Zobrazeno 1 - 10
of 144
pro vyhledávání: '"Markku S. KULOMAA"'
Autor:
Nitin Agrawal, Soili I Lehtonen, Meri Uusi-Mäkelä, Purvi Jain, Sari Viitala, Juha A E Määttä, Niklas Kähkönen, Latifeh Azizi, Tiina A Riihimäki, Markku S Kulomaa, Mark S Johnson, Vesa P Hytönen, Tomi T Airenne
Publikováno v:
PLoS ONE, Vol 14, Iss 2, p e0212339 (2019)
Chicken avidin (Avd) and streptavidin from Streptomyces avidinii are extensively used in bionanotechnology due to their extremely tight binding to biotin (Kd ~ 10-15 M for chicken Avd). We previously reported engineered Avds known as antidins, which
Externí odkaz:
https://doaj.org/article/addaf38daa174d15b4a834c6349f099d
Autor:
Nitin Agrawal, Juha A E Määttä, Markku S Kulomaa, Vesa P Hytönen, Mark S Johnson, Tomi T Airenne
Publikováno v:
PLoS ONE, Vol 12, Iss 4, p e0176086 (2017)
Bradavidin is a tetrameric biotin-binding protein similar to chicken avidin and bacterial streptavidin, and was originally cloned from the nitrogen-fixing bacteria Bradyrhizobium diazoefficiens. We have previously reported the crystal structure of th
Externí odkaz:
https://doaj.org/article/06a88481ded44a36a0b742921da3e389
Autor:
Barbara Taskinen, Tomi T Airenne, Janne Jänis, Rolle Rahikainen, Mark S Johnson, Markku S Kulomaa, Vesa P Hytönen
Publikováno v:
PLoS ONE, Vol 9, Iss 3, p e92058 (2014)
Avidins are a family of proteins widely employed in biotechnology. We have previously shown that functional chimeric mutant proteins can be created from avidin and avidin-related protein 2 using a methodology combining random mutagenesis by recombina
Externí odkaz:
https://doaj.org/article/e9426aca06ff43049770e7730ba55592
Autor:
Helena Tossavainen, Sampo Kukkurainen, Juha A E Määttä, Niklas Kähkönen, Tero Pihlajamaa, Vesa P Hytönen, Markku S Kulomaa, Perttu Permi
Publikováno v:
PLoS ONE, Vol 9, Iss 6, p e100564 (2014)
Chimeric avidin (ChiAVD) is a product of rational protein engineering remarkably resistant to heat and harsh conditions. In quest of the fundamentals behind factors affecting stability we have elucidated the solution NMR spectroscopic structure of th
Externí odkaz:
https://doaj.org/article/acb133fd2df44da89ad01488a8d8f4c1
Autor:
Barbara Taskinen, Joanna Zmurko, Markus Ojanen, Sampo Kukkurainen, Marimuthu Parthiban, Juha A E Määttä, Jenni Leppiniemi, Janne Jänis, Mataleena Parikka, Hannu Turpeinen, Mika Rämet, Marko Pesu, Mark S Johnson, Markku S Kulomaa, Tomi T Airenne, Vesa P Hytönen
Publikováno v:
PLoS ONE, Vol 8, Iss 10, p e77207 (2013)
The avidin protein family members are well known for their high affinity towards D-biotin and high structural stability. These properties make avidins valuable tools for a wide range of biotechnology applications. We have identified a new member of t
Externí odkaz:
https://doaj.org/article/67b93c0e76414e249b27e076ce4178f7
Autor:
Jenni Leppiniemi, Toni Grönroos, Juha A E Määttä, Mark S Johnson, Markku S Kulomaa, Vesa P Hytönen, Tomi T Airenne
Publikováno v:
PLoS ONE, Vol 7, Iss 5, p e35962 (2012)
Bradavidin is a homotetrameric biotin-binding protein from Bradyrhizobium japonicum, a nitrogen fixing and root nodule-forming symbiotic bacterium of the soybean. Wild-type (wt) bradavidin has 138 amino acid residues, whereas the C-terminally truncat
Externí odkaz:
https://doaj.org/article/e1e3167e1c6743e0a1ae020c0ad4ce11
Autor:
Jenni Leppiniemi, Juha A E Määttä, Henrik Hammaren, Mikko Soikkeli, Mikko Laitaoja, Janne Jänis, Markku S Kulomaa, Vesa P Hytönen
Publikováno v:
PLoS ONE, Vol 6, Iss 1, p e16576 (2011)
The extensive use of avidin and streptavidin in life sciences originates from the extraordinary tight biotin-binding affinity of these tetrameric proteins. Numerous studies have been performed to modify the biotin-binding affinity of (strept)avidin t
Externí odkaz:
https://doaj.org/article/1371767d19524fb4a9a0ef731d4811d5
Autor:
Tiina A Riihimäki, Sampo Kukkurainen, Suvi Varjonen, Jarno Hörhä, Thomas K M Nyholm, Markku S Kulomaa, Vesa P Hytönen
Publikováno v:
PLoS ONE, Vol 6, Iss 5, p e20535 (2011)
BACKGROUND: Avidin is a chicken egg-white protein with high affinity to vitamin H, also known as D-biotin. Many applications in life science research are based on this strong interaction. Avidin is a homotetrameric protein, which promotes its modific
Externí odkaz:
https://doaj.org/article/aafe2a26b2ed4d0d8dd4e0fdede9eb28
Autor:
Markku S. Kulomaa, Sampo Kukkurainen, Tiina A. Riihimäki, Nitin Agrawal, Masi Koskinen, Mark S. Johnson, Antti Tullila, Niklas Kähkönen, Tomi T. Airenne, Tarja K. Nevanen, Soili I. Lehtonen, Vesa P. Hytönen
Publikováno v:
Lehtonen, S I, Tullila, A, Agrawal, N, Kukkurainen, S, Kähkönen, N, Koskinen, M, Nevanen, T K, Johnson, M S, Airenne, T T, Kulomaa, M S, Riihimäki, T A & Hytönen, V P 2016, ' Artificial avidin-based receptors for a panel of small molecules ', ACS Chemical Biology, vol. 11, no. 1, pp. 211-221 . https://doi.org/10.1021/acschembio.5b00906
Proteins with high specificity, affinity, and stability are needed for biomolecular recognition in a plethora of applications. Antibodies are powerful affinity tools, but they may also suffer from limitations such as low stability and high production
His-tagged norovirus-like particles : a versatile platform for cellular delivery and surface display
Autor:
Markku S. Kulomaa, Ralph Wieneke, Vesna Blazevic, Tiia Koho, Robert Tampé, Varpu Marjomäki, Rolle Rahikainen, Teemu O. Ihalainen, Hanni Uusi-Kerttula, Vesa P. Hytönen, Marie Stark
Publikováno v:
European Journal of Pharmaceutics and Biopharmaceutics. 96:22-31
In addition to vaccines, noninfectious virus-like particles (VLPs) that mimic the viral capsid show an attractive possibility of presenting immunogenic epitopes or targeting molecules on their surface. Here, functionalization of norovirus-derived VLP