Chemistry Reference
In-Depth Information
Gray TE, Fersht AR (1991) Cooperativity in ATP hydrolysis by GroEL is increased by GroES.
FEBS Lett 292:254-258
Guidry JJ, Shewmaker F, Maskos K, Landry S, Wittung-Stafshede P (2003) Probing the interface
in a human co-chaperonin heptamer: residues disrupting oligomeric unfolded state identified.
BMC Biochem 4:14
Guisbert E, Herman C, Lu CZ, Gross CA (2004) A chaperone network controls the heat shock
response in
E. coli
. Genes Dev 18:2812-2821
Gupta P, Aggarwal N, Batra P, Mishra S, Chaudhuri TK (2006) Co-expression of chaperonin Gro-
EL/GroES enhances in vivo folding of yeast mitochondrial aconitase and alters the growth
characteristics of
Escherichia coli
. Int J Biochem Cell Biol 38:1975-1985
Hansen JJ, Bross P, Westergaard M, Nielsen MN, Eiberg H, Borglum AD, Mogensen J, Kristiansen
K, Bolund L, Gregersen N (2003) Genomic structure of the human mitochondrial chaperonin
genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirec-
tional promoter. Human Genet 112:71-77
Hansen J, Svenstrup K, Ang D, Nielsen MN, Christensen JH, Gregersen N, Nielsen JE, Georgo-
poulos C, Bross P (2007) A novel mutation in the HSPD1 gene in a patient with hereditary
spastic paraplegia. J Neurol 254:897-900
Hartl FU (1996) Molecular chaperones in cellular protein folding. Nature 381:571-579
Hartl FU, Hayer-Hartl M (2002) Molecular chaperones in the cytosol: from nascent chain to folded
protein. Science 295:1852-1858
Hartl FU, Hayer-Hartl M (2009) Converging concepts of protein folding in vitro and in vivo. Nat
Struct Mol Biol 16:574-581
Hartl FU, Martin J (1995) Molecular chaperones in cellular protein folding. Curr Opin Struct Biol
5:92-102
Hartl FU, Martin J, Neupert W (1992) Protein folding in the cell: the role of molecular chaperones
Hsp70 and Hsp60. Annu Rev Biophys Biomol Struct 21:293-322
Hartman DJ, Surin BP, Dixon NE, Hoogenraad NJ, Hoj PB (1993) Substoichiometric amounts
of the molecular chaperones GroEL and GroES prevent thermal denaturation and aggrega-
tion of mammalian mitochondrial malate dehydrogenase in vitro. Proc Natl Acad Sci U S A
90:2276-2280
Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT, Georgopoulos CP, Hendrix
RW, Ellis RJ (1988) Homologous plant and bacterial proteins chaperone oligomeric protein
assembly. Nature 333:330-334
Henderson B, Martin A (2011) Bacterial virulence in the moonlight: multitasking bacterial moon-
lighting proteins are virulence determinants in infectious disease. Infect Immun 79:3476-3491
Hertveldt K, Lavigne R, Pleteneva E, Sernova N, Kurochkina L, Korchevskii R, Robben J, Mesy-
anzhinov V, Krylov VN, Volckaert G (2005) Genome comparison of
Pseudomonas aeruginosa
large phages. J Mol Biol 354:536-545
Hill JE, Hemmingsen SM (2001) Arabidopsis thaliana type I and II chaperonins. Cell Stress Chap-
erones 6:190-200
Horovitz A, Willison KR (2005) Allosteric regulation of chaperonins. Curr Opin Struct Biol
15:646-651
Horovitz A, Fridmann Y, Kafri G, Yifrach O (2001) Review: allostery in chaperonins. J Struct Biol
135:104-114
Horwich AL, Saibil HR (1998) The thermosome: chaperonin with a built-in lid. Nat Struct Biol
5:333-336
Horwich AL, Low KB, Fenton WA, Hirshfield IN, Furtak K (1993) Folding in vivo of bacterial
cytoplasmic proteins: role of GroEL. Cell 74:909-917
Horwich AL, Fenton WA, Chapman E, Farr GW (2007) Two families of chaperonin: physiology
and mechanism. Annu Rev Cell Dev Biol 23:115-145
Houry WA, Frishman D, Eckerskorn C, Lottspeich F, Hartl FU (1999) Identification of in vivo
substrates of the chaperonin GroEL. Nature 402:147-154
Search WWH ::
Custom Search