COBRE: U KS: P1: ID OF HSP90 COCHAPERONES, IMMUNOPHILINS & PROTEINS

COBRE：UK KS：P1：HSP90 辅助伴侣、免疫亲和素的 ID

• 批准号: 7720669
• 负责人: Brian S J Blagg
• 金额: $ 2.61万
• 依托单位: UNIVERSITY OF KANSAS LAWRENCE
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-05-15 至 2009-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7720669
• 关键词: Centers of Research Excellence; Client; Computer Retrieval of Information on Scientific Projects Database; Enzymes; FK506 binding protein 5; Funding; GRP94; Grant; Heat-Shock Proteins 90; Immunophilins; Individual; Institution; Molecular Chaperones; Names; Nitric Oxide Synthase; Peptides; Peptidylprolyl Isomerase; Proteins; Research; Research Personnel; Resources; Role; Source; TP53 gene; Telomerase; United States National Institutes of Health; cancer therapy; genetic regulatory protein; mutant; protein folding; raf Kinases; receptor; src-Family Kinases; steroid hormone receptor; tacrolimus binding protein 4

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Hsp90 molecular chaperones are responsible for the conformational maturation of linear peptides into active three-dimensional enzymes and receptors. Examples of proteins dependent on the Hsp90 protein folding machinery include steroid hormone receptors, Src kinase, Her-2 kinase, Raf, p185, mutant p53, telomerase, PKR, telomerase, nitric oxide synthase, CDK-4 and CDK-6 to name a few. As Hsp90 continues to evolve into a popular target for the treatment of cancer more information is required to validate its role in the maturation of key regulatory proteins. For example, it is not known how many client proteins require Hsp90 for folding, or which of the four known forms of Hsp90 (a, b, GRP94, or TRP), immunophilin (FKBP51, FKBP52, or Cyp40), or cochaperone participate in the folding of various individual client proteins.

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 热休克蛋白90分子伴侣负责线性肽构象成熟为活性三维酶和受体。依赖于Hsp 90蛋白折叠机制的蛋白质的实例包括类固醇激素受体、Src激酶、Her-2激酶、Raf、p185、突变型p53、端粒酶、PKR、端粒酶、一氧化氮合酶、CDK-4和CDK-6，仅举几例。随着热休克蛋白90继续发展成为一个流行的癌症治疗靶点，需要更多的信息来验证其在关键调控蛋白成熟中的作用。例如，不知道有多少客户蛋白需要Hsp 90来折叠，或者Hsp 90的四种已知形式（a、B、GRP 94或TRP）、亲免蛋白（FKBP 51、FKBP 52或Cyp 40）或辅伴侣蛋白中的哪一种参与各种单个客户蛋白的折叠。