Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Vimal Parkash"'
Autor:
Vimal Parkash, Yashraj Kulkarni, Josy ter Beek, Polina V. Shcherbakova, Shina Caroline Lynn Kamerlin, Erik Johansson
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
Mutations in the human POLE gene are associated with tumours with high mutational loads. Here the authors provide a structural rationale for the mutagenic activity of the cancer-associated DNA polymerase ε P286R variant.
Externí odkaz:
https://doaj.org/article/347e31414f014ab19733e8e7a0a88110
Autor:
Heli Elovaara, Vimal Parkash, Ruth Fair-Mäkelä, Outi M H Salo-Ahen, Gabriela Guédez, Eva Bligt-Lindén, Janne Grönholm, Sirpa Jalkanen, Tiina A Salminen
Publikováno v:
PLoS ONE, Vol 11, Iss 11, p e0166935 (2016)
Sialic acid-binding immunoglobulin-like lectin-9 (Siglec-9) on leukocyte surface is a counter-receptor for endothelial cell surface adhesin, human primary amine oxidase (hAOC3), a target protein for anti-inflammatory agents. This interaction can be u
Externí odkaz:
https://doaj.org/article/8c28acb7f5c642b7be657bdfafb317fc
Evolution, three-dimensional model and localization of truncated hemoglobin PttTrHb of hybrid aspen.
Autor:
Estelle Dumont, Soile Jokipii-Lukkari, Vimal Parkash, Jaana Vuosku, Robin Sundström, Yvonne Nymalm, Suvi Sutela, Katariina Taskinen, Pauli T Kallio, Tiina A Salminen, Hely Häggman
Publikováno v:
PLoS ONE, Vol 9, Iss 2, p e88573 (2014)
Thus far, research on plant hemoglobins (Hbs) has mainly concentrated on symbiotic and non-symbiotic Hbs, and information on truncated Hbs (TrHbs) is scarce. The aim of this study was to examine the origin, structure and localization of the truncated
Externí odkaz:
https://doaj.org/article/b1279006955f429bbc608b193c2db0f5
Autor:
Stephanie R Barbari, Annette K Beach, Joel G Markgren, Vimal Parkash, Elizabeth A Moore, Erik Johansson, Polina V Shcherbakova
Publikováno v:
Nucleic Acids Research. 50:8023-8040
Amino acid substitutions in the exonuclease domain of DNA polymerase ϵ (Polϵ) cause ultramutated tumors. Studies in model organisms suggested pathogenic mechanisms distinct from a simple loss of exonuclease. These mechanisms remain unclear for most
Autor:
Pia Osterman, Erik Johansson, A. Elisabeth Sauer-Eriksson, Vimal Parkash, Göran O. Bylund, Josy ter Beek
Publikováno v:
'Nucleic Acids Research ', vol: 47, pages: 5712-5722 (2019)
Nucleic Acids Research
Nucleic Acids Research
DNA polymerase epsilon (Pol epsilon), the major leading-strand DNA polymerase in eukaryotes, has a catalytic subunit (Pol2) and three non-catalytic subunits. The N-terminal half of Pol2 (Pol2(CORE)) exhibits both polymerase and exonuclease activity.
Autor:
Erik Johansson, Yashraj Kulkarni, Shina Caroline Lynn Kamerlin, Vimal Parkash, Polina V. Shcherbakova, Josy ter Beek
Publikováno v:
'Nature Communications ', vol: 10, pages: 373-1-373-13 (2019)
Nature Communications
Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
Nature Communications
Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
The most frequently recurring cancer-associated DNA polymerase ε (Pol ε) mutation is a P286R substitution in the exonuclease domain. While originally proposed to increase genome instability by disrupting exonucleolytic proofreading, the P286R varia
Autor:
Esa Läärä, Soile Jokipii-Lukkari, Olga Blokhina, Robin Sundström, Nélida Leiva-Eriksson, Yvonne Nymalm, Hely Häggman, Pauli T. Kallio, J. Kalervo Hiltunen, Steffen Ohlmeier, Tiina A. Salminen, Vimal Parkash, Alexander J. Kastaniotis, Leif Bülow, Kurt V. Fagerstedt, Eija Kukkola
Publikováno v:
Plant science : an international journal of experimental plant biology. 247
Previous reports have connected non-symbiotic and truncated hemoglobins (Hbs) to metabolism of nitric oxide (NO), an important signalling molecule involved in wood formation. We have studied the capability of poplar (Populus tremula × tremuloides) H
Autor:
Anna-Maria Brandt, Henri Niskanen, Vimal Parkash, Jyrki Heino, Jarmo Käpylä, Tiina A. Salminen, Matti Lahti, Eva Bligt, Pekka Patrikainen, Johanna Jokinen
Publikováno v:
Journal of Biological Chemistry. 286:43343-43351
We have analyzed the structure and function of the integrin α(1)I domain harboring a gain-of-function mutation E317A. To promote protein crystallization, a double variant with an additional C139S mutation was used. In cell adhesion assays, the E317A
The structure of the conserved neurotrophic factors MANF and CDNF explains why they are bifunctional
Autor:
Mart Saarma, Adrian Goldman, Johan Peränen, Esko Oksanen, Vimal Parkash, Veli-Matti Leppänen, Nisse Kalkkinen, Päivi Lindholm
Publikováno v:
Protein Engineering Design and Selection
Protein Engineering Design and Selection; Vol 22
Protein Engineering Design and Selection; Vol 22
We have solved the structures of mammalian mesencephalic astrocyte-derived neurotrophic factor (MANF) and conserved dopamine neurotrophic factor (CDNF). CDNF protects and repairs midbrain dopaminergic neurons in vivo; MANF supports their survival in
Autor:
Mart Saarma, Heidi Virtanen, Adrian Goldman, Pia Runeberg-Roos, Vimal Parkash, Jaana M. Jurvansuu, Yulia Sidorova, Veli-Matti Leppänen, Maxim M. Bespalov
Publikováno v:
Journal of Biological Chemistry. 283:35164-35172
Glial cell line-derived neurotrophic factor (GDNF), a neuronal survival factor, binds its co-receptor GDNF family receptor α1 (GFRα1) in a 2:2 ratio and signals through the receptor tyrosine kinase RET. We have solved the GDNF2·GFRα12 complex str