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

Structural basis for misfolding in myocilin-associated glaucoma.

Human molecular genetics - 15 Apr 2015

Donegan Rebecca K, Hill Shannon E, Freeman Dana M, Nguyen Elaine, Orwig Susan D, Turnage Katherine C, Lieberman Raquel L

Abstract excerpt

Olfactomedin (OLF) domain-containing proteins play roles in fundamental cellular processes and have been implicated in disorders ranging from glaucoma, cancers and inflammatory bowel disorder, to attention deficit disorder and childhood obesity. We solved crystal structures of the OLF domain of m...

Read the complete abstract on PubMed

Topics

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

Share to Proteostasis Deficiencies
Share to Crystallization
Share to Cytoskeletal Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Eye Proteins

Share to Glaucoma

Share to Glycoproteins

Share to Protein Folding

Share to Protein Structure, Secondary

Source

Open in PubMed Open full text

Identifiers

PMID: 25524706
DOI: 10.1093/hmg/ddu730
PMCID: PMC4380063

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-25524706-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis for misfolding in myocilin-associated glaucoma.PMID 25524706Read ↗

The glaucoma-associated olfactomedin domain of myocilin is a novel calcium binding protein.Semantic proximity Read ↗

Common and rare myocilin variants: Predicting glaucoma pathogenicity based on genetics, clinical, and laboratory misfolding data.Semantic proximity Read ↗

The stability of myocilin olfactomedin domain variants provides new insight into glaucoma as a protein misfolding disorder.Semantic proximity Read ↗

Structure and misfolding of the flexible tripartite coiled coil domain of glaucoma-associated myocilinSemantic proximity Read ↗

Quantitative differentiation of benign and misfolded glaucoma-causing myocilin variants on the basis of protein thermal stability.Semantic proximity Read ↗

Aggregation-Prone Region Mapping in Olfactomedin Domain of Myocilin through Classical and Enhanced Sampling Molecular Dynamics SimulationsSemantic proximity Read ↗

Structural basis for anomalous cellular trafficking behavior of glaucoma-associated A427T mutant myocilinSemantic proximity Read ↗

Binding Interaction Between Two Mutant Myocilin Olfactomedin Domain Monomers in a Homodimer.Semantic proximity Read ↗

Expression and characterization of the olfactomedin domain of human myocilin.Semantic proximity Read ↗

Functional analysis of the glaucoma-causing TIGR/myocilin protein: integrity of amino-terminal coiled-coil regions and olfactomedin homology domain is essential for extracellular adhesion and secretion.Semantic proximity Read ↗

Competition between inside-out unfolding and pathogenic aggregation in an amyloid-forming β-propeller.Semantic proximity Read ↗

Systemic Genotype-Phenotype Analysis of MYOC Variants Based on Exome Sequencing and Literature Review.Semantic proximity Read ↗

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