• Thumbnail for Chaperone (protein)
    biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There...
    29 KB (3,499 words) - 07:16, 20 February 2024
  • Thumbnail for Binding immunoglobulin protein
    BiP is a HSP70 molecular chaperone located in the lumen of the endoplasmic reticulum (ER) that binds newly synthesized proteins as they are translocated...
    31 KB (3,521 words) - 04:06, 19 March 2024
  • Thumbnail for Protein folding
    temperature, the possible presence of cofactors and of molecular chaperones. Proteins will have limitations on their folding abilities by the restricted...
    75 KB (8,663 words) - 11:40, 10 May 2024
  • Thumbnail for Hsp90
    Hsp90 (redirect from Heat shock protein 90)
    shock protein 90) is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in protein degradation...
    51 KB (5,537 words) - 04:59, 26 April 2024
  • Middle Ages Chaperone (protein), a protein that assists non-covalent folding/unfolding Co-chaperone, a protein that assists a chaperone in protein folding...
    1 KB (185 words) - 23:31, 22 August 2021
  • Thumbnail for Hsp70
    Hsp70 (redirect from Heat-shock protein 70)
    Hsp70s are an important part of the cell's machinery for protein folding, performing chaperoning functions, and helping to protect cells from the adverse...
    49 KB (5,631 words) - 04:36, 26 April 2024
  • Thumbnail for Chaperone DnaJ
    In molecular biology, chaperone DnaJ, also known as Hsp40 (heat shock protein 40 kDa), is a molecular chaperone protein. It is expressed in a wide variety...
    7 KB (818 words) - 16:58, 9 March 2024
  • Thumbnail for Heat shock protein 47
    Heat shock protein 47, also known as SERPINH1 is a serpin which serves as a human chaperone protein for collagen. This protein is a member of the serpin...
    13 KB (1,577 words) - 20:40, 31 March 2024
  • Thumbnail for Protein tertiary structure
    translated. Protein chaperones within the cytoplasm of a cell assist a newly synthesised polypeptide to attain its native state. Some chaperone proteins are highly...
    15 KB (1,603 words) - 17:26, 23 April 2024
  • Within the ER, the protein is first covered by a chaperone protein to protect it from the high concentration of other proteins in the ER, giving it...
    52 KB (6,394 words) - 03:48, 19 March 2024
  • of this group perform chaperone functions by stabilizing new proteins to ensure correct folding or by helping to refold proteins that were damaged by the...
    49 KB (5,525 words) - 05:03, 26 April 2024
  • Thumbnail for HSP90B1
    HSP90B1 (category Molecular chaperones)
    Heat shock protein 90kDa beta member 1 (HSP90B1), known also as endoplasmin, gp96, grp94, or ERp99, is a chaperone protein that in humans is encoded by...
    12 KB (1,487 words) - 01:02, 4 March 2023
  • Thumbnail for HSPA8
    the heat shock protein 70 family and a chaperone protein, it facilitates the proper folding of newly translated and misfolded proteins, as well as stabilize...
    29 KB (3,533 words) - 15:28, 2 April 2024
  • Thumbnail for Hop (protein)
    for Hsp70-Hsp90 Organizing Protein. It functions as a co-chaperone which reversibly links together the protein chaperones Hsp70 and Hsp90. Hop belongs...
    16 KB (1,954 words) - 17:25, 1 April 2024
  • Thumbnail for LDL-receptor-related protein-associated protein
    density lipoprotein receptor-related protein-associated protein 1 also known as LRPAP1 or RAP is a chaperone protein which in humans is encoded by the LRPAP1...
    22 KB (2,608 words) - 18:02, 3 April 2024
  • maintaining proteostasis include regulated protein translation, chaperone assisted protein folding, and protein degradation pathways. Adjusting each of these...
    25 KB (2,922 words) - 16:16, 10 January 2024
  • Thumbnail for Sigma-1 receptor
    sigma-1 receptor (σ1R), one of two sigma receptor subtypes, is a chaperone protein at the endoplasmic reticulum (ER) that modulates calcium signaling...
    27 KB (3,004 words) - 22:36, 18 May 2024
  • Chemical chaperones are a class of small molecules that function to enhance the folding and/or stability of proteins. Chemical chaperones are a broad and...
    11 KB (1,382 words) - 20:45, 8 January 2024
  • Thumbnail for CLIP (protein)
    HLA-DO functions as the accessory protein. Both HLA-DM and HLA-DO interact with each other to act as chaperone proteins and prevent the denaturing of MHC...
    5 KB (468 words) - 19:21, 26 April 2024
  • Thumbnail for Osteogenesis imperfecta
    of chaperone protein HP47 to unbind from collagen type I, as to do so it needs to bind to the missing ER lumen protein retaining receptor 2 protein encoded...
    150 KB (15,363 words) - 22:39, 18 April 2024
  • Thumbnail for Clusterin
    Clusterin (redirect from CLU (protein))
    gene on chromosome 8. CLU is an extracellular molecular chaperone which binds to misfolded proteins in body fluids to neutralise their toxicity and mediate...
    22 KB (2,433 words) - 05:09, 24 January 2024
  • Thumbnail for Peripheral myelin protein 22
    PMP22 protein is glycosylated with an N terminus-linked sugar and co-localized with the chaperone protein calnexin in the ER. After the protein is transported...
    12 KB (1,472 words) - 15:34, 9 December 2023
  • Co-chaperones are proteins that assist chaperones in protein folding and other functions. Co-chaperones are the non-client binding molecules that assist...
    6 KB (777 words) - 06:55, 13 May 2024
  • Thumbnail for Hsp27
    Hsp27 (redirect from Heat shock protein 27)
    shock protein 27 (Hsp27) also known as heat shock protein beta-1 (HSPB1) is a protein that in humans is encoded by the HSPB1 gene. Hsp27 is a chaperone of...
    27 KB (3,341 words) - 18:34, 4 January 2024
  • Thumbnail for Heat shock response
    response that increases the number of molecular chaperones to combat the negative effects on proteins caused by stressors such as increased temperatures...
    21 KB (2,435 words) - 22:09, 30 December 2023
  • Thumbnail for Capsid
    Capsid (redirect from Core protein)
    structure. The bacteriophage encoded gp31 protein appears to be functionally homologous to E. coli chaperone protein GroES and able to substitute for it in...
    22 KB (2,554 words) - 01:23, 21 April 2024
  • bacterial chromosome. The translocase itself comprises 7 proteins, including a chaperone protein (SecB), an ATPase (SecA), an integral membrane complex...
    6 KB (634 words) - 17:25, 3 August 2023
  • pathways that lead to increasing the production of molecular chaperones involved in protein folding. If these objectives are not achieved within a certain...
    31 KB (3,579 words) - 01:21, 10 February 2024
  • A pharmacological chaperone or pharmacoperone is a drug that acts as a protein chaperone. That is, it contains small molecules that enter cells and serve...
    3 KB (338 words) - 16:01, 13 September 2021
  • Thumbnail for SecY protein
    peptide into the periplasm (SecD and SecF). The chaperone protein SecB is a highly acidic homotetrameric protein that exists as a "dimer of dimers" in the bacterial...
    5 KB (595 words) - 09:39, 19 September 2023