M
Mats Carlquist
Researcher at Novum
Publications - 20
Citations - 5346
Mats Carlquist is an academic researcher from Novum. The author has contributed to research in topics: Ligand (biochemistry) & Estrogen receptor. The author has an hindex of 13, co-authored 20 publications receiving 5178 citations.
Papers
More filters
Journal ArticleDOI
Molecular basis of agonism and antagonism in the oestrogen receptor.
Andrzej M. Brzozowski,Ashley C. W. Pike,Zbigniew Dauter,Roderick E. Hubbard,Tomas Bonn,Owe Engström,Lars Öhman,Geoffrey L. Greene,Jan-Åke Gustafsson,Mats Carlquist +9 more
TL;DR: The crystal structures of the LBD of ER in complex with the endogenous oestrogen, 17β-oestradiol, and the selective antagonist raloxifene provide a molecular basis for the distinctive pharmacophore of the ER and its catholic binding properties.
Journal ArticleDOI
Structure of the Ligand-Binding Domain of Oestrogen Receptor Beta in the Presence of a Partial Agonist and a Full Antagonist
Ashley C. W. Pike,Andrzej M. Brzozowski,Roderick E. Hubbard,Tomas Bonn,Ann Gerd Thorsell,Owe Engström,Jan Ljunggren,Jan-Åke Gustafsson,Mats Carlquist +8 more
TL;DR: The three‐dimensional structure of the oestrogen receptor beta isoform (ERβ) ligand‐binding domain (LBD) in the presence of the phyto‐oestrogen genistein and the antagonist raloxifene is reported.
Journal ArticleDOI
Structural insights into the mode of action of a pure antiestrogen.
Ashley C. W. Pike,A. Marek Brzozowski,Julia Walton,Roderick E. Hubbard,Ann Gerd Thorsell,Yi Lin Li,Jan-Åke Gustafsson,Mats Carlquist +7 more
TL;DR: The novel observation that binding of ICI results in the complete destabilization of H12 provides some indications as to a possible mechanism for pure receptor antagonism.
Journal ArticleDOI
The Three-dimensional Structures of Antagonistic and Agonistic Forms of the Glucocorticoid Receptor Ligand-binding Domain RU-486 INDUCES A TRANSCONFORMATION THAT LEADS TO ACTIVE ANTAGONISM
Björn Kauppi,Clarissa G. Jakob,Mathias Färnegårdh,Jie Yang,Harri Ahola,Maria Alarcon,Karin Calles,Owe Engström,John M. Harlan,Steven W. Muchmore,Anna Karin Ramqvist,Susanne Thorell,Lars Öhman,Jonathan Greer,Jan-Åke Gustafsson,Jan Carlstedt-Duke,Mats Carlquist +16 more
TL;DR: All three RU-486 GR-LBD structures show that GR has a very flexible region between the end of helix 11 and the endof helix 12, and the subunits of the GR3 dimers are covalently connected via a disulfide bond between the Cys-736 residues in the two molecules.
Journal ArticleDOI
The Three-dimensional Structure of the Liver X Receptor β Reveals a Flexible Ligand-binding Pocket That Can Accommodate Fundamentally Different Ligands
Mathias Färnegårdh,Tomas Bonn,Sherry Sun,Jan Ljunggren,Harri Ahola,Anna Wilhelmsson,Jan-Åke Gustafsson,Mats Carlquist +7 more
TL;DR: The structures of the liver X receptor LXRβ (NR1H2) have been determined in complexes with two synthetic ligands, T0901317 and GW3965, to 2.1 and 2.4 Å, respectively, revealing a flexible ligand-binding pocket that can adjust to accommodate fundamentally different ligands.