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

Novel 150- and 180-kDa glycoproteins that bind transforming growth factor (TGF)-beta 1 but not TGF-beta 2 are present in several cell lines.

The Journal of biological chemistry - 25 May 1991

MacKay K, Danielpour D

Abstract excerpt

We identified transforming growth factor-beta (TGF-beta)-binding proteins which are distinct from previously described TGF-beta receptors or TGF-beta-binding proteins. These TGF-beta-binding proteins migrate as 150- and 180-kDa 125I-TGF-beta 1 affinity-labeled complexes which are consistently co-expressed in A549, Mv1Lu, MG-63, and BS-C-1 cells. They differ from the types I, II, and III TGF-beta receptors in...

Read the complete abstract on PubMed

Topics

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

Share to Cell Line
Share to Electrophoresis, Polyacrylamide Gel

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Glycoproteins

Share to Molecular Weight

Share to Phenotype

Share to Receptors, Cell Surface

Share to Substrate Specificity

Source

Identifiers

PMID: 1851759

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Novel 150- and 180-kDa glycoproteins that bind transforming growth factor (TGF)-beta 1 but not TGF-beta 2 are present in several cell lines.PMID 1851759Read ↗

The unglycosylated extracellular domain of type-II receptor for transforming growth factor-beta. A novel assay for characterizing ligand affinity and specificity.Semantic proximity Read ↗

Cellular growth inhibition by IGFBP‐3 and TGF‐β <sub>1</sub> requires LRP‐1Semantic proximity Read ↗

Transforming growth factor-beta 1, -beta 2, and -beta 3 secreted by a human glioblastoma cell line. Identification of small and different forms of large latent complexes.Semantic proximity Read ↗

Glycoproteomic analysis of two mouse mammary cell lines during transforming growth factor (TGF)-beta induced epithelial to mesenchymal transitionSemantic proximity Read ↗

Phenotypic alterations in fibroblasts and fibrosarcoma cells that overexpress latent transforming growth factor-beta 1.Semantic proximity Read ↗

A role of the latent TGF‐beta 1‐binding protein in the assembly and secretion of TGF‐beta 1.Semantic proximity Read ↗

Characterization of mutated transforming growth factor-beta s which possess unique biological properties.Semantic proximity Read ↗

[Functional analysis of transforming growth factor-beta type I receptor].Semantic proximity Read ↗

Loss of high affinity transforming growth factor-beta 1 (TGF-beta 1) binding to a nephritogenic T cell results in absence of growth inhibition by TGF-beta 1 and augmented nephritogenicity.Semantic proximity Read ↗

Transforming growth factor beta peptide antagonists and their conversion to partial agonists.Semantic proximity Read ↗

Receptors for immune complexes activate gene expression and synthesis of matrix proteins in cultured rat and human mesangial cells: role of TGF-betaSemantic proximity Read ↗

The pro domain of pre-pro-transforming growth factor beta 1 when independently expressed is a functional binding protein for the mature growth factor.Semantic proximity Read ↗

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