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Ariel Lustig
Researcher at University of Basel
Publications - 99
Citations - 7152
Ariel Lustig is an academic researcher from University of Basel. The author has contributed to research in topics: Peptide sequence & Protein structure. The author has an hindex of 50, co-authored 99 publications receiving 6833 citations. Previous affiliations of Ariel Lustig include Max Planck Society & University of Crete.
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Three-Dimensional Structure of Human Monoamine Oxidase a (Mao A): Relation to the Structures of Rat Mao a and Human Mao B
TL;DR: Data support the proposal that hMAO A involves a change from the dimeric to the monomeric form through a Glu-151 --> Lys mutation that is specific of hMAo A and put into question the use of MAO A from nonhuman sources in drug development for use in humans.
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Structure and Assembly Properties of the Intermediate Filament Protein Vimentin: The Role of its Head, Rod and Tail Domains
Harald Herrmann,Markus Häner,Monika Brettel,Shirley A. Müller,Kenneth N. Goldie,Bettina Fedtke,Ariel Lustig,Werner W. Franke,Ueli Aebi +8 more
TL;DR: The functional role of the non-helical end domains of vimentin on its assembly properties using truncated Xenopus and human recombinant proteins suggests that assembly occurred by a principally similar mechanism involving the end-on-fusion or annealing of unit-length filaments.
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The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase
TL;DR: A stable, misfolded luciferase species that can be efficiently renatured by substoichiometric amounts of bacterial Hsp70-Hsp40-NEF is described and apparent V(max)' and K(m)' values for a chaperone-mediated renaturation reaction for the first time are determined.
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Stabilization of short collagen-like triple helices by protein engineering.
Sabine Frank,Richard A. Kammerer,Diane E. Mechling,Therese Schulthess,Ruth Landwehr,James G. Bann,James G. Bann,Yuan Guo,Ariel Lustig,Hans Peter Bächinger,Jürgen Engel +10 more
TL;DR: A method to stabilize collagen-like peptides by fusing them to the N terminus of the bacteriophage T4 fibritin foldon domain is reported, and it is shown that the foldondomain, which comprises only 27 amino acid residues, forms an obligatory trimer with a high degree of thermal stability.
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Structure and interactions of heparan sulfate proteoglycans from a mouse tumor basement membrane.
TL;DR: Various forms of heparan sulfate proteoglycan were solubilized from the mouse Engelbreth-Holm-Swarm (EHS) sarcoma by extraction with 0.5 M NaCl, collagenase digestion and extraction with 4 M guanidine and demonstrated preferential incorporation of radioactive sulfate in the high-density form.