[HTML][HTML] Polymerizing Laminins in Development, Health and Disease

PD Yurchenco, AW Kulczyk - Journal of Biological Chemistry, 2024 - Elsevier
Polymerizing laminins are multi-domain basement membrane (BM) glycoproteins that self-
assemble into cell-anchored planar lattices to establish the initial BM scaffold. Nidogens …

Tailored placement of a turn-forming PA tag into the structured domain of a protein to probe its conformational state

Y Fujii, Y Matsunaga, T Arimori, Y Kitago… - Journal of Cell …, 2016 - journals.biologists.com
Placement of a tag sequence is usually limited to either terminal end of the target protein,
reducing the potential of epitope tags for various labeling applications. The PA tag is a …

Insights from molecular dynamics simulations: structural basis for the V567D mutation-induced instability of zebrafish alpha-dystroglycan and comparison with the …

D Pirolli, F Sciandra, M Bozzi, B Giardina… - PLoS …, 2014 - journals.plos.org
A missense amino acid mutation of valine to aspartic acid in 567 position of alpha-
dystroglycan (DG), identified in dag1-mutated zebrafish, results in a reduced transcription …

Analysis of the GFP-labelled β-dystroglycan interactome in HEK-293 transfected cells reveals novel intracellular networks

F Sciandra, C Desiderio, F Vincenzoni… - Biochemical and …, 2024 - Elsevier
Dystroglycan (DG) is a cell adhesion complex that is widely expressed in tissues. It is
composed by two subunits, α-DG, a highly glycosylated protein that interacts with several …

A dystroglycan mutation (p. Cys667Phe) associated to muscle‐eye‐brain disease with multicystic leucodystrophy results in ER‐retention of the mutant protein

G Signorino, S Covaceuszach, M Bozzi… - Human …, 2018 - Wiley Online Library
Dystroglycan (DG) is a cell adhesion complex composed by two subunits, the highly
glycosylated α‐DG and the transmembrane β‐DG. In skeletal muscle, DG is involved in …

[HTML][HTML] α-Dystroglycan hypoglycosylation affects cell migration by influencing β-dystroglycan membrane clustering and filopodia length: a multiscale confocal …

V Palmieri, M Bozzi, G Signorino, M Papi… - … et Biophysica Acta (BBA …, 2017 - Elsevier
Dystroglycan (DG) serves as an adhesion complex linking the actin cytoskeleton to the
extracellular matrix. DG is encoded by a single gene as a precursor, which is constitutively …

[HTML][HTML] Dystroglycan is associated to the disulfide isomerase Erp57

F Sciandra, E Angelucci, F Altieri, D Ricci… - Experimental cell …, 2012 - Elsevier
Dystroglycan (DG) is an extracellular receptor composed of two subunits, α-DG and β-DG,
connected through the α-DG C-terminal domain and the β-DG N-terminal domain. We report …

[HTML][HTML] β-dystroglycan is regulated by a balance between WWP1-mediated degradation and protection from WWP1 by dystrophin and utrophin

EB Cho, W Yoo, SK Yoon, JB Yoon - Biochimica et Biophysica Acta (BBA) …, 2018 - Elsevier
Dystroglycan is a ubiquitous membrane protein that functions as a mechanical connection
between the extracellular matrix and cytoskeleton. In skeletal muscle, dystroglycan plays an …

α-dystroglycan is a potential target of matrix metalloproteinase MMP-2

D Sbardella, F Sciandra, M Gioia, S Marini, A Gori… - Matrix Biology, 2015 - Elsevier
Dystroglycan (DG) is a member of the glycoprotein complex associated to dystrophin and
composed by two subunits, the β-DG, a transmembrane protein, and the α-DG, an …

The structure of the T190M mutant of murine α-dystroglycan at high resolution: insight into the molecular basis of a primary dystroglycanopathy

M Bozzi, A Cassetta, S Covaceuszach, MG Bigotti… - PLoS …, 2015 - journals.plos.org
The severe dystroglycanopathy known as a form of limb-girdle muscular dystrophy
(LGMD2P) is an autosomal recessive disease caused by the point mutation T192M in α …