Mitochondrial import of the human chaperonin (HSP60) protein.

[1]  F. Hartl,et al.  Protein sorting to mitochondria: evolutionary conservations of folding and assembly. , 1990, Science.

[2]  G. Lorimer,et al.  Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP , 1989, Nature.

[3]  J. Rothman.  Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells , 1989, Cell.

[4]  H. Roy,et al.  Rubisco assembly: a model system for studying the mechanism of chaperonin action. , 1989, The Plant cell.

[5]  R. Gupta,et al.  A novel ubiquitous protein 'chaperonin' supports the endosymbiotic origin of mitochondrion and plant chloroplast. , 1989, Biochemical and biophysical research communications.

[6]  C. Mayanil,et al.  Molecular cloning of a Chinese hamster mitochondrial protein related to the "chaperonin" family of bacterial and plant proteins. , 1989, The Journal of biological chemistry.

[7]  C. Harley,et al.  Primary structure of a human mitochondrial protein homologous to the bacterial and plant chaperonins and to the 65-kilodalton mycobacterial antigen , 1989, Molecular and cellular biology.

[8]  A. Myers,et al.  Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor , 1989, Nature.

[9]  F. Hartl,et al.  Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria , 1989, Nature.

[10]  F. Lottspeich,et al.  Amino-acid sequence homology of a polymorphic cellular protein from human lymphocytes and the chaperonins from Escherichia coli (groEL) and chloroplasts (Rubisco-binding protein). , 1988, Biological chemistry Hoppe-Seyler.

[11]  Gordon C. Shore,et al.  Topogenesis of mitochondrial inner membrane uncoupling protein. Rerouting transmembrane segments to the soluble matrix compartment , 1988, The Journal of cell biology.

[12]  Roger W. Hendrix,et al.  Homologous plant and bacterial proteins chaperone oligomeric protein assembly , 1988, Nature.

[13]  J. Williams,et al.  The Mycobacterium tuberculosis 65-kilodalton antigen is a heat shock protein which corresponds to common antigen and to the Escherichia coli GroEL protein , 1988, Infection and immunity.

[14]  R. Gupta,et al.  Mitochondrial matrix localization of a protein altered in mutants resistant to the microtubule inhibitor podophyllotoxin. , 1987, European journal of cell biology.

[15]  W. Neupert,et al.  Mitochondrial protein import: involvement of the mature part of a cleavable precursor protein in the binding to receptor sites. , 1987, The EMBO journal.

[16]  G. Schatz.  17th Sir Hans Krebs lecture. Signals guiding proteins to their correct locations in mitochondria. , 1987, European journal of biochemistry.

[17]  G. Gerber,et al.  Complete nucleotide and derived amino acid sequence of cDNA encoding the mitochondrial uncoupling protein of rat brown adipose tissue: lack of a mitochondrial targeting presequence. , 1986, Nucleic acids research.

[18]  C. J. Lusty,et al.  Import and processing of hybrid proteins by mammalian mitochondria in vitro. , 1986, The Journal of biological chemistry.

[19]  S. Chien,et al.  Import of rat liver mitochondrial malate dehydrogenase. Synthesis, transport, and processing in vitro of its precursor. , 1984, The Journal of biological chemistry.

[20]  C. J. Lusty,et al.  Membrane and cytosolic components affecting transport of the precursor for ornithine carbamyltransferase into mitochondria. , 1983, The Journal of biological chemistry.