Results 61 to 70 of about 27,623 (198)
Journal of Biological Chemistry, 1992 An IgG1 monoclonal antibody (mAb 54G8) which binds to both Bordetella pertussis chaperonin-60 (cpn60) and Escherichia coli cpn60 (GroEL) was produced. mAb 54G8 as well as Fab fragments prepared from this antibody were found to abolish the ability of chaperonin-10 (cpn10, GroES) to inhibit the ATPase activity of both B. pertussis cpn60 and E. coli cpn60.
D L, Burns +4 more
openaire +2 more sources
A yeast two-hybrid screen reveals a strong interaction between the Legionella chaperonin Hsp60 and the host cell small heat shock protein Hsp10 [PDF]
, 2015 L. pneumophila is an intracellular bacterium that replicates inside a membrane-bound vacuole called Legionella-containing vacuole (LCV), where it plentifully liberates its HtpB chaperonin.
Nasrallah, Gheyath K.
core +1 more source
Formation and Function of the Rbl2p-beta-Tubulin Complex [PDF]
, 1998 The yeast protein Rbl2p suppresses the deleterious effects of excess beta-tubulin as efficiently as does alpha-tubulin. Both in vivo and in vitro, Rbl2p forms a complex with beta-tubulin that does not contain alpha-tubulin, thus defining a second pool of
Archer, Julie E. +3 more
core
Purification and characterization of chaperonins 60 and 10 from Methylobacillus glycogenes
Cell Stress & Chaperones, 1998 Two proteins belonging to the group I chaperonin family were isolated from an obligate methanotroph, Methylobacillus glycogenes. The two proteins, one a GroEL homologue (cpn60: M. glycogenes 60 kDa chaperonin) and the other a GroES homologue (cpn10: M. glycogenes 10 kDa chaperonin), composed a heteropolymeric complex in the presence of ATP.
Y, Kawata +4 more
openaire +3 more sources
BMC Cancer, 2018 Background Heat Shock Proteins (HSPs), a family of genes with key roles in proteostasis, have been extensively associated with cancer behaviour. However, the HSP family is quite large and many of its members have not been investigated in breast cancer ...
Felipe C. M. Zoppino +3 more
doaj +1 more source
Expression in Escherichia coli, purification and functional activity of recombinant human chaperonin 10 [PDF]
FEBS Letters, 1995 We have recently reported the cloning of a cDNA coding for a stress inducible human chaperonin 10. The protein was shown to possess 100% identity with the bovine homologue and a single amino acid replacement (glycine to serine at position 52) compared to rat chaperonin 10. Here we report the heterologous expression of human chaperonin 10 in Escherichia
Legname, Giuseppe +5 more
openaire +2 more sources
Directed transport as a mechanism for protein folding in vivo
, 2009 We propose a model for protein folding in vivo based on a Brownian-ratchet mechanism in the multidimensional energy landscape space. The device is able to produce directed transport taking advantage of the assumed intrinsic asymmetric properties of the ...
Alberts B. +9 more
core +1 more source
PhytoFrontiersBacillus mojavensis KRS009 was identified as an antagonistic strain with a strong inhibitory effect on various phytopathogenic fungi. To provide further insight into its biocontrol mechanisms and ability to improve plant salt tolerance, the high quality ...
Fu-Hua Zhao +9 more
doaj +1 more source
Proteomics Profiling of Chikungunya-Infected Aedes albopictus C6/36 Cells Reveal Important Mosquito Cell Factors in Virus Replication [PDF]
, 2015 10.1371/journal.pntd.0003544PLoS Neglected Tropical ...
Chu, Jang Hann, Lee, Regina Ching Hua
core +3 more sources
Systematic interaction network filtering identifies CRMP1 as a novel suppressor of huntingtin misfolding and neurotoxicity [PDF]
, 2015 Assemblies of huntingtin (HTT) fragments with expanded polyglutamine (polyQ) tracts are a pathological hallmark of Huntington's disease (HD). The molecular mechanisms by which these structures are formed and cause neuronal dysfunction and toxicity are ...
Andrade-Navarro, Miguel A. +24 more
core +2 more sources