Membrane Proteins and their Interactions
Bibliographic record
Abstract
The high water permeability of certain biological membranes is due to the presence of aquaporin water channel proteins.AQP1 was discovered in human red cells.AQP1 has been thoroughly characterized biophysically, and the atomic structure of AQP1 has been elucidated.Ten homologs have been identified in humans.These are selectively permeated by water (aquaporins) or water plus glycerol (aquaglyceroporins).The sites of expression predict the clinical phenotypes in humans.Individuals lacking Colton blood group antigens have mutations in the AQP1 gene.When deprived of water, AQP1-null individuals exhibit a defect in urine concentration and a marked reduction in fluid exchange between capillary and interstitium in lung.AQP1 is expressed in multiple tissues where physiologically important fluid secretion is known to occur including choroid plexus and anterior chamber of eye.AQP0 is expressed in lens fiber cells and mutations result in familial cataracts.AQP2 is expressed in renal collecting duct principal cells where membrane trafficking is regulated by vasopressin.Mutations in the human AQP2 gene result in nephrogenic diabetes insipidus, but underexpression is found in clinical disorders with reduced urinary concentration (e.g.lithium therapy and nocturnal enuresis) and overexpression is found in disorders with fluid retention (e.g.congestive heart failure and pregnancy).AQP5 is expressed in the apical membranes of salivary and lacrimal gland acini, and mistargeting has been identified in some patients with Sjogren's syndrome.Involvement of aquaporins is expected in other human clinical disorders such as brain edema and muscular dystrophy (AQP4), anhidrosis (AQP5) renal tubular acidosis (AQP6), conversion of glycerol to glucose during starvation (AQP7 and AQP9), and cystic fibrosis (several aquaporins).Aquaporins are known to protect micro-organisms from freezing and osmotic shock.Plant aquaporins are involved in numerous processes including the uptake of water by rootlets and carbon dioxide by leaves.The physiological roles of aquaporin homologs are being pursued by multiple laboratories worldwide.
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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 | 0.000 | 0.000 |
| Meta-epidemiology (narrow) | 0.000 | 0.000 |
| Meta-epidemiology (broad) | 0.000 | 0.000 |
| Bibliometrics | 0.000 | 0.000 |
| Science and technology studies | 0.001 | 0.000 |
| Scholarly communication | 0.001 | 0.001 |
| Open science | 0.000 | 0.001 |
| Research integrity | 0.001 | 0.001 |
| Insufficient payload (model declined to judge) | 0.002 | 0.001 |
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".