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

Internal dynamics and ionization states of the macrophage migration inhibitory factor: comparison between wild-type and mutant forms.

Biopolymers - 15 Nov 2002

Soares T A, Lins R D, Straatsma T P, Briggs J M

Abstract excerpt

The macrophage migration inhibitory factor (MIF) is a cytokine that shares a common structural architecture and catalytic strategy with three isomerases: 4-oxalocrotonate tautomerase, 5-carboxymethyl-2-hydroxymuconate isomerase, and D-dopachrome tautomerase. A highly conserved N-terminal proline acts as a base-acid during the proton transfer reaction catalyzed by these enzymes. Such unusual catalytic strategy...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Hydrogen-Ion Concentration

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to In Vitro Techniques

Share to Macrophage Migration-Inhibitory Factors

Share to Models, Molecular

Share to Protein Conformation

Share to Thermodynamics

Source

Identifiers

PMID: 12382291
DOI: 10.1002/bip.10252

Genes

MIF

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Internal dynamics and ionization states of the macrophage migration inhibitory factor: comparison between wild-type and mutant forms.PMID 12382291Read ↗

Characterization of molecular determinants of the conformational stability of macrophage migration inhibitory factor: leucine 46 hydrophobic pocket.Semantic proximity Read ↗

Mechanism of the phenylpyruvate tautomerase activity of macrophage migration inhibitory factor: properties of the P1G, P1A, Y95F, and N97A mutants.Semantic proximity Read ↗

A tautomerase-null macrophage migration-inhibitory factor (MIF) gene knock-in mouse model reveals that protein interactions and not enzymatic activity mediate MIF-dependent growth regulation.Semantic proximity Read ↗

Theoretical 3D model of histamine N-methyltransferase: insights into the effects of a genetic polymorphism on enzymatic activity and thermal stability.Semantic proximity Read ↗

Redox-dependent Structure and Dynamics of Macrophage Migration Inhibitory Factor Reveal Sites of Latent AllosterySemantic proximity Read ↗

Can Mutational Analysis Be Used To Assist Structure Determination of Peptides?Semantic proximity Read ↗

Enhancing the thermal stability of a single-chain Fv fragment by in vivo global fluorination of the proline residuesSemantic proximity Read ↗

In Silico Analysis of Conformational Changes Induced by Normal and Mutation of Macrophage Infectivity Potentiator Catalytic Residues and its Interactions with Rapamycin.Semantic proximity Read ↗

Exploring the structural constraints at cleavage site of mucin 1 isoform through molecular dynamics simulation.Semantic proximity Read ↗

Incorporation of a glycine within the conserved TCPCP motif of human neuronal growth inhibitory factor significantly reduces its bioactivity.Semantic proximity Read ↗

HFIP-induced structures and assemblies of the peptides from the transmembrane domain 4 of membrane protein Nramp1.Semantic proximity Read ↗

Understanding the enzymatic activity of 4-oxalocrotonate tautomerase and its mutant analogues: a computational study.Semantic proximity Read ↗

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