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

Mutational analysis of thrombopoietin for identification of receptor and neutralizing antibody sites.

The Journal of biological chemistry - 15 Aug 1997

Pearce K H, Potts B J, Presta L G, Bald L N, Fendly B M, Wells J A

Abstract excerpt

Thrombopoietin (TPO) is a hematopoietin important for megakaryocyte proliferation and production of blood platelets. We sought to characterize how TPO binds and activates its receptor, myeloproliferative leukemia virus receptor. The erythropoietin-like domain of TPO (TPO1-153) has been fused to the gIII coat protein of M13 bacteriophage. Forty residues were chosen for mutation to alanine using the criteria that...

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 Antibodies, Monoclonal

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

Share to Binding Sites

Share to Mice, Inbred BALB C

Share to Molecular Sequence Data

Share to Mutation

Share to Sequence Alignment

Source

Identifiers

PMID: 9252374
DOI: 10.1074/jbc.272.33.20595

Genes

TPO

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

Mutational analysis of thrombopoietin for identification of receptor and neutralizing antibody sites.PMID 9252374Read ↗

Human thrombopoietin structure-function relationships: identification of functionally important residues.Semantic proximity Read ↗

Identification of individual human immunodeficiency virus type 1 gp120 amino acids important for CD4 receptor binding.Semantic proximity Read ↗

Human thrombopoietin: gene structure, cDNA sequence, expression, and chromosomal localization.Semantic proximity Read ↗

Mutations in the Trp-Ser-X-Trp-Ser motif of the erythropoietin receptor abolish processing, ligand binding, and activation of the receptor.Semantic proximity Read ↗

Identification of the primary collagen-binding surface on human glycoprotein VI by site-directed mutagenesis and by a blocking phage antibodySemantic proximity Read ↗

Amino acid residues 268-276 of the erythropoietin receptor contain an endocytosis motif and are required for erythropoietin-mediated proliferation.Semantic proximity Read ↗

Internalization of the thrombopoietin receptor is regulated by 2 cytoplasmic motifs.Semantic proximity Read ↗

Mapping of the Active Site of Recombinant Human ErythropoietinSemantic proximity Read ↗

Cell surface site for mitogenic interaction of erythropoietin receptors with the membrane glycoprotein encoded by Friend erythroleukemia virus.Semantic proximity Read ↗

Characterization of novel non-peptide thrombopoietin mimetics, their species specificity and the activation mechanism of the thrombopoietin receptor.Semantic proximity Read ↗

Erythropoietin structure-function relationships. Mutant proteins that test a model of tertiary structure.Semantic proximity Read ↗

Characterization of the truncated thrombopoietin variants.Semantic proximity Read ↗

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