ArticleProceedings of the National Academy of Sciences of the United States of America1991
Identification of a 160-kDa polypeptide that binds to the tight junction protein ZO-1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 141 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
141 citing papers in PubMed, 517 citations in OpenAlex.
- Article
- Food-derived molecules as regulators of intestinal tight junctions and barrier function: mechanisms and implications.Frontiers in drug delivery · 2026Review
- Dietary Flavonoids as Cross-System Modulators of Hypertension and Intestinal Permeability.Molecules (Basel, Switzerland) · 2025Review
- Understanding the Blood-Brain Barrier: From Physiology to Pathology.Advances in experimental medicine and biology · 2025Review
- Article
- Progressive familial intrahepatic cholestasis type 4: a case report.Journal of medical case reports · 2024Article
- ZO-1 interacts with YB-1 in endothelial cells to regulate stress granule formation during angiogenesis.Nature communications · 2024Article
- Canonical and Non-Canonical Localization of Tight Junction Proteins during Early Murine Cranial Development.International journal of molecular sciences · 2024Article
- A Rare Case of Progressive Familial Intrahepatic Cholestasis Type 4: A Case Report and Literature Review.Cureus · 2023Article
- Research progress of Claudin-low breast cancer.Frontiers in oncology · 2023Review
- Stroke-induced damage on the blood-brain barrier.Frontiers in neurology · 2023Review
- Transgenic animal models to explore and modulate the blood brain and blood retinal barriers of the CNS.Fluids and barriers of the CNS · 2022Review
- Article
- Differential expression and localization of tight junction proteins in the goat epididymis.Journal of animal science and technology · 2022Article
- Cingulin binds to the ZU5 domain of scaffolding protein ZO-1 to promote its extended conformation, stabilization, and tight junction accumulation.The Journal of biological chemistry · 2022Article
- Newer variants of progressive familial intrahepatic cholestasis.World journal of hepatology · 2021Review
- Article
- The Epithelial Cell Leak Pathway.International journal of molecular sciences · 2021Review
- Larazotide acetate: a pharmacological peptide approach to tight junction regulation.American journal of physiology. Gastrointestinal and liver physiology · 2021Review
- Partners in Leaky Gut Syndrome: Intestinal Dysbiosis and Autoimmunity.Frontiers in immunology · 2021Review
81 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
ZO-1 is a 210- to 220-kDa peripheral membrane protein associated with the cytoplasmic surface of the epithelial tight junction. Because ZO-1 may interact with other unidentified tight junction proteins, we have looked for other polypeptides that bind to ZO-1. A 160-kDa polypeptide was identified that coimmunoprecipitates with ZO-1 from detergent extracts of metabolically labeled Madin-Darby canine kidney (MDCK) cells. This polypeptide appears to be distinct from ZO-1, rather than a degradation product, by several criteria. It lacks ZO-1 epitopes recognized by both monoclonal antibodies and a polyclonal serum to ZO-1, since it is not detectable in immunoblots of either whole cell extracts or ZO-1 immunoprecipitates. Also, it exhibits a peptide map different from that of ZO-1 on one-dimensional "Cleveland gels." Moreover, because the kinetics of appearance of newly synthesized 160-kDa polypeptide in anti-ZO-1 immunoprecipitates is much slower than that of ZO-1, its presence in immunoprecipitates cannot be simply explained by degradation of ZO-1 during cell lysis. Like ZO-1, the 160-kDa polypeptide seems to be a cytoplasmic peripheral membrane protein. It cannot be labeled by two different cell surface labeling reagents. It can be extracted from the membrane by high salt concentration in the absence of detergents. As expected for a protein complex, the 160-kDa polypeptide and ZO-1 turn over with similar kinetics. We propose that the 160-kDa polypeptide is a component of the tight junction.
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.