Výsledky vyhledávání - "Morten K. Grøftehauge"

Akademický článek

Structural and Biochemical Characterization of Chlamydia trachomatis DsbA Reveals a Cysteine-Rich and Weakly Oxidising Oxidoreductase.

Autor: Signe Christensen, Morten K Grøftehauge, Karl Byriel, Wilhelmina M Huston, Emily Furlong, Begoña Heras, Jennifer L Martin, Róisín M McMahon

Publikováno v: PLoS ONE, Vol 11, Iss 12, p e0168485 (2016)

The Gram negative bacteria Chlamydia trachomatis is an obligate intracellular human pathogen that can cause pelvic inflammatory disease, infertility and blinding trachoma. C. trachomatis encodes a homolog of the dithiol oxidoreductase DsbA. Bacterial

Externí odkaz: https://doaj.org/article/e9ee2f4b96be47488c0921f366f16e95

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Functional and phylogenetic evidence of a bacterial origin for the first enzyme in sphingolipid biosynthesis in a phylum of eukaryotic protozoan parasites

Autor: Paul W. Denny, Ehmke Pohl, Amjed Qays Al-Qaisi, Morten K. Grøftehauge, Louise E. Bird, Hosam Shams-Eldin, Julie K. Thye, Steven Pratt, Robert H. Dods, Jackie A. Mosely, John G. Mina, Ralph T. Schwarz

Publikováno v: The Journal of Biological Chemistry
Journal of biological chemistry, 2017, Vol.292(29), pp.12208-12219 [Peer Reviewed Journal]

Toxoplasma gondii is an obligate, intracellular eukaryotic apicomplexan protozoan parasite that can cause fetal damage and abortion in both animals and humans. Sphingolipids are essential and ubiquitous components of eukaryotic membranes that are bot

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca7d2f9725c0290d3ed912353f3931f1
https://doi.org/10.1074/jbc.m117.792374

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Crystal Structure of a Hidden Protein, YcaC, a Putative Cysteine Hydrolase from Pseudomonas aeruginosa, with and without an Acrylamide Adduct

Autor: Michael L. Vasil, Daphné Truan, Morten K. Grøftehauge, Adriana I. Vasil, Paul W. Denny, Ehmke Pohl

Publikováno v: International Journal of Molecular Sciences
International journal of molecular sciences, 2015, Vol.16(7), pp.15971-15984 [Peer Reviewed Journal]
International Journal of Molecular Sciences, Vol 16, Iss 7, Pp 15971-15984 (2015)
Volume 16
Issue 7
Pages 15971-15984

As part of the ongoing effort to functionally and structurally characterize virulence factors in the opportunistic pathogen Pseudomonas aeruginosa, we determined the crystal structure of YcaC co-purified with the target protein at resolutions of 2.34

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5717dc9d30e84138a7185cc21e54cd10
https://doi.org/10.3390/ijms160715971

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Protein–ligand interactions investigated by thermal shift assays (TSA) and dual polarization interferometry (DPI)

Autor: Nelly R. Hajizadeh, Ehmke Pohl, Marcus J. Swann, Morten K. Grøftehauge

Publikováno v: Acta Crystallographica Section D: Biological Crystallography

The biophysical characterization of protein–ligand interactions in solution using techniques such as thermal shift assay, or on surfaces using, for example, dual polarization interferometry, plays an increasingly important role in complementing cry

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d7dd237d61cf73066fef36672d163a0
https://doi.org/10.1107/s1399004714016617

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Revisiting the structure of the Vps10 domain of human sortilin and its interaction with neurotensin

Autor: Peder Madsen, Morten K. Grøftehauge, Esben S. Sørensen, Esben M. Quistgaard, Poul Nissen, Lone Tjener Pallesen, Brian Christensen, Søren Thirup, Claus Munck Petersen

Publikováno v: Protein Science. 23:1291-1300

Sortilin is a multifunctional receptor involved in sorting and apoptosis. We have previously reported a 2.0-A structure of the Vps10 ectodomain in complex with one of its ligands, the tridecapeptide neurotensin. Here we set out to further characteriz

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::befda019a5007f08af77436705278773
https://doi.org/10.1002/pro.2512

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Structural and Biochemical Characterization of Chlamydia trachomatis DsbA Reveals a Cysteine-Rich and Weakly Oxidising Oxidoreductase

Autor: Wilhelmina M. Huston, Begoña Heras, Morten K. Grøftehauge, Signe Christensen, Róisín M. McMahon, Emily Furlong, Jennifer L. Martin, Karl A. Byriel

Publikováno v: PLoS ONE
PLoS ONE, Vol 11, Iss 12, p e0168485 (2016)

Copyright © 2016 Christensen et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9fecd83a8a6fc4b4d608101bcd11ab9b
https://doi.org/10.1371/journal.pone.0168485

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Identifying ligand-binding hot spots in proteins using brominated fragments

Autor: J. Preben Morth, Morten K. Grøftehauge, Poul Nissen, Troels Skrydstrup, M. Therkelsen, Rolf H. Taaning

Publikováno v: Grøftehauge, M K, Therkelsen, M O, Taaning, R, Skrydstrup, T, Morth, J P & Nissen, P 2013, ' Identifying ligand-binding hot spots in proteins using brominated fragments ', Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, vol. 69, no. Pt 9, pp. 1060-1065 . https://doi.org/10.1107/S1744309113018551

High-quality crystals of Thermus thermophilus EF-Tu in the GTP-bound conformation at 1.7-2.7 Å resolution were used to test 18 small organic molecules, all brominated for confident identification in the anomalous difference maps. From this relativel

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6dda4fe06c46865d6ac7be79995530fe
https://pure.au.dk/portal/da/publications/identifying-ligandbinding-hot-spots-in-proteins-using-brominated-fragments(2af4f99b-08ca-4e58-b815-0ecfb5f74419).html

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Ligands bind to Sortilin in the tunnel of a ten-bladed beta-propeller domain

Autor: Morten K. Grøftehauge, Claus Munck Petersen, Søren Thirup, Esben M. Quistgaard, Peder Madsen, Poul Nissen

Publikováno v: Nature structural & molecular biology 16(1), 96-98 (2009). doi:10.1038/nsmb.1543
Quistgaard, E M, Madsen, P, Grøftehauge, M K, Nissen, P, Petersen, C M & Thirup, S S 2009, ' Ligands bind to Sortilin in the tunnel of a ten-bladed beta-propeller domain ', Nature Structural and Molecular Biology, vol. 16, no. 1, pp. 96-8 . https://doi.org/10.1038/nsmb.1543

Nature structural & molecular biology 16(1), 96-98 (2009). doi:10.1038/nsmb.1543
Published by Nature Publishing Group, London [u.a.]

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35895e2266ada2e05cb6a218f2cdeeec
https://pubmed.ncbi.nlm.nih.gov/19122660

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