Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Juho Kellosalo"'
Autor:
Kun-Mou Li, Craig Wilkinson, Juho Kellosalo, Jia-Yin Tsai, Tommi Kajander, Lars J. C. Jeuken, Yuh-Ju Sun, Adrian Goldman
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
In some parasites, membrane-bound pyrophosphatases, which couple proton and sodium ion transport across the membrane, are important for infectivity. Here, the authors report crystal structures of these proteins alongside biophysical analyses that all
Externí odkaz:
https://doaj.org/article/9bf03144000f411fad9765f84873b5f9
Signal peptides are short amino acid segments present at the N-terminus of newly synthesized proteins that facilitate protein translocation into the lumen of the endoplasmic reticulum, after which they are cleaved off. Specific regions of signal pept
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c7ce3e48816a8c45f6477f186cc17e8a
https://doi.org/10.1101/2022.06.02.493958
https://doi.org/10.1101/2022.06.02.493958
Autor:
Jane E. Ishmael, Juho Kellosalo, Anja O. Paatero, Shinya Oishi, Soheila Kazemi, Jeffrey D. Serrill, Uwe Richter, Shinsaku Kawaguchi, Ville O. Paavilainen, Daphne R. Mattos, Christopher C. Thornburg, Walter K. Vogel, Xuemei Wan, Dale Tranter, Kerry L. McPhail
Publikováno v:
ACS Chemical Biology
Coibamide A (CbA) is a marine natural product with potent antiproliferative activity against human cancer cells and a unique selectivity profile. Despite promising antitumor activity, the mechanism of cytotoxicity and specific cellular target of CbA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5fca17dd4f6b29f56e39ec7d5d1c5124
http://hdl.handle.net/10138/319505
http://hdl.handle.net/10138/319505
Autor:
Britta Knapp, Thomas Lochmann, Juho Kellosalo, Dale Tranter, David Estoppey, Dominic Hoepfner, Dominik Pistorius, Axel Meissner, Ireos Filipuzzi, Ville O. Paavilainen
Publikováno v:
Journal of Natural Products
Kendomycin is a small-molecule natural product that has gained significant attention due to reported cytotoxicity against pathogenic bacteria and fungi as well as a number of cancer cell lines. Despite significant biomedical interest and attempts to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2a37b917cb9ec474a44bc530a16806e
http://hdl.handle.net/10138/320332
http://hdl.handle.net/10138/320332
Autor:
Dale Tranter, Anja Paatero, Shinsaku Kawaguchi, Soheila Kazemi, Jeffrey D. Serrill, Juho Kellosalo, Walter K. Vogel, Uwe Richter, Christopher C. Thornburg, Shinya Oishi, Kerry L. McPhail, Jane E. Ishmael, Ville Paavilainen
Coibamide A (CbA) is a marine natural product with potent antiproliferative activity against human cancer cells and a unique selectivity profile. Despite promising antitumor activity, the mechanism of cytotoxicity and specific cellular target remain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78e9408df5769a427dc35c48a97723dc
https://doi.org/10.26434/chemrxiv.10092182
https://doi.org/10.26434/chemrxiv.10092182
Autor:
Bryan M. Dunyak, William H. Gerwick, Juho Kellosalo, Jack Taunton, Jehad Almaliti, Jason E. Gestwicki, Ville O. Paavilainen, Anja O. Paatero
Publikováno v:
Cell Chemical Biology. 23:561-566
Apratoxin A is a cytotoxic natural product that prevents the biogenesis of secretory and membrane proteins. Biochemically, apratoxin A inhibits cotranslational translocation into the ER, but its cellular target and mechanism of action have remained c
Membrane-bound pyrophosphatases (mPPases) are homodimeric integral membrane proteins that hydrolyse pyrophosphate into orthophosphates coupled to the active transport of protons or sodium ions across membranes. They occur in bacteria, archaea, plants
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d42417a67abe8b86ef60e0bfd0d6123f
http://hdl.handle.net/10138/237234
http://hdl.handle.net/10138/237234
Autor:
Juho Kellosalo, Adrian Goldman
Publikováno v:
Encyclopedia of Inorganic and Bioinorganic Chemistry
Membrane-bound pyrophosphatases (M-PPases) are homodimeric enzymes that couple the vectorial transport of protons and/or sodium ions to pyrophosphate (PPi) hydrolysis or synthesis. They are found in prokaryotes, plants, and protists and are thus pres
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::139c5194ecc6b7e2bfe5c931c742ad08
https://doi.org/10.1002/9781119951438.eibc2268
https://doi.org/10.1002/9781119951438.eibc2268
Publikováno v:
Current opinion in structural biology. 27
Membrane-bound pyrophosphatases (M-PPases) are homodimeric enzymes that couple the generation and utilization of membrane potentials to pyrophosphate (PPi) hydrolysis and synthesis. Since the discovery of the link between PPi use and proton transport
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 71:s23-s24