Article

A spectrum of clinically-identified cysteine mutations in fibulin-3 (EFEMP1) highlight its disulfide bonding complexity and potential to induce stress response activation

2024-07-23

Abstract excerpt

<h4>ABSTRACT</h4> Fibulin-3 (FBLN3), also known as EFEMP1, is a secreted extracellular matrix (ECM) glycoprotein that contains forty cysteine residues. These cysteines, which are distributed across one atypical and five canonical calcium-binding epidermal growth factor (EGF) domains, are important for regulating FBLN3 structure, secretion, and presumably function. As evidence of this importance, a rare homozygous...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: c11e249b-1d17-5eb6-9bc3-84862509b24d
DOI: 10.1101/2024.07.22.604634

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

A spectrum of clinically-identified cysteine mutations in fibulin-3 (EFEMP1) highlight its disulfide bonding complexity and potential to induce stress response activationDOI 10.1101/2024.07.22.604634Read

A loss-of-function cysteine mutant in fibulin-3 (EFEMP1) forms aberrant extracellular disulfide-linked homodimers and alters extracellular matrix compositionSemantic proximity Read

A loss-of-function cysteine mutant in fibulin-3 (EFEMP1) forms aberrant extracellular disulfide-linked homodimers and alters extracellular matrix composition.Semantic proximity Read

Fibrillin-1 Misfolding and DiseaseSemantic proximity Read

A G1127S change in calcium-binding epidermal growth factor-like domain 13 of human fibrillin-1 causes short range conformational effects.Semantic proximity Read

Differential tolerance of 'pseudo-pathogenic' tryptophan residues in calcium-binding EGF domains of short fibulin proteins.Semantic proximity Read

Clinically-identified C-terminal mutations in fibulin-3 are prone to misfolding and destabilization.Semantic proximity Read

Marfan syndrome variation of the POGLUT2 and POGLUT3 consensus sequence can produce aberrant fibrillin-1 O-glucosylationSemantic proximity Read

Reclassification of an FBN1 variant emphasizes the importance of segregation analysis, information sharing, and multidisciplinary teamwork in understanding genetic variants in health and disease.Semantic proximity Read

Mutation of fibulin-1 causes a novel syndrome involving the central nervous system and connective tissues.Semantic proximity Read

Consequences of cysteine mutations in calcium-binding epidermal growth factor modules of fibrillin-1.Semantic proximity Read

Cellular and molecular studies of Marfan syndrome mutations identify co-operative protein folding in the cbEGF12-13 region of fibrillin-1.Semantic proximity Read

Cysteine substitutions in epidermal growth factor-like domains of fibrillin-1: distinct effects on biochemical and clinical phenotypes.Semantic proximity Read