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Proteins|July 4, 2012
Peptide binding to the PDZ3 domain by conformational selectionSandra Steiner, Amedeo CaflischJournal of the American Chemical Society|February 12, 2015
Evolutionary conserved Tyr169 stabilizes the β2-α2 loop of the prion proteinDanzhi Huang, Amedeo CaflischScience (New York, N.Y.)|November 23, 2023
Mechanical properties pattern the skinSamhita P Banavar, Celeste M NelsonDer Hautarzt; Zeitschrift Fur Dermatologie, Venerologie, Und Verwandte Gebiete|February 1, 1981
[Multiple idiopathic hemorrhagic sarcoma (Kaposi's disease)]C Zortea-Caflisch, R PanizzonBiochimica Et Biophysica Acta. Proteins and Proteomics|August 5, 2022
Antibody binding increases the flexibility of the prion proteinIoana M Ilie, Amedeo CaflischChemical Reviews|April 12, 2019
Simulation Studies of Amyloidogenic Polypeptides and Their AggregatesIoana M Ilie, Amedeo CaflischJournal of Clinical Microbiology|May 17, 2019
Implications of Bacteriophage- and Bacteriophage Component-Based Therapies for the Clinical Microbiology LaboratoryKatherine M Caflisch, Robin PatelStructure (London, England : 1993)|October 12, 2005
Functional plasticity in the substrate binding site of beta-secretaseAlemayehu A Gorfe, Amedeo CaflischProteins|April 5, 2007
Computational analysis of the S. cerevisiae proteome reveals the function and cellular localization of the least and most amyloidogenic proteinsGian Gaetano Tartaglia, Amedeo CaflischFASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology|May 25, 2007
Ser170 controls the conformational multiplicity of the loop 166-175 in prion proteins: implication for conversion and species barrierAlemayehu A Gorfe, Amedeo CaflischPageof 6,903