ReviewJournal of medicinal chemistry2016
Peptidyl-Proline Isomerases (PPIases): Targets for Natural Products and Natural Product-Inspired Compounds.
Review in Journal of medicinal chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
64 citing papers in PubMed, 125 citations in OpenAlex.
- Comparative proteomics reveals protein signatures shared between and unique to bona fide plant EVs and other plant-derived vesicles.Plant physiology · 2026Article
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- The impact of Iso-mukaadial acetate on Plasmodium falciparum transcriptional gene regulation.Scientific reports · 2025Article
- Biologically Active Benzimidazole Hybrids as Cancer Therapeutics: Recent Advances.Pharmaceuticals (Basel, Switzerland) · 2025Review
- Transfer RNA Aspartic Acid Methyltransferase 1 (TRDMT1/DNMT2) Regulates Plant Development and Gene Expression in the Moss Physcomitrium patens.Molecular genetics and genomics : MGG · 2025Article
- A human gut bacterium antagonizes neighboring bacteria by altering their protein-folding ability.Cell host & microbe · 2025Article
- Calcium-binding protein CALU-1 is essential for proper collagen formation in Caenorhabditis elegans.Cellular and molecular life sciences : CMLS · 2025Article
- Chaperone-mediated insertion of mitochondrial import receptor TOM70 protects against diet-induced obesity.Nature cell biology · 2025Article
- Genome-wide identification and expression analyses ofPhysiology and molecular biology of plants : an international journal of functional plant biology · 2024Article
- Evaluating the potential of non-immunosuppressive cyclosporin analogs for targeting Toxoplasma gondii cyclophilin: Insights from structural studies.Protein science : a publication of the Protein Society · 2024Article
- Insights into Peptidyl-ProlylPathogens (Basel, Switzerland) · 2024Review
- Article
- Long non-coding RNA-mediated modulation of endoplasmic reticulum stress under pathological conditions.Journal of cellular and molecular medicine · 2024Review
- Structure of prolylrapamycin: confirmation through a revised and detailed NMR assignment study.The Journal of antibiotics · 2024Article
- Article
- Proteomics Analysis Reveals the Underlying Factors of Mucilage Disappearance inFoods (Basel, Switzerland) · 2024Article
- Cyclophilin inhibition as a strategy for the treatment of human disease.Frontiers in pharmacology · 2024Review
- The role of the master cancer regulator Pin1 in the development and treatment of cancer.Frontiers in cell and developmental biology · 2024Review
- PPIH as a poor prognostic factor increases cell proliferation and m6A RNA methylation in hepatocellular carcinoma.American journal of cancer research · 2024Article
- Nicotine Exposure in a Phencyclidine-Induced Mice Model of Schizophrenia: Sex-Selective Medial Prefrontal Cortex Protein Markers of the Combined Insults in Adolescent Mice.International journal of molecular sciences · 2023Article
4 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Peptidyl-proline isomerases (PPIases) are a chaperone superfamily comprising the FK506-binding proteins (FKBPs), cyclophilins, and parvulins. PPIases catalyze the cis/trans isomerization of proline, acting as a regulatory switch during folding, activation, and/or degradation of many proteins. These "clients" include proteins with key roles in cancer, neurodegeneration, and psychiatric disorders, suggesting that PPIase inhibitors could be important therapeutics. However, the active site of PPIases is shallow, solvent-exposed, and well conserved between family members, making selective inhibitor design challenging. Despite these hurdles, macrocyclic natural products, including FK506, rapamycin, and cyclosporin, bind PPIases with nanomolar or better affinity. De novo attempts to derive new classes of inhibitors have been somewhat less successful, often showcasing the "undruggable" features of PPIases. Interestingly, the most potent of these next-generation molecules tend to integrate features of the natural products, including macrocyclization or proline mimicry strategies. Here, we review recent developments and ongoing challenges in the inhibition of PPIases, with a focus on how natural products might inform the creation of potent and selective inhibitors.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.