ArticleJournal of amino acids2011
Serpin Inhibition Mechanism: A Delicate Balance between Native Metastable State and Polymerization.
Article in Journal of amino acids, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
What it found
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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.
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Who cites it
47 citing papers in PubMed, 87 citations in OpenAlex.
- The Serpin Superfamily in Adipose Tissue Remodeling: Molecular Drivers of Immune-Metabolic Crosstalk and Insulin Sensitivity.Biology · 2026Review
- Reversal of filarial serpin Wb123-urokinase plasminogen activator receptor mediated alternative macrophage activation by monoclonal antibody.PLoS neglected tropical diseases · 2025Article
- Functional mass spectrometry indicates anti-protease and complement activity increase with COVID-19 severity.Experimental biology and medicine (Maywood, N.J.) · 2025Article
- Regulation of CNS pathology by Serpina3n/SERPINA3: The knowns and the puzzles.Neuropathology and applied neurobiology · 2024Review
- SERPINC1 c.1247dupC: a novel SERPINC1 gene mutation associated with familial thrombosis results in a secretion defect and quantitative antithrombin deficiency.Thrombosis journal · 2024Article
- Alpha-1-antitrypsin as novel substrate forFrontiers in immunology · 2024Article
- A Genome-Wide Analysis of Serine Protease Inhibitors inInternational journal of molecular sciences · 2023Article
- Conformational transition of the Ixodes ricinus salivary serpin Iripin-4.Acta crystallographica. Section D, Structural biology · 2023Article
- Article
- Insights into the pathogenesis of hereditary angioedema using genetic sequencing and recombinant protein expression analyses.The Journal of allergy and clinical immunology · 2023Article
- Iripin-1, a new anti-inflammatory tick serpin, inhibits leukocyte recruitmentFrontiers in immunology · 2023Article
- Genome-Wide Characterization and Comparative Genomic Analysis of the Serpin Gene Family in MicrosporidianInternational journal of molecular sciences · 2022Article
- Strand 1A variant in neuroserpin shows increased aggregation and no loss of inhibition: implication in ameliorating polymerization to retain activity.Bioscience reports · 2022Article
- New variants of alpha-1-antitrypsin: structural simulations and clinical expression.Respiratory research · 2022Article
- The Role of Selected Serpins in Gastrointestinal (GI) Malignancies.Journal of clinical medicine · 2022Review
- Vision-related convergent gene losses revealeLife · 2022Article
- Like Brothers in Arms: How Hormonal Stimuli and Changes in the Metabolism Signaling Cooperate, Leading HPV Infection to Drive the Onset of Cervical Cancer.International journal of molecular sciences · 2022Review
- Grass carp SERPINA1 inhibits GCRV infection through degrading CF2.Frontiers in immunology · 2022Article
- Review
- The role of SERPIN citrullination in thrombosis.Cell chemical biology · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The serpins (serine proteinase inhibitors) are structurally similar but functionally diverse proteins that fold into a conserved structure and employ a unique suicide substrate-like inhibitory mechanism. Serpins play absolutely critical role in the control of proteases involved in the inflammatory, complement, coagulation and fibrinolytic pathways and are associated with many conformational diseases. Serpin's native state is a metastable state which transforms to a more stable state during its inhibitory mechanism. Serpin in the native form is in the stressed (S) conformation that undergoes a transition to a relaxed (R) conformation for the protease inhibition. During this transition the region called as reactive center loop which interacts with target proteases, inserts itself into the center of β-sheet A to form an extra strand. Serpin is delicately balanced to perform its function with many critical residues involved in maintaining metastability. However due to its typical mechanism of inhibition, naturally occurring serpin variants produces conformational instability that allows insertion of RCL of one molecule into the β-sheet A of another to form a loop-sheet linkage leading to its polymerization and aggregation. Thus understanding the molecular basis and amino acid involved in serpin polymerization mechanism is critical to devising strategies for its cure.
Identifiers
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.