Globular domain of the prion protein needs to be unlocked by domain swapping to support prion protein conversion

Journal of Biological Chemistry

Volumn 286, Issue 14, 2011, Pages 12149-12156

  Hafner Bratkovič, Iva ^a   Bester, Romina ^b   Pristovšek, Primož ^a   Gaedtke, Lars ^b   Veranič, Peter ^c   Gašperšič, Jernej ^a   Manček Keber, Mateja ^a   Avbelj, Matevž ^a   Polymenidou, Magdalini ^d,f   Julius, Christian ^d   Aguzzi, Adriano ^d   Vorberg, Ina ^b,g   Jerala, Roman ^a,c,e  

^a NATIONAL INSTITUTE OF CHEMISTRY   (Slovenia)

^b TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^c UNIVERSITY OF LJUBLJANA   (Slovenia)

^d UNIVERSITY HOSPITAL ZURICH   (Switzerland)

^e EN FIST CENTRE OF EXCELLENCE   (Slovenia)

^f UNIVERSITY OF CALIFORNIA   (United States)

^g GERMAN CENTER FOR NEURODEGENERATIVE DISEASES DZNE   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID FORMATION; BUILDING BLOCKES; CONVERSION PROCESS; DISULFIDE BRIDGE; DOMAIN SWAPPING; GLOBULAR DOMAINS; HIGH-RESOLUTION STRUCTURES; HIGH-RESOLUTION TECHNIQUES; IN-VITRO; INFECTED CELLS; MAMMALIAN SPECIES; MODEL-BASED; PRION DISEASE; PRION PROTEIN; PROTEINASE K; RATE-LIMITING STEPS; SECONDARY STRUCTURE ELEMENTS; SHEET STRUCTURE; STRUCTURAL ELEMENTS; STRUCTURAL MODELS; SUB-DOMAINS; SUBDOMAIN; THERAPEUTIC INTERVENTION;

AMINO ACIDS; CELL CULTURE; COVALENT BONDS; MAMMALS; MODEL STRUCTURES; PROTEINS; SCANDIUM;

NEURODEGENERATIVE DISEASES;

AMYLOID; CYSTEINE; PRION PROTEIN; PROTEINASE K;

ARTICLE; CELL CULTURE; DIMERIZATION; DISULFIDE BOND; DOMAIN SWAPPING; GLOBULAR DOMAIN; IN VITRO STUDY; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; PROTEIN TARGETING; THERMODYNAMICS;

ANIMALS; CELL LINE; CIRCULAR DICHROISM; DISULFIDES; ENZYME-LINKED IMMUNOSORBENT ASSAY; FLOW CYTOMETRY; MICE; MICROSCOPY, ATOMIC FORCE; MICROSCOPY, ELECTRON, TRANSMISSION; MUTATION; PRIONS;

MAMMALIA;

EID: 79953321018     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.213926     Document Type: Article

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