Results 81 to 90 of about 24,426,163 (152)

Six New Cases of 22q13.2 Gain Including TFC20: First Report of Triplication and Smallest Duplication Associated With Neurodevelopmental Delays

Clinical Genetics, Volume 108, Issue 6, Page 731-741, December 2025.
This study reports six new cases of 22q13.2 duplication and triplication, including the TCF20 gene, associated with neurodevelopmental disorders and various morphological and systemic abnormalities. The findings suggest a variable expressivity, but their complete penetrance remains uncertain compared to well‐established loss‐of‐function variants ...
Etienne Bizot, Dima Jouni, Caroline Rooryck, Juliet Taylor, Marine Legendre, Lorelei Charbonnier, Julia Metreau, Emmanuelle Benaloun, Audrey Pinson, Geneviève Quenum, Jérôme Bouligand, Gérard Tachdjian, Philippe Labrune, Lucie Tosca   +13 more
wiley   +1 more source

Exploring a Circulating miRNA Signature for PMM2‐CDG: Initial Insights Toward Diagnosis, Stratification, and Monitoring

Journal of Inherited Metabolic Disease, Volume 48, Issue 6, November 2025.
ABSTRACT Phosphomannomutase deficiency (PMM2‐CDG) is the most common congenital disorder of glycosylation, characterized by variable early‐onset neurological (hypotonia, cerebellar syndrome, developmental delay) and multi‐organ manifestations. Although several clinical trials are ongoing, current biomarkers lack prognostic or monitoring utility ...
Florencia Epifani, Lluc Cabus, Gregorio A. Nolasco, Mercè Bolasell, Jennifer Pérez, Adrián Alcalá, Patricia Fernández, Esther Lizano, Gisela Márquez, Sonia Belmonte, Sílvia Carbonell‐Sala, Julien Lagarde, Joao Curado, Cristina Hernando‐Davalillo, Mercedes Serrano   +14 more
wiley   +1 more source

Exploring ligand interactions with human phosphomannomutases using recombinant bacterial thermal shift assay and biochemical validation [PDF]

PMM2-CDG, a disease caused by mutations in phosphomannomutase-2, is the most common congenital disorder of glycosylation. Yet, it still lacks a cure. Targeting phosphomannomutase-2 with pharmacological chaperones or inhibiting the phosphatase activity of
Andreotti, Giuseppina, Cubellis, Maria Vittoria, Wright, Demi Marie, Guerriero, Simone, Monticelli, Maria, Hay Mele, Bruno   +5 more
core   +3 more sources

Expanding the phenotype of phosphomannomutase-2 gene congenital disorder of glycosylation: Cervical dystonia

Journal of the Neurological Sciences, 2017
Fil: Rossi, Malco Damian. Fundacion para la Lucha contra las Enfermedades Neurologicas de la Infancia; Argentina.
Malco Rossi, Alex Medina Escobar, Lucia Ameghino, Marcelo Merello   +3 more
openaire   +2 more sources

Optimizing (Bio) Catalysis with Liquid‐Liquid Phase Separation Systems

ChemSystemsChem, Volume 7, Issue 6, November 2025.
This review highlights how LLPS creates membraneless compartments involved in different scenarios in nature. It further explores different examples that focus on the development of synthetic coacervates that enhance catalytic efficiency by concentrating reactants, or by the direct influence of the coacervates building blocks themselves.
David Q. P. Reis, Joana Calvário, Inês Chibeles, Mohit Kumar, Ana S. Pina   +4 more
wiley   +1 more source

Mammalian phosphomannomutase PMM1 is the brain IMP-sensitive glucose-1,6-bisphosphatase

, 2008
Glucose 1,6-bisphosphate (Glc-1,6-P(2)) concentration in brain is much higher than what is required for the functioning of phosphoglucomutase, suggesting that this compound has a role other than as a cofactor of phosphomutases.
Vleugels, Wendy, Veiga da Cunha, Maria, Veiga-da-Cunha, Maria, Maliekal, Pushpa, Matthijs, Gert, Van Schaftingen, Emile   +5 more
core   +1 more source

Incidence and prevalence of phosphomannomutase 2-congenital disorder of glycosylation: Past, present, and future

Molecular Genetics and Metabolism
Phosphomannomutase 2-congenital disorder of glycosylation (PMM2-CDG) accounts for about 60 % of all CDGs and is caused by pathogenic variants of the gene encoding PMM2, which catalyzes an essential early step in N-linked glycosylation. Efforts to derive an accurate prevalence estimate for this often life-threatening disorder, for which there are ...
Andrew C, Edmondson, Tomáš, Honzík, Christina, Lam, Katrin, Õunap, Peter, McWilliams, Eva, Morava   +5 more
openaire   +2 more sources

Mutations in PMM2, a phosphomannomutase gene on chromosome 16p13, in carbohydrate-deficient glycoprotein type I syndrome (Jaeken syndrome)

, 1997
Carbohydrate-deficient glycoprotein syndrome type 1 (CDG1 or Jaeken syndrome) is the prototype of a class of genetic multisystem disorders characterized by defective glycosylation of glycoconjugates(1-4).
Veiga-da-Cunha, Maria, Gert Matthijs, Pardon, Els, Schollen, Els, Jaak Jaeken, Jaeken, Jaak, Els Schollen, Jean-Jacques Cassiman, Emile Van Schaftingen, Maria Veiga-Da-Cunha, Matthijs, Gert, Cassiman, Jean-Jacques, Van Schaftingen, Emile, Els Pardon   +13 more
core   +1 more source

Neural and metabolic dysregulation in PMM2-deficient human in vitro neural models

Cell Reports
Summary: Phosphomannomutase 2-congenital disorder of glycosylation (PMM2-CDG) is a rare inborn error of metabolism caused by deficiency of the PMM2 enzyme, which leads to impaired protein glycosylation.
Silvia Radenkovic, Rohit Budhraja, Teun Klein-Gunnewiek, Alexia Tyler King, Tarun N. Bhatia, Anna N. Ligezka, Karen Driesen, Rameen Shah, Bart Ghesquière, Akhilesh Pandey, Nael Nadif Kasri, Steven A. Sloan, Eva Morava, Tamas Kozicz   +13 more
doaj   +1 more source

Clinical severity and cardiac phenotype in phosphomannomutase 2‐congenital disorders of glycosylation : Insights into genetics and management recommendations [PDF]

Journal of Inherited Metabolic Disease
AbstractCardiac involvement (CI) in phosphomannomutase 2‐congenital disorders of glycosylation (PMM2‐CDG) is part of the multisystemic presentation contributing to high mortality rates. The most common cardiac manifestations are pericardial effusion, cardiomyopathy, and structural heart defects.
Holubova, V., Barone, R., Grunewald, S., Tesařová, M., Hansíková, H., Augustínová, J., Sykut-Cegielska, J., De Nictolis, F., Diaz-Moreno, U., Elangovan, R., Epifani, F., Gasperini, S., Janssen, M.C.H., Janssen, M.C.H., Lefeber, D.J., Lefeber, D.J., Maksym-Gasiorek, D., Diego, M., Ounap, K., Pettinato, F., Põder, H., Rymen, D., Vals, M.A., Serrano, M., Witters, P., Honzík, T.   +25 more
openaire   +5 more sources