O
Olli T. Pentikäinen
Researcher at University of Turku
Publications - 99
Citations - 3345
Olli T. Pentikäinen is an academic researcher from University of Turku. The author has contributed to research in topics: Virtual screening & Integrin. The author has an hindex of 30, co-authored 93 publications receiving 2911 citations. Previous affiliations of Olli T. Pentikäinen include University of Bristol & Finnish Institute of Occupational Health.
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BODIL: a molecular modeling environment for structure-function analysis and drug design
Jukka V. Lehtonen,Dan-Johan Still,Ville-Veikko Rantanen,Jan Ekholm,Dag Björklund,Zuhair Iftikhar,Mikko Huhtala,Susanna Repo,Antti Jussila,Jussi Jaakkola,Olli T. Pentikäinen,Tommi Nyrönen,Tiina A. Salminen,Mats Gyllenberg,Mats Gyllenberg,Mark S. Johnson +15 more
TL;DR: BODIL is a molecular modeling environment geared to help the user to quickly identify key features of proteins critical to molecular recognition, especially in drug discovery applications, and to understand the structural basis for function.
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Selective Binding of Collagen Subtypes by Integrin α1I, α2I, and α10I Domains
Mira Tulla,Olli T. Pentikäinen,Tiina Viitasalo,Jarmo Käpylä,Ulla Impola,Petri Nykvist,Liisa Nissinen,Liisa Nissinen,Mark S. Johnson,Jyrki Heino,Jyrki Heino +10 more
TL;DR: All three collagen receptors appear to differ in their ability to recognize distinct collagen subtypes, and the relatively small structural differences on their collagen binding surfaces may explain the functional specifics.
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MMGBSA as a tool to understand the binding affinities of filamin-peptide interactions.
TL;DR: Computationally estimated the binding free energies of filamin A (FLNa) subunits with bound peptides using the molecular mechanics-generalized Born surface area (MMGBSA) method and demonstrated that molecular dynamics combined with free energy calculations are applicable to estimating the energetics of protein-protein interactions.
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α11β1 Integrin Recognizes the GFOGER Sequence in Interstitial Collagens
Wan-Ming Zhang,Jarmo Käpylä,J. Santeri Puranen,C. Graham Knight,Carl-Fredrik Tiger,Olli T. Pentikäinen,Mark S. Johnson,Richard W. Farndale,Jyrki Heino,Donald Gullberg +9 more
TL;DR: The data indicate that the GFOGER sequence in fibrillar collagens is a common recognition motif used by α1β1, α2 β1, and also α11β1 integrins, despite their distinct binding specificity for various collagen subtypes.
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Structure of three tandem filamin domains reveals auto-inhibition of ligand binding.
Yatish Lad,Tiila R. Kiema,Pengju Jiang,Olli T. Pentikäinen,C.H. Coles,Iain D. Campbell,David A. Calderwood,Jari Ylänne +7 more
TL;DR: Structural and functional analysis of other IgFLN domains suggests that auto‐inhibition by adjacent IgFLn domains may be a general mechanism controlling filamin–ligand interactions, which can explain the increased integrin binding of filamin splice variants and provides a mechanism by which ligand binding might impact filamin structure.