ReviewCentral European journal of urology2011
The calpain system as a potential target for pelvic muscle reinforcement.
Review in Central European journal of urology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed, 3 citations in OpenAlex.
- Trade-off between branching and polarity controls decision-making during cell migration.Science advances · 2026Article
- Age-associated proinflammatory elastic fiber remodeling in large arteries.Mechanisms of ageing and development · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The fascial and muscular components within the pelvic floor create a support mechanism that facilitates storage and voiding of urine. Their constituents are mainly fibrillar collagens I and III, which are responsible for maintaining tensile strength. Stretching and recoiling is enabled by the elastic fibers consisting of elastin on a scaffold of microfibrils, fibrillin-1 and -2. Calpains are intracellular Ca2+ -dependent cysteine proteases found in almost all eukaryotes and some bacteria. Calpains display limited proteolytic activity at neutral pH, proteolyzing substrates to transform and modulate their structures and activities, and are therefore called "modulator proteases". By making selective limited proteolytic cleavages, they modulate the activity of enzymes, including key signaling molecules, and induce specific cytoskeletal rearrangements, accounting for their roles in signal transduction and structural stabilization. Understanding these mechanisms should provide avenues for novel therapeutic strategies to treat pathological processes such as urinary incontinence and pelvic prolapse.
Indexed as
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.