Zobrazeno 1 - 10
of 47
pro vyhledávání: '"Tuomo Glumoff"'
Autor:
Antti Hassinen, Fawzi Khoder-Agha, Elham Khosrowabadi, Daniela Mennerich, Deborah Harrus, Maxence Noel, Elitsa Y. Dimova, Tuomo Glumoff, Anne Harduin-Lepers, Thomas Kietzmann, Sakari Kellokumpu
Publikováno v:
Redox Biology, Vol 24, Iss , Pp - (2019)
Glycosylation, a common modification of cellular proteins and lipids, is often altered in diseases and pathophysiological states such as hypoxia, yet the underlying molecular causes remain poorly understood. By utilizing lectin microarray glycan prof
Externí odkaz:
https://doaj.org/article/412cfa2ca46241bdb0cf7f9892aaa153
Autor:
Deborah Harrus, Fawzi Khoder-Agha, Miika Peltoniemi, Antti Hassinen, Lloyd Ruddock, Sakari Kellokumpu, Tuomo Glumoff
Publikováno v:
PLoS ONE, Vol 13, Iss 10, p e0205571 (2018)
Most glycosyltransferases, including B4GalT1 (EC 2.4.1.38), are known to assemble into enzyme homomers and functionally relevant heteromers in vivo. However, it remains unclear why and how these enzymes interact at the molecular/atomic level. Here, w
Externí odkaz:
https://doaj.org/article/c31236d83f934f24a5bec6bf9cfb54f6
Publikováno v:
PLoS ONE, Vol 8, Iss 1, p e53688 (2013)
Molecular basis of D-bifunctional protein (D-BP) deficiency was studied with wild type and five disease-causing variants of 3R-hydroxyacyl-CoA dehydrogenase fragment of the human MFE-2 (multifunctional enzyme type 2) protein. Complementation analysis
Externí odkaz:
https://doaj.org/article/a4b1ec5485804990a6b27f3921a68a2f
Autor:
J. Kalervo Hiltunen, Tuomo Glumoff, Alexander J. Kastaniotis, Zhijun Chen, Guangyu Jiang, Kaija J. Autio
Publikováno v:
Molecular and Cellular Endocrinology. 489:107-118
17β-Hydroxysteroid dehydrogenases (HSD17B) catalyze the oxidation/reduction of 17β-hydroxy/keto group in position C17 in C18- and C19 steroids. Most HSD17Bs are also catalytically active with substrates other than steroids. A subset of these enzyme
Publikováno v:
Journal of Structural Biology
Journal of Structural Biology, 2020, 212 (2), pp.107628. ⟨10.1016/j.jsb.2020.107628⟩
Journal of Structural Biology, Elsevier, 2020, 212 (2), pp.107628. ⟨10.1016/j.jsb.2020.107628⟩
Journal of Structural Biology, 2020, 212 (2), pp.107628. ⟨10.1016/j.jsb.2020.107628⟩
Journal of Structural Biology, Elsevier, 2020, 212 (2), pp.107628. ⟨10.1016/j.jsb.2020.107628⟩
Sialic acid residues found as terminal monosaccharides in various types of glycan chains in cell surface glycoproteins and glycolipids have been identified as important contributors of cell-cell interactions in normal vs. abnormal cellular behavior a
Publikováno v:
BioEssays. 44:2100240
ADP-ribosylation is a post-translational modification catalyzed by writer enzymes - ADP-ribosyltransferases. The modification is part of many signaling events, can modulate the function and stability of target proteins, and often results in the recru
Publikováno v:
Cellular and Molecular Life Sciences. 75:833-848
Glycosyltransferases (GTases) transfer sugar moieties to proteins, lipids or existing glycan or polysaccharide molecules. GTases form an important group of enzymes in the Golgi, where the synthesis and modification of glycoproteins and glycolipids ta
Autor:
Fawzi Khoder-Agha, Tuomo Glumoff, Anne Harduin-Lepers, Marc F. Lensink, Guillaume Brysbaert, Deborah Harrus, Sakari Kellokumpu
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2019, 294 (39), pp.14383-14393. ⟨10.1074/jbc.RA119.009539⟩
J Biol Chem
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2019, pp.jbc.RA119.009539. ⟨10.1074/jbc.RA119.009539⟩
Journal of Biological Chemistry, 2019, 294 (39), pp.14383-14393. ⟨10.1074/jbc.RA119.009539⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2019, 294 (39), pp.14383-14393. ⟨10.1074/jbc.RA119.009539⟩
J Biol Chem
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2019, pp.jbc.RA119.009539. ⟨10.1074/jbc.RA119.009539⟩
Journal of Biological Chemistry, 2019, 294 (39), pp.14383-14393. ⟨10.1074/jbc.RA119.009539⟩
International audience; Edited by Gerald W. Hart -1,4-Galactosyltransferase 1 (B4GALT1) and ST6 -galac-toside ␣-2,6-sialyltransferase 1 (ST6GAL1) catalyze the successive addition of terminal -1,4-linked galactose and ␣-2,6-linked sialic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47fbc49d6bcacd95a9df8db9d86b708d
https://hal.archives-ouvertes.fr/hal-02343482
https://hal.archives-ouvertes.fr/hal-02343482
Autor:
Thomas Kietzmann, Deborah Harrus, Elham Khosrowabadi, Daniela Mennerich, Antti Hassinen, Sakari Kellokumpu, Anne Harduin-Lepers, Fawzi Khoder-Agha, Elitsa Y. Dimova, Tuomo Glumoff, Maxence Noel
Publikováno v:
Redox Biology
Redox Biology, Elsevier, 2019, 24, pp.101182. ⟨10.1016/j.redox.2019.101182⟩
Redox Biology, 2019, 24, pp.101182. ⟨10.1016/j.redox.2019.101182⟩
Redox Biology, Vol 24, Iss, Pp-(2019)
Redox Biology, Elsevier, 2019, 24, pp.101182. ⟨10.1016/j.redox.2019.101182⟩
Redox Biology, 2019, 24, pp.101182. ⟨10.1016/j.redox.2019.101182⟩
Redox Biology, Vol 24, Iss, Pp-(2019)
Glycosylation, a common modification of cellular proteins and lipids, is often altered in diseases and pathophysiological states such as hypoxia, yet the underlying molecular causes remain poorly understood. By utilizing lectin microarray glycan prof
Autor:
Tuomo Glumoff, Thomas Kietzmann, Nina Kokkonen, Sakari Kellokumpu, Deborah Harrus, Antti Hassinen, Elham Khosrowabadi
Aims: Carcinoembryonic antigen (CEACAM5, CEA) is a known tumor marker for colorectal cancer that localizes in a polarized manner to the apical surface in normal colon epithelial cells whereas in cancer cells it is present at both the apical and basol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f0907bd42f289a6634fd21b3c1cb263
http://urn.fi/urn:nbn:fi-fe2019071022983
http://urn.fi/urn:nbn:fi-fe2019071022983