Chemistry Reference
In-Depth Information
Hu Y, Henderson B, Lund PA, Tormay P, Ahmed MT, Gurcha SS, Besra GS, Coates AR (2008) A
Mycobacterium tuberculosis mutant lacking the groEL homologue cpn60.1 is viable but fails to
induce an inflammatory response in animal models of infection. Infect Immun 76:1535-1546
Hunt JF, Weaver AJ, Landry SJ, Gierasch L, Deisenhofer J (1996) The crystal structure of the
GroES co-chaperonin at 2.8 A resolution. Nature 379:37-45
Hunt JF, Earnest TN, Bousche O, Kalghatgi K, Reilly K, Horvath C, Rothschild KJ, Engelman DM
(1997) A biophysical study of integral membrane protein folding. Biochemistry 36:15156-
15176
Janouskovec J, Horak A, Obornik M, Lukes J, Keeling PJ (2010) A common red algal origin of the
apicomplexan, dinoflagellate, and heterokont plastids. Proc Natl Acad Sci U S A 107:10949-
10954
Jewett AI, Shea JE (2010) Reconciling theories of chaperonin accelerated folding with experimen-
tal evidence. Cell Mol Life Sci 67:255-276
Jia H, Halilou AI, Hu L, Cai W, Liu J, Huang B (2011) Heat shock protein 10 (Hsp10) in immune-
related diseases: one coin, two sides. Int J Biochem Mol Biol 2:47-57
Johnson BJ, Le TT, Dobbin CA, Banovic T, Howard CB, Flores Fde M, Vanags D, Naylor DJ, Hill
GR, Suhrbier A (2005) Heat shock protein 10 inhibits lipopolysaccharide-induced inflamma-
tory mediator production. J Biol Chem 280:4037-4047
Kampinga HH, Hageman J, Vos MJ, Kubota H, Tanguay RM, Bruford EA, Cheetham ME, Chen
B, Hightower LE (2009) Guidelines for the nomenclature of the human heat shock proteins.
Cell Stress Chaperones 14:105-111
Kaufman BA, Kolesar JE, Perlman PS, Butow RA (2003) A function for the mitochondrial chap-
eronin Hsp60 in the structure and transmission of mitochondrial DNA nucleoids in Saccharo-
myces cerevisiae. J Cell Biol 163:457-461
Kaufmann SH (1992) The cellular immune response to heat shock proteins. Experientia
48:640-643
Kawata Y, Kawagoe M, Hongo K, Miyazaki T, Higurashi T, Mizobata T, Nagai J (1999) Functional
communications between the apical and equatorial domains of GroEL through the intermediate
domain. Biochemistry 38:15731-15740
Keppel F, Rychner M, Georgopoulos C (2002) Bacteriophage-encoded cochaperonins can substi-
tute for
Escherichia coli's
essential GroES protein. EMBO Rep 3:893-898
Kerner MJ, Naylor DJ, Ishihama Y, Maier T, Chang HC, Stines AP, Georgopoulos C, Frishman D,
Hayer-Hartl M, Mann M, Hartl FU (2005) Proteome-wide analysis of chaperonin-dependent
protein folding in
Escherichia coli
. Cell 122:209-220
Knowlton AA, Gupta S (2003) HSP60, Bax, and cardiac apoptosis. Cardiovasc Toxicol 3:263-268
Kong TH, Coates AR, Butcher PD, Hickman CJ, Shinnick TM (1993) Mycobacterium tuberculo-
sis expresses two chaperonin-60 homologs. Proc Natl Acad Sci U S A 90:2608-2612
Koumoto Y, Shimada T, Kondo M, Hara-Nishimura I, Nishimura M (2001) Chloroplasts have
a novel Cpn10 in addition to Cpn20 as co-chaperonins in Arabidopsis thaliana. J Biol Chem
276:29688-29694
Kubota H, Hynes G, Carne A, Ashworth A, Willison K (1994) Identification of six Tcp-1-related
genes encoding divergent subunits of the TCP-1-containing chaperonin. Curr Biol 4:89-99
Kurochkina LP, Semenyuk PI, Orlov VN, Robben J, Sykilinda NN, Mesyanzhinov VV (2012)
Expression and functional characterization of the first bacteriophage-encoded chaperonin. J
Virol 86:10103-10111
Landry SJ, Zeilstra-Ryalls J, Fayet O, Georgopoulos C, Gierasch LM (1993) Characterization of a
functionally important mobile domain of GroES. Nature 364:255-258
Landry SJ, Taher A, Georgopoulos C, van der Vies SM (1996) Interplay of structure and disorder
in cochaperonin mobile loops. Proc Natl Acad Sci U S A 93:11622-11627
Lenz G, Ron EZ (2014) Novel interaction between the major bacterial heat shock chaperone
(GroESL) and an RNA chaperone (CspC). J Mol Biol 426:460-466
Leroux MR (2001) Protein folding and molecular chaperones in archaea. Adv Appl Microbiol
50:219-277
Search WWH ::
Custom Search