Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Mārtiņš Otikovs"'
Publikováno v:
ProteinsREFERENCES. 89(5)
Lyme disease is the most widespread vector‐transmitted disease in North America and Europe, caused by infection with Borrelia burgdorferi sensu lato complex spirochetes. We report the solution NMR structure of the B. burgdorferi outer surface lipop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2247e19af3506cf190d1f314998c1a9f
https://pubmed.ncbi.nlm.nih.gov/32949018
https://pubmed.ncbi.nlm.nih.gov/32949018
Autor:
Martins Otikovs, Noam Nissan, Edna Furman-Haran, Debbie Anaby, Ravit Agassi, Miri Sklair-Levy, Lucio Frydman
Publikováno v:
Diagnostics, Vol 13, Iss 23, p 3516 (2023)
Quantitative correlations between T2 and ADC values were explored on cancerous breast lesions using spatiotemporally encoded (SPEN) MRI. To this end, T2 maps of patients were measured at more than one b-value, and ADC maps at several echo time values
Externí odkaz:
https://doaj.org/article/c27adde6e7684b8188f1d76c685953a4
Autor:
Megija Šede, Jēkabs Fridmanis, Martins Otikovs, Jan Johansson, Anna Rising, Nina Kronqvist, Kristaps Jaudzems
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
The spidroin N-terminal domain (NT) is responsible for high solubility and pH-dependent assembly of spider silk proteins during storage and fiber formation, respectively. It forms a monomeric five-helix bundle at neutral pH and dimerizes at lowered p
Externí odkaz:
https://doaj.org/article/f4058a6ac28b4096adb54c9e3563d646
Autor:
Nina Kronqvist, Médoune Sarr, Anton Lindqvist, Kerstin Nordling, Martins Otikovs, Luca Venturi, Barbara Pioselli, Pasi Purhonen, Michael Landreh, Henrik Biverstål, Zigmantas Toleikis, Lisa Sjöberg, Carol V. Robinson, Nicola Pelizzi, Hans Jörnvall, Hans Hebert, Kristaps Jaudzems, Tore Curstedt, Anna Rising, Jan Johansson
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-15 (2017)
The properties of many transmembrane or aggregation-prone proteins make them difficult to recombinantly express. Here the authors use a modified N-terminal domain of a spider silk protein to express and purify several difficult to express proteins at
Externí odkaz:
https://doaj.org/article/6e88916356bd45a19c0f201d1ebfd6e8
Autor:
Marlene Andersson, Gefei Chen, Martins Otikovs, Michael Landreh, Kerstin Nordling, Nina Kronqvist, Per Westermark, Hans Jörnvall, Stefan Knight, Yvonne Ridderstråle, Lena Holm, Qing Meng, Kristaps Jaudzems, Mitchell Chesler, Jan Johansson, Anna Rising
Publikováno v:
PLoS Biology, Vol 12, Iss 8, p e1001921 (2014)
Spider silk fibers are produced from soluble proteins (spidroins) under ambient conditions in a complex but poorly understood process. Spidroins are highly repetitive in sequence but capped by nonrepetitive N- and C-terminal domains (NT and CT) that
Externí odkaz:
https://doaj.org/article/515cf5c1c8cc4539aa383c6277366ab2