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

Biochemical Analysis of Interaction between Kringle Domains of Plasminogen and Prion Proteins with Q167R Mutation.

Journal of microbiology and biotechnology - 28 May 2017

Lee Jeongmin, Lee Byoung Woo, Kang Hae-Eun, Choe Kevine K, Kwon Moosik, Ryou Chongsuk

Abstract excerpt

The conformational change of cellular prion protein (PrPC) to its misfolded counterpart, termed PrPSc, is mediated by a hypothesized cellular cofactor. This cofactor is believed to interact directly with certain amino acid residues of PrPC. When these are mutated into cationic amino acid residues, PrPSc formation and prion replication halt in a dominant negative (DN) manner, presumably due to strong binding of...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to Bacteria

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Coenzymes

Share to Kringles

Share to Plasminogen

Share to Prion Proteins

Share to Protein Folding

Share to Protein Interaction Domains and Motifs

Source

Identifiers

PMID: 28274104
DOI: 10.4014/jmb.1702.02029

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Biochemical Analysis of Interaction between Kringle Domains of Plasminogen and Prion Proteins with Q167R Mutation.PMID 28274104Read ↗

Cryptic peptides of the kringle domains preferentially bind to disease-associated prion protein.Semantic proximity Read ↗

Both lysine-clusters of the NH2-terminal prion-protein fragment PrP23-110 are essential for t-PA mediated plasminogen activation.Semantic proximity Read ↗

The Plasminogen-Binding Group A Streptococcal M Protein-Related Protein Prp Binds Plasminogen via Arginine and Histidine ResiduesSemantic proximity Read ↗

The unfolding of the prion protein sheds light on the mechanisms of prion susceptibility and species barrier.Semantic proximity Read ↗

Prion proteins with pathogenic and protective mutations show similar structure and dynamics.Semantic proximity Read ↗

The kringle domains of human plasminogen.Semantic proximity Read ↗

PlasminogenSemantic proximity Read ↗

Expression, isolation and characterization of a mutated human plasminogen kringle 3 with a functional lysine binding site.Semantic proximity Read ↗

Cooperative binding of dominant-negative prion protein to kringle domains.Semantic proximity Read ↗

High yield purification and physico-chemical properties of full-length recombinant allelic variants of sheep prion protein linked to scrapie susceptibility.Semantic proximity Read ↗

Staphylokinase Requires NH2-terminal Proteolysis for Plasminogen ActivationSemantic proximity Read ↗

Coevolutionary patterns in plasminogen activation.Semantic proximity Read ↗

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