ArticleThe EMBO journal2001
Crystal structure of the M-fragment of alpha-catenin: implications for modulation of cell adhesion.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 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
41 citing papers in PubMed, 72 citations in OpenAlex.
- Article
- Binding partner- and force-promoted changes in αE-catenin conformation probed by native cysteine labeling.Scientific reports · 2019Article
- Mechanical stability of αT-catenin and its activation by force for vinculin binding.Molecular biology of the cell · 2019Article
- α-Catenin Structure and Nanoscale Dynamics in Solution and in Complex with F-Actin.Biophysical journal · 2018Article
- Nonmuscle myosin IIA is involved in recruitment of apical junction components through activation of α-catenin.Biology open · 2018Article
- Establishment of a human primary pancreatic cancer mouse model to examine and investigate gemcitabine resistance.Oncology reports · 2017Article
- Biophysical Tools to Study Cellular Mechanotransduction.Bioengineering (Basel, Switzerland) · 2017Review
- αT-Catenin Is a Constitutive Actin-binding α-Catenin That Directly Couples the Cadherin·Catenin Complex to Actin Filaments.The Journal of biological chemistry · 2016Article
- Mechano-adaptive sensory mechanism of α-catenin under tension.Scientific reports · 2016Article
- Atomic-Resolution Structures of the APC/C Subunits Apc4 and the Apc5 N-Terminal Domain.Journal of molecular biology · 2015Article
- Structural Determinants of the Mechanical Stability of α-Catenin.The Journal of biological chemistry · 2015Article
- α-Catenin phosphorylation promotes intercellular adhesion through a dual-kinase mechanism.Journal of cell science · 2015Article
- Cell adhesion. The minimal cadherin-catenin complex binds to actin filaments under force.Science (New York, N.Y.) · 2014Article
- Structural and thermodynamic characterization of cadherin·β-catenin·α-catenin complex formation.The Journal of biological chemistry · 2014Article
- α-Catenin is an inhibitor of transcription.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- αE-catenin actin-binding domain alters actin filament conformation and regulates binding of nucleation and disassembly factors.Molecular biology of the cell · 2013Article
- The maternal-to-zygotic transition targets actin to promote robustness during morphogenesis.PLoS genetics · 2013Article
- An autoinhibited structure of α-catenin and its implications for vinculin recruitment to adherens junctions.The Journal of biological chemistry · 2013Article
- Monomeric α-catenin links cadherin to the actin cytoskeleton.Nature cell biology · 2013Article
- α-Catenin and vinculin cooperate to promote high E-cadherin-based adhesion strength.The Journal of biological chemistry · 2013Article
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
Abstract
The cytoskeletal protein alpha-catenin, which shares structural similarity with vinculin, is required for cadherin-mediated cell adhesion, and functions to modulate cell adhesive strength and to link the cadherins to the actin-based cytoskeleton. Here we describe the crystal structure of a region of alpha-catenin (residues 377-633) termed the M-fragment. The M-fragment is composed of a tandem repeat of two antiparallel four-helix bundles of virtually identical architectures that are related in structure to the dimerization domain of alpha-catenin and the tail region of vinculin. These results suggest that alpha-catenin is composed of repeating antiparallel helical domains. The region of alpha-catenin previously defined as an adhesion modulation domain corresponds to the C-terminal four-helix bundle of the M-fragment, and in the crystal lattice these domains exist as dimers. Evidence for dimerization of the M-fragment of alpha-catenin in solution was detected by chemical cross-linking experiments. The tendency of the adhesion modulation domain to form dimers may explain its biological activity of promoting cell-cell adhesiveness by inducing lateral dimerization of the associated cadherin molecule.
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.