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Structural and functional insights into the E3 ligase, RNF126

Autor: Ewelina M, Krysztofinska, Santiago, Martínez-Lumbreras, Arjun, Thapaliya, Nicola J, Evans, Stephen, High, Rivka L, Isaacson

Publikováno v: Scientific Reports

RNF126 is an E3 ubiquitin ligase that collaborates with the BAG6 sortase complex to ubiquitinate hydrophobic substrates in the cytoplasm that are destined for proteasomal recycling. Composed of a trimeric complex of BAG6, TRC35 and UBL4A the BAG6 sor

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ea33ee962d6aa144b6a411d7242ac14c
https://pubmed.ncbi.nlm.nih.gov/27193484

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Structural and Functional Insights into Small, Glutamine-Rich, Tetratricopeptide Repeat Protein Alpha

Autor: Rivka L. Isaacson, Ewelina M. Krysztofinska, Joanna D. Roberts, Arjun Thapaliya, Santiago Martínez-Lumbreras

Publikováno v: Frontiers in Molecular Biosciences, Vol 2 (2015)
Frontiers in Molecular Biosciences
Roberts, J D, Thapaliya, A, Martínez-Lumbreras, S, Krysztofinska, E M & Isaacson, R L 2015, ' Structural and Functional Insights into Small, Glutamine-Rich, Tetratricopeptide Repeat Protein Alpha ', Frontiers in Bioscience, vol. 2, pp. 71 . https://doi.org/10.3389/fmolb.2015.00071

The small glutamine-rich, tetratricopeptide repeat-containing protein alpha (SGTA) is an emerging player in the quality control of secretory and membrane proteins mislocalized to the cytosol, with established roles in tail-anchored (TA) membrane prot

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f24867a9a9c804f607cd942709420213

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ZBTB17 (MIZ1) Is Important for the Cardiac Stress Response and a Novel Candidate Gene for Cardiomyopathy and Heart Failure

Autor: Byambajav Buyandelger, Martin Eilers, Rachel Buchan, Ju Chen, Albrecht Schmidt, Francesco Pesce, Norbert Hubner, Wilhelm Haverkamp, Angharad M. Roberts, Keat-Eng Ng, Peter Nürnberg, Francesco Mazzarotto, Michael D. Schneider, Rivka L. Isaacson, Enrico Petretto, Hendrik Milting, James S. Ware, Niels Teucher, Gerd Hasenfuss, Paul J.R. Barton, Enrique Lara-Pezzi, Conny Pfeiffer, Leanne E. Felkin, Thomas Brand, Martin Teichmann, Ian R. Gould, Heming Wei, Mohammad R. Toliat, Catherine Mansfield, Sylvia Gunkel, Thomas Braun, Sara J. McSweeney, Vera Regitz-Zagrosek, Jesús M. Gómez-Salinero, Declan P. O'Regan, Sawa Kostin, Andreas Perrot, Ewelina M. Krysztofinska, Marina López-Olañeta, Josee Vouffo, Onjee Choi, Sebastian Schafer, Ralph Knöll, Dudley J. Pennell, Sanjay Prasad, Gudrun Knöll, Kristina M. Ilieva

Background— Mutations in sarcomeric and cytoskeletal proteins are a major cause of hereditary cardiomyopathies, but our knowledge remains incomplete as to how the genetic defects execute their effects. Methods and Results— We used cysteine and gl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35a2bc1f43c46a768e4ae1aeb599a74e
http://hdl.handle.net/11379/545714

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Solution Structure of the SGTA Dimerisation Domain and Investigation of Its Interactions with the Ubiquitin-Like Domains of BAG6 and UBL4A

Autor: Aline C. Simon, Pawel Leznicki, Peter Simpson, Santiago Martínez-Lumbreras, Lisa R. Hale, David S. Bishop, Arjun Thapaliya, John F. Darby, Ewelina M. Krysztofinska, Rivka L. Isaacson, Newran Sriskandarajah, Stephen High, Caterina Alfano, Maria R. Conte

Publikováno v: Darby, J F, Krysztofinska, E M, Simpson, P J, Simon, A C, Leznicki, P, Sriskandarajah, N, Bishop, D S, Hale, L R, Alfano, C, Conte, M R, Martínez-Lumbreras, S, Thapaliya, A, High, S & Isaacson, R L 2014, ' Solution Structure of the SGTA Dimerisation Domain and Investigation of Its Interactions with the Ubiquitin-Like Domains of BAG6 and UBL4A ', PLOS One, vol. 9, no. 11, e113281 . https://doi.org/10.1371/journal.pone.0113281
PLoS ONE, Vol 9, Iss 11, p e113281 (2014)
PLoS ONE

Background The BAG6 complex resides in the cytosol and acts as a sorting point to target diverse hydrophobic protein substrates along their appropriate paths, including proteasomal degradation and ER membrane insertion. Composed of a trimeric complex

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d7dfb54b6c239d7d45bf64b655e9d102
https://kclpure.kcl.ac.uk/en/publications/00b58205-a08f-41e2-aac3-f41dc79d3e36

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