Bibliographic record
Abstract
Background: Protein phosphorylation and dephosphorylation is an integral component of many cellular signaling pathways and regulatory mechanisms. Phosphatases are enzymes that catalyze the removal of phosphate groups from proteins. The phosphatases of regenerating liver (PRLs) are a family of phosphatases which have been correlated with cancer development and metastasis. However, they appear to have weak phosphatase activity and little is known about their physiological substrates. This review discusses PRL from a structural and functional perspective, including recent findings on its interaction with another family of proteins, cyclin M (CNNM). Methods: Articles were obtained from the scientific literature using databases like PubMed and McGill University’s open access institutional repository. This paper specifically focuses on those articles that provided an overview of phosphatases, PRLs, CNNMs, and structural and functional studies of PRLs and CNNMs. In total, 40 articles were selected for the purpose of this review. Summary: Although PRLs retain many of the structural features of other protein tyrosine phosphatases (PTPs) including the phosphatase catalytic motif and regulation via oxidation, other structural features such as mutation of a conserved serine/threonine residue to alanine in the active site disfavor catalytic activity. Moreover, PRL interaction with CNNM appears to be responsible for its oncogenic potential, yet this inter- action does not appear to require PRL phosphatase activity. Thus, PRL may be best classified as a pseudo-phosphatase, which are phosphatase-like proteins that are structurally similar to phosphatases but have acquired a dominant function that does not require phosphatase activity.
Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.
How this classification was reachedexpand
Full frame machine prediction
Teacher imitationNot calibrated prevalence, not ground truth. Human validation pending. The Gemma side is a direct model label for every work in the frame, read from the title-only record. The Codex side is a classifier learned from the 10,348 direct Codex labels and calibrated to design-weighted sample rates; fields without enough sample support carry no Codex call. Candidate is the union of the two sides; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels.
Distilled classifier scores by category (both heads)
| Category | Codex | Gemma |
|---|---|---|
| Metaresearch | 0.003 | 0.010 |
| Meta-epidemiology (narrow) | 0.001 | 0.000 |
| Meta-epidemiology (broad) | 0.001 | 0.001 |
| Bibliometrics | 0.003 | 0.002 |
| Science and technology studies | 0.001 | 0.005 |
| Scholarly communication | 0.004 | 0.008 |
| Open science | 0.001 | 0.002 |
| Research integrity | 0.005 | 0.004 |
| Insufficient payload (model declined to judge) | 0.003 | 0.002 |
Machine scores (provisional)
The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.
Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.
score_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from itClassification
machine, unvalidatedMachine predicted; a candidate call from one source (direct Gemma or distilled Codex), not a consensus.
How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".