ReviewJournal of molecular biology2011
Structure-guided identification of a laminin binding site on the laminin receptor precursor.
Review in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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
17 citing papers in PubMed, 25 citations in OpenAlex.
- Comprehensive analysis of LMNB2 in pan-cancer and identification of its biological role in sarcoma.Aging · 2024Article
- Channeling the Natural Properties of Sindbis Alphavirus for Targeted Tumor Therapy.International journal of molecular sciences · 2023Review
- Article
- Mutations in RPSA and NKX2-3 link development of the spleen and intestinal vasculature.Human mutation · 2020Article
- Selection of a novel DNA aptamer against OFA/iLRP for targeted delivery of doxorubicin to AML cells.Scientific reports · 2019Article
- A dock derived compound against laminin receptor (37 LR) exhibits anti-cancer properties in a prostate cancer cell line model.Oncotarget · 2018Article
- Looking into laminin receptor: critical discussion regarding the non-integrin 37/67-kDa laminin receptor/RPSA protein.Biological reviews of the Cambridge Philosophical Society · 2016Review
- Discovery of new small molecules inhibiting 67 kDa laminin receptor interaction with laminin and cancer cell invasion.Oncotarget · 2015Article
- Proteomic Analysis of Duodenal Tissue from Escherichia coli F18-Resistant and -Susceptible Weaned Piglets.PloS one · 2015Article
- Deciphering the complex three-way interaction between the non-integrin laminin receptor, galectin-3 and Neisseria meningitidis.Open biology · 2014Article
- From scourge to cure: tumour-selective viral pathogenesis as a new strategy against cancer.PLoS pathogens · 2014Review
- Fusion-related host proteins are actively regulated by NA during influenza infection as revealed by quantitative proteomics analysis.PloS one · 2014Article
- Article
- Comprehensive proteomic analysis of nonintegrin laminin receptor interacting proteins.Journal of proteome research · 2012Article
- PED/PEA-15 interacts with the 67 kD laminin receptor and regulates cell adhesion, migration, proliferation and apoptosis.Journal of cellular and molecular medicine · 2012Article
- Conformational switch of a flexible loop in human laminin receptor determines laminin-1 interaction.European biophysics journal : EBJ · 2012Article
- Interactions between laminin receptor and the cytoskeleton during translation and cell motility.PloS one · 2011Article
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
The 37/ 67-kDa human laminin receptor (LamR) is a cell surface receptor for laminin, prion protein, and a variety of viruses. Because of its wide range of ligands, LamR plays a role in numerous pathologies. LamR overexpression correlates with a highly invasive cell phenotype and increased metastatic ability, mediated by interactions between LamR and laminin. In addition, the specific targeting of LamR with small interfering RNAs, blocking antibodies, and Sindbis viral vectors confers anti-tumor effects. We adopted a structure-based approach to map a laminin binding site on human LamR by comparing the sequences and crystal structures of LamR and Archaeoglobus fulgidus S2p, a non-laminin-binding ortholog. Here, we identify a laminin binding site on LamR, comprising residues Phe32, Glu35, and Arg155, which are conserved among mammalian species. Mutation of these residues results in a significant loss of laminin binding. Further, recombinant wild-type LamR is able to act as a soluble decoy to inhibit cellular migration towards laminin. Mutation of this laminin binding site results in loss of migration inhibition, which demonstrates the physiological role of Phe32, Glu35, and Arg155 for laminin binding activity. Mapping of the LamR binding site should contribute to the development of therapeutics that inhibit LamR interactions with laminin and may aid in the prevention of tumor growth and metastasis.
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.