Chaperon ins

Hartl, F.U. Molecular chaperones in cellular protein folding. Nature 381 571-580, 1996. 

Chaperones. Table 1 Molecular Chaperones in Humans (note this list is not meant to be exhaustive). Synonyms are given in parentheses... 

A small compound that mimicks a molecular chaperone in activity. 

Kv 3 -subunits are auxiliary subunits of Shaker-related Kv-channels, which belong to the Kvl subfamily of voltage-gated potassium channels. Kv(3 -subunits may function as chaperones in Kva -subunit assembly and may modulate the gating properties of Kv-channels. In particular, some Kv(3 -subunits may confer a rapid inactivation to otherwise non-inactivating Kv-channels. 

Manning-Krieg, U.C., Scherer, P.E., Schatz, G. (1991), Sequential action of mitochondrial chaperon-ins in protein import into the matrix. EMBO J. 10,3273-3280. 

N-ethylmaleimide-sensitive Trimeric ATPase required for in vitro membrane fusion during vesicular transport. Probably function as factor (NSF) chaperones in synaptic vesicle recycling. 

Figure 1. Different histone chaperones in the key histone metabolic pathways Functions of histone chaperones range from the storage of newly synthesized histones in the cytoplasm, its transfer into the nucleus and in histone assembly into nucleosomes. Apart from diis die histone chaperones are also involved in histone exchange, maintenance of heterochromatin and in the regulation of chromatin structure during transcription. (See Colour Plate 10.)...

A new insight into the problem of insolnbUity of heterologous proteins has evolved from further information regarding the in vivo function of molecnlar chaperones in protein folding. As reviewed by Baneyx, co-expression of chaperones in the bacterial system can improve the folding and hence the yield of heterologous proteins [96]. 

To prevent incorrect folding of the growing protein during protein biosynthesis, chaperones (see B) in the lumen of the rER bind to the peptide chain and stabilize it until translation has been completed. Binding protein (BiP) is an important chaperone in the ER. 

Hard FU, Hlodan R, Langer T (1994) Molecular chaperones in protein folding the art of avoiding sticky situations. Trends Biochem Sci 19 20-25 Hausler T, Stierhof YD, Blattner J, Clayton C (1997) Conservation of mitochondrial targeting sequence function in mitochondrial and hydrogenosomal proteins from the early-branching eukaryotes Crithidia, Trypanosoma and Trichomonas. Eur J Cell Biol 73 240-251... 

Schlitzer, D. S. Novak, B. M. Trapped Kinetic States, Chiral Amplification and Molecular Chaperoning in Synthetic Polymers Chiral Induction in Polyguanidines through Ion Pair Interactions, J. Am. Chem. Soc. 1998, 120, 2196-2197. 

FIGURE 4-30 Chaperones in protein folding. The cyclic pathway by which chaperones bind and release polypeptides is illustrated for the . coli chaperone proteins DnaK and DnaJ, homologs of the eukaryotic chaperones Hsp70 and Hsp40. The chaperones do not actively promote the folding of the substrate protein, but instead prevent aggregation of unfolded peptides. For a population of polypeptides, some... 

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