{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nThe provided abstracts primarily address the key roles of phosphomannomutase 2 (PMM2) in protein glycosylation and developmental processes, rather than discussing ACTL10. Indeed, these studies describe how PMM2 is indispensable for early embryonic viability, proper glycoprotein synthesis, and overall organismal development, as illustrated by targeted disruption and mutant mouse models that recapitulate aspects of congenital disorders of glycosylation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nA separate series of investigations explored the complementary expression patterns of PMM1 and PMM2 in neural tissues, revealing that despite overlapping expression, PMM1 does not compensate for PMM2 deficiency in the brain. This emphasizes that the pathological features of CDG-Ia stem from specific functional deficits of PMM2 rather than from a redundancy with related enzymes."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditional studies have detailed the ontogeny of mannose transport and enzymatic activity in the intestine, as well as the potential rescue of destabilizing PMM2 mutations through pharmacochaperones. Despite the broad exploration of glycosylation pathways and therapeutic strategies, none of the presented abstracts provide evidence for a functional role of ACTL10 in these processes. Consequently, while these papers significantly advance our understanding of PMM2-related glycosylation disorders, they do not address or elucidate any function for ACTL10."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Christian Thiel, Torben Lübke, Gert Matthijs, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Targeted disruption of the mouse phosphomannomutase 2 gene causes early embryonic lethality."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.02391-05"}], "href": "https://doi.org/10.1128/MCB.02391-05"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16847317"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16847317"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Barden Chan, Michelle Clasquin, Gromoslaw A Smolen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A mouse model of a human congenital disorder of glycosylation caused by loss of PMM2."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hum Mol Genet (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/hmg/ddw085"}], "href": "https://doi.org/10.1093/hmg/ddw085"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27053713"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27053713"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "K Cromphout, L Keldermans, A Snellinx, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Tissue distribution of the murine phosphomannomutases Pmm1 and Pmm2 during brain development."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Eur J Neurosci (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/j.1460-9568.2005.04266.x"}], "href": "https://doi.org/10.1111/j.1460-9568.2005.04266.x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16115222"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16115222"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Mecedes Cano, Anunciación A Ilundain "}, {"type": "b", "children": [{"type": "t", "text": "Ontogeny of D-mannose transport and metabolism in rat small intestine."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Membr Biol (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s00232-010-9259-0"}], "href": "https://doi.org/10.1007/s00232-010-9259-0"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20523973"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20523973"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Cristina Segovia-Falquina, Alicia Vilas, Fátima Leal, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A functional platform for the selection of pathogenic variants of PMM2 amenable to rescue via the use of pharmacological chaperones."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hum Mutat (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/humu.24431"}], "href": "https://doi.org/10.1002/humu.24431"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35789514"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35789514"}]}]}]}