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Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor proteinX-ray Structures of Human Furin in Complex with Competitive InhibitorsCrystal structure of the antimicrobial peptidase lysostaphin fromStaphylococcus simulansThe amyloid precursor protein shows a pH-dependent conformational switch in its E1 domainAnalysis of the overall structure of the multi-domain amyloid precursor protein (APP).The structure of a furin-antibody complex explains non-competitive inhibition by steric exclusion of substrate conformers.Structure of the unliganded form of the proprotein convertase furin suggests activation by a substrate-induced mechanism.Structural Studies Revealed Active Site Distortions of Human Furin by a Small Molecule Inhibitor.Localization and orientation of heavy-atom cluster compounds in protein crystals using molecular replacement.X-ray structures of the proprotein convertase furin bound with substrate analog inhibitors reveal substrate specificity determinants beyond the S4 pocket.Optimization of Substrate-Analogue Furin Inhibitors.Engineering a Constrained Peptidic Scaffold towards Potent and Selective Furin Inhibitors.Heparin induced dimerization of APP is primarily mediated by E1 and regulated by its acidic domainStructural and functional analysis of cystatin E reveals enzymologically relevant dimer and amyloid fibril statesSirtilins - the new old members of the vitamin K-dependent coagulation factor familyDesign, Synthesis, and Characterization of Macrocyclic Inhibitors of the Proprotein Convertase Furin
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description
investigador
@es
researcher
@en
wetenschapper
@nl
name
Sven O Dahms
@en
Sven O Dahms
@nl
type
label
Sven O Dahms
@en
Sven O Dahms
@nl
prefLabel
Sven O Dahms
@en
Sven O Dahms
@nl
P31
P496
0000-0002-0915-7579