Chaperones: Difference between revisions

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== Function ==
== Function ==
Chaperones bind to the newly synthesized and unfolded proteins helping them acquire their properly folded 3D structure <ref>PMID: 3112578</ref>. Besides, chaperones help in targeting the native proteins to their respective organelles <ref>PMID:3282178</ref><ref>DOI: 10.1002/iub.1272</ref>. The first identified chaperones were the histone chaperones that are continously involved in histone metabolism thus regulating genome function, stability and identity<ref>doi: 10.1146/annurev-biochem-060713-035536</ref>. Many protozoan parasites such as ''Plasmodium falciparum'' requires these proteins for cytoprotection <ref>PMID: 14711509</ref> <ref>PMID: 19339102</ref>. Chaperones actively participate in the maintenance of proteome integrity and protein homeostasis (proteostasis) which requires a syncrhonization in various chaperone's tuning the process <ref>DOI: 10.1146/annurev-biochem-060208-092442</ref>.
Chaperones bind to the newly synthesized and unfolded proteins helping them acquire their properly folded 3D structure <ref>PMID: 3112578</ref>. Besides, chaperones help in targeting the native proteins to their respective organelles <ref>PMID:3282178</ref><ref>DOI: 10.1002/iub.1272</ref>. The first identified chaperones were the histone chaperones that are continously involved in histone metabolism thus regulating genome function, stability and identity<ref>doi: 10.1146/annurev-biochem-060713-035536</ref>. Many protozoan parasites such as ''Plasmodium falciparum'' requires these proteins for cytoprotection <ref>PMID: 14711509</ref> <ref>PMID: 19339102</ref>. Chaperones actively participate in the maintenance of proteome integrity and protein homeostasis (proteostasis) which requires a syncrhonization in various chaperone's tuning the process <ref>DOI: 10.1146/annurev-biochem-060208-092442</ref>.
== Disease ==
== Disease ==
Chaperones are instrumental in protein folding processes. Alteration in this process may lead to protein aggregation and formation of inclusion bodies. Protein misfolding may result in various diseases such as Alzheimer<ref>PMID: 16048838</ref>,Parkinson<ref>PMID: 16610362</ref>,Familial amyotrophic lateral sclerosis  <ref>doi:10.1002/prca.200780023</ref>, Huntington<ref>PMID:24323530</ref, Spinocerebellar ataxia 1, 2, 3<ref>doi:10.1016/B978-0-444-51892-7.00027-9</ref>, Spinobulbar muscular atrophy<ref>doi: 10.1093/hmg/11.5.515</ref> and ageing<ref>doi:10.1111/j.1742-4658.2006.05181.x</ref>.
Chaperones are instrumental in protein folding processes. Alteration in this process may lead to protein aggregation and formation of inclusion bodies. Protein misfolding may result in various diseases such as Alzheimer <ref>PMID:16048838</ref>, Parkinson <ref>PMID:16610362</ref>, Familial amyotrophic lateral sclerosis  <ref>doi:10.1002/prca.200780023</ref>, Huntington<ref>PMID:24323530</ref, Spinocerebellar ataxia 1, 2, 3 <ref>doi:10.1016/B978-0-444-51892-7.00027-9</ref>, Spinobulbar muscular atrophy <ref>doi: 10.1093/hmg/11.5.515</ref> and ageing <ref>doi:10.1111/j.1742-4658.2006.05181.x</ref>.
              
              
== Relevance ==
== Relevance ==

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Gauri Misra, Michal Harel, Alexander Berchansky