Target Name: PPIL1
NCBI ID: G51645
Review Report on PPIL1 Target / Biomarker Content of Review Report on PPIL1 Target / Biomarker
PPIL1
Other Name(s): Rotamase PPIL1 | CYPL1 | Peptidylprolyl isomerase like 1 | rotamase PPIL1 | cyclophilin like 1 | Peptidyl-prolyl cis-trans isomerase-like 1 | PCH14 | OTTHUMP00000016310 | MGC678 | Cyclophilin-related gene 1 | PPIL1_HUMAN | CGI-124 | cyclophilin-related gene 1 | peptidyl-prolyl cis-trans isomerase | peptidylprolyl isomerase like 1 | hCyPX | Peptidyl-prolyl cis-trans isomerase | PPIase | Peptidylprolyl Isomerase-like 1 | peptidylprolyl isomerase (cyclophilin)-like 1

PPIL1: A Promising Drug Target and Biomarker for Rotamase Enlightenment

Rotamase is an enzyme involved in the breakdown of rosin, a crucial component in cell membranes, which is essential for various cellular processes. The poly (ADP-ribose) polymerase (PARP) is a key enzyme in the regulation of DNA repair, and it has been implicated in the development of many diseases, including cancer. The PARP/Rotamase interaction is a promising area of research for the development of new therapeutic strategies.

PPIL1: A novel protein involved in the Rotamase-PARP interaction

The Parkin gene is a well-known gene associated with the development of Parkinson's disease, a neurodegenerative disorder that affects millions of people worldwide. The Parkin gene has four splice variants, and the most abundant variant is encoding a protein named Parkin, which is involved in the development of neurodegeneration.

Recent studies have suggested that the Parkin gene may also be involved in the development of other diseases, including cancer. The Rotamase enzyme, which is critical for the breakdown of rosin in cell membranes, has been linked to the development of various diseases, including cancer. The Rotamase-PARP interaction is a promising area of research for the development of new therapeutic strategies.

PPIL1: A novel protein that can modulate the activity of PARP

The PARP/Rotamase interaction is a complex process that involves the interaction of the Rotamase enzyme with the PARP protein. The PARP protein is a key enzyme involved in the regulation of DNA repair, and it has been implicated in the development of many diseases, including cancer.

Recent studies have shown that the PARP protein can interact with the Rotamase enzyme, leading to changes in the activity of the PARP enzyme. The interaction between the PARP and Rotamase enzymes is critical for the regulation of DNA repair processes, which are essential for the development and maintenance of healthy cell membranes.

PPIL1: A novel protein that can modulate the activity of PARP

The Parkin gene has four splice variants, and the most abundant variant is encoding a protein named Parkin. The Parkin protein is involved in the development of neurodegeneration, and it has been linked to the development of various diseases, including cancer.

Recent studies have suggested that the Parkin gene may also be involved in the development of other diseases, including cancer. The Rotamase enzyme, which is critical for the breakdown of rosin in cell membranes, has been linked to the development of various diseases, including cancer. The Rotamase-PARP interaction is a promising area of research for the development of new therapeutic strategies.

PPIL1: Potential drug targets for the treatment of cancer

The Rotamase-PARP interaction is a critical process involved in the development and maintenance of healthy cell membranes. The interaction between the PARP and Rotamase enzymes is essential for the regulation of DNA repair processes, which are essential for

Protein Name: Peptidylprolyl Isomerase Like 1

Functions: Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:28502770, PubMed:28076346, PubMed:33220177). PPIases accelerate the folding of proteins. Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (PubMed:16595688). Catalyzes prolyl peptide bond isomerization in CDC40/PRP17 (PubMed:33220177). Plays an important role in embryonic brain development; this function is independent of its isomerase activity (PubMed:33220177)

The "PPIL1 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about PPIL1 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

More Common Targets

PPIL2 | PPIL3 | PPIL4 | PPIL6 | PPIP5K1 | PPIP5K2 | PPL | PPM1A | PPM1B | PPM1D | PPM1E | PPM1F | PPM1G | PPM1H | PPM1J | PPM1K | PPM1K-DT | PPM1L | PPM1M | PPM1N | PPME1 | PPOX | PPP1CA | PPP1CB | PPP1CC | PPP1R10 | PPP1R11 | PPP1R12A | PPP1R12A-AS1 | PPP1R12B | PPP1R12C | PPP1R13B | PPP1R13B-DT | PPP1R13L | PPP1R14A | PPP1R14B | PPP1R14B-AS1 | PPP1R14BP3 | PPP1R14C | PPP1R14D | PPP1R15A | PPP1R15B | PPP1R16A | PPP1R16B | PPP1R17 | PPP1R18 | PPP1R1A | PPP1R1B | PPP1R1C | PPP1R2 | PPP1R21 | PPP1R26 | PPP1R26-AS1 | PPP1R26P2 | PPP1R27 | PPP1R2B | PPP1R2C | PPP1R2P1 | PPP1R2P2 | PPP1R2P4 | PPP1R2P5 | PPP1R32 | PPP1R35 | PPP1R36 | PPP1R37 | PPP1R3A | PPP1R3B | PPP1R3B-DT | PPP1R3C | PPP1R3D | PPP1R3E | PPP1R3F | PPP1R3G | PPP1R42 | PPP1R7 | PPP1R8 | PPP1R9A | PPP1R9B | PPP2CA | PPP2CB | PPP2R1A | PPP2R1B | PPP2R2A | PPP2R2B | PPP2R2B-IT1 | PPP2R2C | PPP2R2D | PPP2R3A | PPP2R3B | PPP2R3C | PPP2R5A | PPP2R5B | PPP2R5C | PPP2R5D | PPP2R5E | PPP3CA | PPP3CB | PPP3CB-AS1 | PPP3CC | PPP3R1