Target type: biologicalprocess
Any process that activates or increases the frequency, rate or extent of protein refolding. [GO_REF:0000058, GOC:TermGenie, PMID:11360998]
Positive regulation of protein refolding is a crucial cellular process that ensures the proper folding and function of proteins. Misfolded proteins can accumulate and lead to various cellular dysfunctions and diseases. Therefore, cells have evolved sophisticated mechanisms to prevent and correct protein misfolding.
**1. Molecular Chaperones:**
* Molecular chaperones are proteins that bind to unfolded or misfolded proteins, preventing aggregation and promoting their proper folding.
* They act as catalysts, facilitating the folding process without becoming part of the final protein structure.
* Key chaperone families include Hsp70, Hsp90, and chaperonins (e.g., GroEL/ES).
* Hsp70 binds to unfolded or misfolded proteins, preventing their aggregation and assisting in their refolding.
* Hsp90 is involved in stabilizing and refolding proteins, particularly those involved in signaling pathways.
* Chaperonins form barrel-shaped structures that encapsulate unfolded proteins, providing a protected environment for refolding.
**2. Protein Disulfide Isomerases (PDIs):**
* PDIs are enzymes that catalyze the formation, breakage, and isomerization of disulfide bonds, which are crucial for stabilizing protein structures.
* They help to ensure the correct formation of disulfide bridges within proteins, preventing misfolding and promoting proper function.
**3. Proteasomal Degradation:**
* The proteasome is a multi-protein complex that degrades misfolded and damaged proteins.
* This process is essential for maintaining protein quality control and removing potentially harmful proteins from the cell.
* The proteasome recognizes and degrades proteins that have been tagged with ubiquitin, a small protein that acts as a degradation signal.
**4. Cellular Stress Response:**
* When cells experience stress, such as heat shock, they activate a cellular stress response known as the unfolded protein response (UPR).
* The UPR involves the upregulation of chaperone proteins, increased protein folding capacity, and enhanced degradation of misfolded proteins.
* This response helps the cell cope with stress and maintain protein homeostasis.
**5. Other Factors:**
* The cellular environment, including pH, temperature, and the presence of co-factors, can also influence protein folding and refolding.
* Post-translational modifications, such as phosphorylation and glycosylation, can also contribute to protein folding and stability.
In summary, positive regulation of protein refolding is a complex and essential process involving multiple cellular mechanisms. These mechanisms work together to ensure that proteins fold correctly and maintain their functional integrity, preventing the accumulation of misfolded proteins and protecting cellular function.'
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| Protein | Definition | Taxonomy |
|---|---|---|
| Heat shock cognate 71 kDa protein | A heat shock cognate 71 kDa protein that is encoded in the genome of human. [PRO:DAN] | Homo sapiens (human) |
| Compound | Definition | Classes | Roles |
|---|---|---|---|
| adenosine diphosphate | Adenosine Diphosphate: Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position. | adenosine 5'-phosphate; purine ribonucleoside 5'-diphosphate | fundamental metabolite; human metabolite |
| tubercidin | tubercidin : An N-glycosylpyrrolopyrimidine that is adenosine in which the in the 5-membered ring that is not attached to the ribose moiety is replaced by a carbon. Tubercidin is produced in the culture broth of Streptomyces tubericidus. Tubercidin: An antibiotic purine ribonucleoside that readily substitutes for adenosine in the biological system, but its incorporation into DNA and RNA has an inhibitory effect on the metabolism of these nucleic acids. | antibiotic antifungal agent; N-glycosylpyrrolopyrimidine; ribonucleoside | antimetabolite; antineoplastic agent; bacterial metabolite |
| toyocamycin | toyocamycin : An N-glycosylpyrrolopyrimidine that is tubercidin in which the hydrogen at position 5 of the pyrrolopyrimidine moiety has been replaced by a cyano group. Toyocamycin: 4-Amino-5-cyano-7-(D-ribofuranosyl)-7H- pyrrolo(2,3-d)pyrimidine. Antibiotic antimetabolite isolated from Streptomyces toyocaensis cultures. It is an analog of adenosine, blocks RNA synthesis and ribosome function, and is used mainly as a tool in biochemistry. | antibiotic antifungal agent; N-glycosylpyrrolopyrimidine; nitrile; ribonucleoside | antimetabolite; antineoplastic agent; apoptosis inducer; bacterial metabolite |
| nsc 65346 | sangivamycin : A nucleoside analogue that is adenosine in which the nitrogen at position 7 is replaced by a carbamoyl-substituted carbon. It is a potent inhibitor of protein kinase C. sangivamycin: RN given refers to parent cpd | nucleoside analogue | protein kinase inhibitor |
| adenosine | quinquefolan B: isolated from roots of Panax quinquefolium L.; RN not in Chemline 10/87; RN from Toxlit | adenosines; purines D-ribonucleoside | analgesic; anti-arrhythmia drug; fundamental metabolite; human metabolite; vasodilator agent |
| 8-aminoadenosine | |||
| 5'-deoxyadenosine | 5'-deoxyadenosine : A 5'-deoxyribonucleoside compound having adenosine as the nucleobase. 5'-deoxyadenosine: main heading DEOXYADENOSINE refers to the 3' cpd | 5'-deoxyribonucleoside; adenosines | Escherichia coli metabolite; human metabolite; mouse metabolite |
| ver 155008 | VER 155008: structure in first source | purine nucleoside | |
| nms-e973 | NMS-E973: structure in first source |