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

The insulin-like growth factor (IGF)binding protein 1 binding epitope on IGF-I probed by heteronuclear NMR spectroscopy and mutational analysis.

The Journal of biological chemistry - 18 Sept 1998

Jansson M, Andersson G, Uhlén M, Nilsson B, Kördel J

Abstract excerpt

NMR spectroscopy studies and biosensor interaction analysis of native and site-directed mutants of insulin-like growth factor I (IGF-I) was applied to identify the involvement of individual residues in IGF-I binding to IGF-binding protein 1 (IGFBP-1). Backbone NMR chemical shifts were found to be affected by IGFBP-1 binding in the following residues: Pro2, Glu3, Cys6, Gly7, Gly19, Pro28-Gly30, Gly32, Arg36,...

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 Binding Sites

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

Share to Cloning, Molecular

Share to DNA Primers

Share to Escherichia coli

Share to Genetic Variation

Share to Kinetics

Share to Polymerase Chain Reaction

Source

Identifiers

PMID: 9733769
DOI: 10.1074/jbc.273.38.24701

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

The insulin-like growth factor (IGF)binding protein 1 binding epitope on IGF-I probed by heteronuclear NMR spectroscopy and mutational analysis.PMID 9733769Read ↗

C-terminal domain of insulin-like growth factor (IGF) binding protein-6: structure and interaction with IGF-II.Semantic proximity Read ↗

How IGF-1 activates its receptor.Semantic proximity Read ↗

Computational model for the IGF-II/IGF2r complex that is predictive of mutational and surface plasmon resonance data.Semantic proximity Read ↗

Mutations at hypothetical binding site 2 in insulin and insulin-like growth factors 1 and 2.Semantic proximity Read ↗

Defining the epitope of a blood–brain barrier crossing single domain antibody specific for the type 1 insulin-like growth factor receptorSemantic proximity Read ↗

Functional characterization of a clinically significant variant of IGF1R (M1054I) - a critical residue involved in defining the binding of small molecules in the allosteric pocket of IGF1R.Semantic proximity Read ↗

Analyzing structural differences between insulin receptor (IR) and IGF1R for designing small molecule allosteric inhibitors of IGF1R as novel anti-cancer agents.Semantic proximity Read ↗

Insulin-like growth factor I and its binding proteins: a study of the binding interface using B-domain analogues.Semantic proximity Read ↗

Structural and functional characteristics of the Val44Met insulin-like growth factor I missense mutation: correlation with effects on growth and development.Semantic proximity Read ↗

Mutation of Arg55/56 to Leu55/Ala56 in insulin-like growth factor-I results in two forms different in disulfide structure and native conformation but similar under reverse-phase conditions.Semantic proximity Read ↗

Structural changes in insulin-like growth factor (IGF) I mutant proteins affecting binding kinetic rates to IGF binding protein 1 and IGF-I receptor.Semantic proximity Read ↗

Truncated forms of the insulin-like growth factor II (IGF-II)/mannose 6-phosphate receptor encompassing the IGF-II binding site: characterization of a point mutation that abolishes IGF-II binding.Semantic proximity Read ↗

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