C
Celestine N. Chi
Researcher at Uppsala University
Publications - 52
Citations - 1516
Celestine N. Chi is an academic researcher from Uppsala University. The author has contributed to research in topics: PDZ domain & Protein domain. The author has an hindex of 21, co-authored 47 publications receiving 1278 citations. Previous affiliations of Celestine N. Chi include École Polytechnique Fédérale de Lausanne & ETH Zurich.
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Journal ArticleDOI
A high-affinity, dimeric inhibitor of PSD-95 bivalently interacts with PDZ1-2 and protects against ischemic brain damage
Anders Bach,Bettina Hjelm Clausen,Magda Møller,Bente Vestergaard,Celestine N. Chi,Adam Round,Pernille L. Sørensen,Klaus B. Nissen,Jette S. Kastrup,Michael Gajhede,Per Jemth,Anders S. Kristensen,Patrik Lundström,Kate Lykke Lambertsen,Kristian Strømgaard +14 more
TL;DR: A novel dimeric inhibitor, Tat-NPEG4(IETDV)2 (Tat-N-dimer), which binds the tandem PDZ1-2 domain of PSD-95 with an unprecedented high affinity, and displays extensive protease-resistance as evaluated in vitro by stability-measurements in human blood plasma.
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Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I
Stefan Bibow,Yevhen Polyhach,Cédric Eichmann,Celestine N. Chi,Julia Kowal,Stefan Albiez,Robert A. McLeod,Henning Stahlberg,Gunnar Jeschke,Peter Güntert,Peter Güntert,Roland Riek +11 more
TL;DR: The three-dimensional structure of reconstituted discoidal HDL (rdHDL) particles is presented, using a shortened construct of human apolipoprotein A-I, determined from a combination of nuclear magnetic resonance (NMR), electron paramagnetic resonance (EPR) and transmission electron microscopy (TEM) data.
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Reassessing a sparse energetic network within a single protein domain
TL;DR: This study reassessed the energetic coupling of these residues by double mutant cycles together with ligand binding and stability experiments and found that coupling is not a special property of the coevolved network of residues in PDZ domains.
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Ligand binding by PDZ domains
TL;DR: This review focuses on the molecular details of how PDZ domains bind their protein ligands and their potential as drug targets in this context.
Journal ArticleDOI
Comparison of successive transition states for folding reveals alternative early folding pathways of two homologous proteins
Nicoletta Calosci,Celestine N. Chi,Barbara Richter,Carlo Camilloni,Åke Engström,Lars Eklund,Carlo Travaglini-Allocatelli,Stefano Gianni,Michele Vendruscolo,Per Jemth +9 more
TL;DR: In this paper, the authors investigated the folding mechanisms of two homologous three-state proteins, PTP-BL PDZ2 and PSD-95 PDZ3, and compared the early and late transition states on their folding pathways.