Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Ari T. MARTTILA"'
Autor:
Eevaleena J. Porkka, Vesa P. Hytönen, Olli H. Laitinen, Ari T. Marttila, Tuomas Kulomaa, Jarno Hörhä, Henri R. Nordlund, Thomas K.M. Nyholm, Markku S. Kulomaa, David E. Hyre, Patrick S. Stayton
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 61:597-607
A recently reported dual-chain avidin was modified further to contain two distinct, independent types of ligand-binding sites within a single polypeptide chain. Chicken avidin is normally a tetrameric glycoprotein that binds water-soluble d-biotin wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a7f6facc005aa576ed21fb570f38b31
https://doi.org/10.1002/prot.20604
https://doi.org/10.1002/prot.20604
Autor:
Ari T. Marttila, Varpu Marjomäki, Olli H. Laitinen, Kari J. Airenne, Seppo Ylä-Herttuala, Markku S. Kulomaa, Vesa P. Hytönen, Anssi J. Mähönen, Jani K. Raty, Pauliina Lehtolainen
Publikováno v:
Molecular Therapy. 9(2):282-291
Flexible alteration of virus surface properties would be beneficial for enhanced and targeted gene delivery. A useful approach could be based on a high-affinity receptor–ligand pair, such as avidin and biotin. In this study, we have constructed an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9cb06a9f25b6ed23dc4268bdd7359378
Autor:
Kari Airenne, A K Taskinen, Ari T. Marttila, Michael A. Horton, Lappalainen M, Petri Lehenkari, Varpu Marjomäki, Kalevi J. Pulkkanen, Seppo Ylä-Herttuala, Olli Leppänen, Markku S. Kulomaa, T. Wirth, P. Lehtolainen
Publikováno v:
Gene Therapy. 10:2090-2097
The very high binding affinity of avidin to biotin is one of the highest to occur in nature. We constructed a fusion protein composed of avidin and the endocytotic LDL receptor in order to target biotinylated molecules to cells of the desired tissues
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b99c4245f9e3be20fad0ea4ad6ae3eff
https://doi.org/10.1038/sj.gt.3302120
https://doi.org/10.1038/sj.gt.3302120
Autor:
Vesa P. Hytönen, Meir Wilchek, Markku S. Kulomaa, Olli H. Laitinen, Ari T. Marttila, Edward A. Bayer
Publikováno v:
Biochemical Journal. 369:249-254
The strong interaction between avidin and biotin is so tight (dissociation constant 10-15M) that conditions usually sufficient for protein denaturing fail to dislodge biotin from the avidin—biotin complex. This kind of irreversible binding hinders
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cba8c2911eb6e4d27f5151b212a9d175
https://doi.org/10.1042/bj20020886
https://doi.org/10.1042/bj20020886
Autor:
Olli H. LAITINEN, Vesa P. HYTÖNEN, Mervi K. AHLROTH, Olli T. PENTIKÄINEN, Ciara GALLAGHER, Henri R. NORDLUND, Vladimir OVOD, Ari T. MARTTILA, Eevaleena PORKKA, Sanna HEINO, Mark S. JOHNSON, Kari J. AIRENNE, Markku S. KULOMAA
Publikováno v:
Biochemical Journal. 363:609-617
Chicken avidin and bacterial streptavidin are proteins familiar from their use in various (strept)avidin—biotin technological applications. Avidin binds the vitamin biotin with the highest affinity known for non-covalent interactions found in natur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6698ddba00f494cc420597ae28ecaf77
https://doi.org/10.1042/bj3630609
https://doi.org/10.1042/bj3630609
Autor:
Kari J. Airenne, Olli H. Laitinen, Tikva Kulik, Markku S. Kulomaa, Meir Wilchek, Oded Livnah, Ari T. Marttila, Edward A. Bayer
Publikováno v:
Journal of Biological Chemistry. 276:8219-8224
Chicken avidin, a homotetramer that binds four molecules of biotin was converted to a monomeric form by successive mutations of interface residues to alanine. The major contribution to monomer formation was the mutation of two aspartic acid residues,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2e3ceef1e80c223619eb3015eeb85954
https://doi.org/10.1074/jbc.m007930200
https://doi.org/10.1074/jbc.m007930200
Autor:
Thomas K.M. Nyholm, Olli H. Laitinen, Giovanni Paganelli, Markku S. Kulomaa, Anu Kettunen, Alessandro Grapputo, Henri R. Nordlund, Ari T. Marttila, Vesa P. Hytönen, Janne Savolainen, Nisse Kalkkinen
Chicken avidin and bacterial streptavidin are proteins used in a wide variety of applications in the life sciences due to their strong affinity for biotin. A new and promising use for them is in medical pretargeting cancer treatments. However, their
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78967b54aebb9f4e37ff897b0c6710b8
https://europepmc.org/articles/PMC1223360/
https://europepmc.org/articles/PMC1223360/
Autor:
Kari J. Airenne, Vesa P. Hytönen, Janne Savolainen, Sanna T.H. Uotila, Meir Wilchek, Oded Livnah, Olli H. Laitinen, Markku S. Kulomaa, Henri R. Nordlund, Ari T. Marttila, Edward A. Bayer
Publikováno v:
The Journal of biological chemistry. 278(6)
Homotetrameric chicken avidin that binds four molecules of biotin was converted to a monomeric form (monoavidin) by mutations of two interface residues: tryptophan 110 in the 1 --> 2 interface was mutated to lysine and asparagine 54 in the 1 --> 4 in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::554c7cce4523cf36328f387332f13c32
https://pubmed.ncbi.nlm.nih.gov/12458212
https://pubmed.ncbi.nlm.nih.gov/12458212
Autor:
Olli H, Laitinen, Vesa P, Hytönen, Mervi K, Ahlroth, Olli T, Pentikäinen, Ciara, Gallagher, Henri R, Nordlund, Vladimir, Ovod, Ari T, Marttila, Eevaleena, Porkka, Sanna, Heino, Mark S, Johnson, Kari J, Airenne, Markku S, Kulomaa
Publikováno v:
The Biochemical journal. 363(Pt 3)
Chicken avidin and bacterial streptavidin are proteins familiar from their use in various (strept)avidin-biotin technological applications. Avidin binds the vitamin biotin with the highest affinity known for non-covalent interactions found in nature.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::25adae9331a8e1656377acf7f3084a51
https://pubmed.ncbi.nlm.nih.gov/11964162
https://pubmed.ncbi.nlm.nih.gov/11964162
Autor:
Meir Wilchek, Markku S. Kulomaa, Olli H. Laitinen, Kari J. Airenne, Tikva Kulik, Ari T. Marttila, Edward A. Bayer
Publikováno v:
FEBS letters. 441(2)
Avidin, a positively charged egg-white glycoprotein, is a widely used tool in biotechnological applications because of its ability to bind biotin strongly. The high pI of avidin (approximately 10.5), however, is a hindrance in certain applications du
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0fabfff234c8a544b9dd0b3e7ee7e651
https://pubmed.ncbi.nlm.nih.gov/9883906
https://pubmed.ncbi.nlm.nih.gov/9883906