Aggregation of hsp70 and hsc70 in vivo is distinct and temperature- dependent and their chaperone function is directly related to non-aggregated forms

European Journal of Biochemistry

Volumn 259, Issue 1-2, 1999, Pages 505-512

  Angelidis, Charalampos E ^b   Lazaridis, Ioannis ^b   Pagoulatos, Gerassimos N ^a  

^a UNIVERSITY OF IOANNINA   (Greece)

^b NONE

Author keywords

Aggregation; Chaperone function; Hsc70; Hsp70; Oligomerization

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONE; HEAT SHOCK PROTEIN 70;

ANIMAL CELL; ARTICLE; HEAT SHOCK; KIDNEY CELL; MONKEY; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN STRUCTURE; TEMPERATURE DEPENDENCE;

ADENOSINE TRIPHOSPHATE; CARRIER PROTEINS; HEAT; HEAT-SHOCK PROTEINS; HSC70 HEAT-SHOCK PROTEINS; HSP40 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; LUCIFERASES; PARTICLE SIZE; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING;

ANIMALIA;

EID: 0010389517     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00078.x     Document Type: Article

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