Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Identification of the molecular recognition sequence which determines the type-specific assembly of procollagen.

The EMBO journal - 3 Mar 1997

Lees J F, Tasab M, Bulleid N J

Abstract excerpt

A key question relating to procollagen biosynthesis is the way in which closely related procollagen chains discriminate between each other to assemble in a type-specific manner. Intracellular assembly of procollagen occurs via an initial interaction between the C-propeptides followed by vectorial propagation of the triple-helical domain in the C to N direction. Recognition signals within the C-propeptides must,...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Electrophoresis, Polyacrylamide Gel
Share to Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Protein Conformation

Share to Recombinant Proteins

Share to Sequence Alignment

Source

Open in PubMed Open full text

Identifiers

PMID: 9118952
DOI: 10.1093/emboj/16.5.908
PMCID: PMC1169691

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of the molecular recognition sequence which determines the type-specific assembly of procollagen.PMID 9118952Read ↗

Type-III procollagen assembly in semi-intact cells: chain association, nucleation and triple-helix folding do not require formation of inter-chain disulphide bonds but triple-helix nucleation does require hydroxylation.Semantic proximity Read ↗

Defective C-propeptides of the proalpha2(I) chain of type I procollagen impede molecular assembly and result in osteogenesis imperfecta.Semantic proximity Read ↗

Structural basis of homo- and heterotrimerization of collagen I.Semantic proximity Read ↗

Position of single amino acid substitutions in the collagen triple helix determines their effect on structure of collagen fibrils.Semantic proximity Read ↗

A Collagen Triple Helix without the Super Helical TwistSemantic proximity Read ↗

Elastin as a self–organizing biomaterial: use of recombinantly expressed human elastin polypeptides as a model for investigations of structure and self–assembly of elastinSemantic proximity Read ↗

A common biosynthetic pathway governs the dimerization and secretion of inhibin and related transforming growth factor beta (TGFbeta) ligands.Semantic proximity Read ↗

Prodomain-growth factor swapping in the structure of pro-TGF-β1.Semantic proximity Read ↗

Design of a heterospecific, tetrameric, 21-residue miniprotein with mixed alpha/beta structure.Semantic proximity Read ↗

The NH2-terminal propeptide of type I procollagen acts intracellularly to modulate cell function.Semantic proximity Read ↗

Functional analysis of propeptide as an intramolecular chaperone for in vivo folding of subtilisin nattokinase.Semantic proximity Read ↗

Folding of peptide models of collagen and misfolding in disease.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.