ReviewThe Biochemical journal2016
Inhibitory serpins. New insights into their folding, polymerization, regulation and clearance.
Review in The Biochemical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 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
55 citing papers in PubMed, 82 citations in OpenAlex.
- Next-generation heparin antidotes: "Exosomes as a biocompatible alternative to protamine sulfate".Molecular biology reports · 2026Article
- Review
- The Plasminogen Activation System in the Central Nervous System: Implications for Epilepsy and Neuropsychiatric Disorders.International journal of molecular sciences · 2025Review
- Host cell and viral protease targets of human SERPINs identified by in silico docking.The EMBO journal · 2025Article
- Harnessing Actinobacteria secondary metabolites for tuberculosis drug discovery: Historical trends, current status and future outlooks.Natural products and bioprospecting · 2025Review
- Physiological significance of antithrombin D-helix interaction with vascular GAGs.Blood advances · 2025Article
- A Contemporary Review of Plasminogen Activator Inhibitor Type 1: Structure, Function, Genetic Architecture, and Intracellular/Extracellular Roles.TH open : companion journal to thrombosis and haemostasis · 2025Review
- A signaling pathway map of plasminogen activator inhibitor-1 (PAI-1/SERPINE-1): a review of an innovative frontier in molecular aging and cellular senescence.Cell communication and signaling : CCS · 2024Review
- Regulation of CNS pathology by Serpina3n/SERPINA3: The knowns and the puzzles.Neuropathology and applied neurobiology · 2024Review
- ER chaperones use a protein folding and quality control glyco-code.Molecular cell · 2023Article
- Current Molecular, Cellular and Genetic Aspects of Peri-Implantitis Disease: A Narrative Review.Dentistry journal · 2023Review
- Landscape of Well-Coordinated Fracture Healing in a Mouse Model Using Molecular and Cellular Analysis.International journal of molecular sciences · 2023Article
- Identification and characterization of two SERPINC1 mutations causing congenital antithrombin deficiency.Thrombosis journal · 2023Article
- Circadian rhythm of plasminogen activator inhibitor-1 and cardiovascular complications in type 2 diabetes.Frontiers in endocrinology · 2023Review
- Pan-cancer analysis of SERPINE family genes as biomarkers of cancer prognosis and response to therapy.Frontiers in molecular biosciences · 2023Article
- The Role of Selected Serpins in Gastrointestinal (GI) Malignancies.Journal of clinical medicine · 2022Review
- Full-length antithrombin frameshift variant with aberrant C-terminus causes endoplasmic reticulum retention with a dominant-negative effect.JCI insight · 2022Article
- Specific Cerebrospinal Fluid SerpinA1 Isoform Pattern in Alzheimer's Disease.International journal of molecular sciences · 2022Article
- PAI-1: A Major Player in the Vascular Dysfunction in Obstructive Sleep Apnea?International journal of molecular sciences · 2022Review
- Fasciola hepatica is refractory to complement killing by preventing attachment of mannose binding lectin (MBL) and inhibiting MBL-associated serine proteases (MASPs) with serpins.PLoS pathogens · 2022Article
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
Serpins are a widely distributed family of high molecular mass protein proteinase inhibitors that can inhibit both serine and cysteine proteinases by a remarkable mechanism-based kinetic trapping of an acyl or thioacyl enzyme intermediate that involves massive conformational transformation. The trapping is based on distortion of the proteinase in the complex, with energy derived from the unique metastability of the active serpin. Serpins are the favoured inhibitors for regulation of proteinases in complex proteolytic cascades, such as are involved in blood coagulation, fibrinolysis and complement activation, by virtue of the ability to modulate their specificity and reactivity. Given their prominence as inhibitors, much work has been carried out to understand not only the mechanism of inhibition, but how it is fine-tuned, both spatially and temporally. The metastability of the active state raises the question of how serpins fold, whereas the misfolding of some serpin variants that leads to polymerization and pathologies of liver disease, emphysema and dementia makes it clinically important to understand how such polymerization might occur. Finally, since binding of serpins and their proteinase complexes, particularly plasminogen activator inhibitor-1 (PAI-1), to the clearance and signalling receptor LRP1 (low density lipoprotein receptor-related protein 1), may affect pathways linked to cell migration, angiogenesis, and tumour progression, it is important to understand the nature and specificity of binding. The current state of understanding of these areas is addressed here.
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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.