<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>50(6)</volume><submitter>Chavda ND</submitter><funding>Biotechnology and Biological Sciences Research Council</funding><pubmed_abstract>Basement membranes (BMs) are structured regions of the extracellular matrix that provide multiple functions including physical support and acting as a barrier, as a repository for nutrients and growth factors, and as biophysical signalling hubs. At the core of all BMs is the laminin (LM) family of proteins. These large heterotrimeric glycoproteins are essential for tissue integrity, and differences between LM family members represent a key nexus in dictating context and tissue-specific functions. These variations reflect genetic diversity within the family, which allows for multiple structurally and functionally distinct heterotrimers to be produced, each with different architectures and affinities for other matrix proteins and cell surface receptors. The ratios of these LM isoforms also i</pubmed_abstract><journal>Biochemical Society transactions</journal><pagination>1541-1553</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9788559</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Laminin N-terminus (LaNt) proteins, laminins and basement membrane regulation.</pubmed_title><pmcid>PMC9788559</pmcid><pubmed_authors>Hamill KJ</pubmed_authors><pubmed_authors>Asiri FM</pubmed_authors><pubmed_authors>Chavda ND</pubmed_authors><pubmed_authors>Sari B</pubmed_authors></additional><is_claimable>false</is_claimable><name>Laminin N-terminus (LaNt) proteins, laminins and basement membrane regulation.</name><description>Basement membranes (BMs) are structured regions of the extracellular matrix that provide multiple functions including physical support and acting as a barrier, as a repository for nutrients and growth factors, and as biophysical signalling hubs. At the core of all BMs is the laminin (LM) family of proteins. These large heterotrimeric glycoproteins are essential for tissue integrity, and differences between LM family members represent a key nexus in dictating context and tissue-specific functions. These variations reflect genetic diversity within the family, which allows for multiple structurally and functionally distinct heterotrimers to be produced, each with different architectures and affinities for other matrix proteins and cell surface receptors. The ratios of these LM isoforms also i</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Dec</publication><modification>2025-04-05T11:24:17.554Z</modification><creation>2025-04-05T11:24:17.554Z</creation></dates><accession>S-EPMC9788559</accession><cross_references><pubmed>36355367</pubmed><doi>10.1042/BST20210240</doi></cross_references></HashMap>