Ask about this productRelated genes to: PPIH Blocking Peptide
- Gene:
- PPIH NIH gene
- Name:
- peptidylprolyl isomerase H
- Previous symbol:
- -
- Synonyms:
- USA-CYP, CYP-20, SnuCyp-20, CYPH, MGC5016
- Chromosome:
- 1p34.2
- Locus Type:
- gene with protein product
- Date approved:
- 2001-03-16
- Date modifiied:
- 2016-10-05
Related products to: PPIH Blocking Peptide
Related articles to: PPIH Blocking Peptide
- Diabetic foot ulcer (DFU) is one of the most common and severe complications of diabetes, with vascular changes, neuropathy, and infections being the primary pathological mechanisms. Disulfidptosis, a recently identified form of programmed cell death, might be involved in the development of diabetic complications. This study aims to identify and validate potential disulfidptosis biomarkers associated with DFU through bioinformatics and machine learning analysis. - Source: PubMed
Publication date: 2025/10/08
Li JIeShi HongshuoCao Yemin - Psoriasis remains a significant global health concern, with a lack of effective treatments, thus driving the need for innovative therapeutic approaches. Polyphyllin I (PPI) has demonstrated potential in mitigating inflammation and controlling cellular growth, although the precise mechanisms underlying its effects and its full therapeutic capabilities in psoriasis require further investigation. - Source: PubMed
Publication date: 2025/12/05
Zhou XiangnanChen QilongChen ZiyinSong BiaoLi JihongNing Jingyuan - Malignant tumors remain a major threat to global human health. This study aimed to systematically integrate multi-omics data to identify a candidate gene with biomarker potential across diverse cancer types and to evaluate its possible clinical applications in oncology. - Source: PubMed
Publication date: 2025/08/14
Lv FenglinZhang XinluWu YanmeiLi ZhipengZheng XiaomenZhou HuaxinWang Wei - The SARS-CoV-2 non-structural protein 1 (Nsp1) acts at multiple points toward the host cell to trigger its mRNA cleavage and decay. Nsp1 is found binding with the 40S ribosomal subunit and inhibiting the translation process, as well as docking with different cyclophilins. Herein, we evaluated the structural physicochemical properties of SARS-CoV-2 Nsp1 protein implementing different computational techniques. The Nsp1 was found to form a structured α-helical C-terminal region, following a conformational switch at residue S166 that is necessary for binding the 40S ribosome subunit. Similarly, the presence of cyclophilins stabilizes the Nsp1 C-terminus making a tilt movement at position 166. In the 40S ribosome-Nsp1 machinery, both the ribosomal uS3 and eS30 components were found equally interacting with Nsp1, which guided construction of their pharmacophores. Among a set of studied cyclophilins, FKBP1B showed the highest affinity with Nsp1 and PPIH made least interactions. The majority of cyclophilins dock to the conserved Nsp1 loop or linker region, which connects the C-terminus to the central domain. Our findings revealed that Nsp1 has a versatile C-terminus region which changes its conformations with respect to its host binding partner. Identified novel binding sites within the Nsp1 can assist in understanding its networking (in current or future such infections), as well as support drug discovery programs aimed at targeting the coronavirus family. - Source: PubMed
Publication date: 2025/06/14
Padariya MonikabenHupp TedKalathiya Umesh - Cholangiocarcinoma (CHOL) is the second most common primary liver malignancy, characterized by high aggressiveness and heterogeneity. It is typically diagnosed at an advanced stage, leading to a poor prognosis. Although Peptidyl Proline Isomerase H (PPIH) has been implicated in various tumors, its role in CHOL remains unexplored. This study aims to investigate the diagnostic value and potential function of PPIH in CHOL. - Source: PubMed
Publication date: 2025/02/07
Ye JunChen ZhitaoZhang ChuanXie RuiChen HainiRen Peng