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2019 8
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Impaired catabolism of free oligosaccharides due to MAN2C1 variants causes a neurodevelopmental disorder.
Maia N, Potelle S, Yildirim H, Duvet S, Akula SK, Schulz C, Wiame E, Gheldof A, O'Kane K, Lai A, Sermon K, Proisy M, Loget P, Attié-Bitach T, Quelin C, Fortuna AM, Soares AR, de Brouwer APM, Van Schaftingen E, Nassogne MC, Walsh CA, Stouffs K, Jorge P, Jansen AC, Foulquier F. Maia N, et al. Am J Hum Genet. 2022 Feb 3;109(2):345-360. doi: 10.1016/j.ajhg.2021.12.010. Epub 2022 Jan 18. Am J Hum Genet. 2022. PMID: 35045343 Free PMC article.
Although little is known about fOS metabolism, the recent identification of NGLY1 deficiency, a congenital disorder of deglycosylation (CDDG) caused by loss of function of an enzyme involved in fOS metabolism, has elicited increased interest in fOS processing. ...
Although little is known about fOS metabolism, the recent identification of NGLY1 deficiency, a congenital disorder of deglycosylatio …
Ferroptosis regulation by the NGLY1/NFE2L1 pathway.
Forcina GC, Pope L, Murray M, Dong W, Abu-Remaileh M, Bertozzi CR, Dixon SJ. Forcina GC, et al. Proc Natl Acad Sci U S A. 2022 Mar 15;119(11):e2118646119. doi: 10.1073/pnas.2118646119. Epub 2022 Mar 10. Proc Natl Acad Sci U S A. 2022. PMID: 35271393 Free PMC article.
Ever-expanding NGLY1 biology.
Suzuki T, Yoshida Y. Suzuki T, et al. J Biochem. 2022 Feb 21;171(2):141-143. doi: 10.1093/jb/mvab134. J Biochem. 2022. PMID: 34969094
The cytosolic peptide:N-glycanase (PNGase; NGLY1 in humans) is a deglycosylating enzyme that is widely conserved in eukaryotes. ...Diverse biological processes have also been found to be affected by compromised NGLY1 activity. In this special is …
The cytosolic peptide:N-glycanase (PNGase; NGLY1 in humans) is a deglycosylating enzyme that is widely conserved …
NGLY1 mutations cause protein aggregation in human neurons.
Manole A, Wong T, Rhee A, Novak S, Chin SM, Tsimring K, Paucar A, Williams A, Newmeyer TF, Schafer ST, Rosh I, Kaushik S, Hoffman R, Chen S, Wang G, Snyder M, Cuervo AM, Andrade L, Manor U, Lee K, Jones JR, Stern S, Marchetto MC, Gage FH. Manole A, et al. Cell Rep. 2023 Dec 26;42(12):113466. doi: 10.1016/j.celrep.2023.113466. Epub 2023 Nov 30. Cell Rep. 2023. PMID: 38039131 Free PMC article.
Biallelic mutations in the gene that encodes the enzyme N-glycanase 1 (NGLY1) cause a rare disease with multi-symptomatic features including developmental delay, intellectual disability, neuropathy, and seizures. ...To understand how NGLY1 gene …
Biallelic mutations in the gene that encodes the enzyme N-glycanase 1 (NGLY1) cause a rare disease with multi-sy …
Loss of peptide:N-glycanase causes proteasome dysfunction mediated by a sugar-recognizing ubiquitin ligase.
Yoshida Y, Asahina M, Murakami A, Kawawaki J, Yoshida M, Fujinawa R, Iwai K, Tozawa R, Matsuda N, Tanaka K, Suzuki T. Yoshida Y, et al. Proc Natl Acad Sci U S A. 2021 Jul 6;118(27):e2102902118. doi: 10.1073/pnas.2102902118. Proc Natl Acad Sci U S A. 2021. PMID: 34215698 Free PMC article.
Mutations in the human peptide:N-glycanase gene (NGLY1), which encodes a cytosolic de-N-glycosylating enzyme, cause a congenital autosomal recessive disorder. In rodents, the loss of Ngly1 results in severe developmental delay or lethality, but the und …
Mutations in the human peptide:N-glycanase gene (NGLY1), which encodes a cytosolic de-N-glycosylating enzyme, cause a c …
Coupled deglycosylation-ubiquitination cascade in regulating PD-1 degradation by MDM2.
Wu Z, Cao Z, Yao H, Yan X, Xu W, Zhang M, Jiao Z, Zhang Z, Chen J, Liu Y, Zhang M, Wang D. Wu Z, et al. Cell Rep. 2023 Jul 25;42(7):112693. doi: 10.1016/j.celrep.2023.112693. Epub 2023 Jun 27. Cell Rep. 2023. PMID: 37379210 Free article.
In addition, the presence of MDM2 facilitates glycosylated PD-1 interaction with glycosidase NGLY1 and promotes subsequent NGLY1-catalyzed PD-1 deglycosylation. ...
In addition, the presence of MDM2 facilitates glycosylated PD-1 interaction with glycosidase NGLY1 and promotes subsequent NGLY1 …
NGLY1 Deficiency, a Congenital Disorder of Deglycosylation: From Disease Gene Function to Pathophysiology.
Pandey A, Adams JM, Han SY, Jafar-Nejad H. Pandey A, et al. Cells. 2022 Mar 29;11(7):1155. doi: 10.3390/cells11071155. Cells. 2022. PMID: 35406718 Free PMC article. Review.
N-Glycanase 1 (NGLY1) is a cytosolic enzyme involved in removing N-linked glycans of misfolded N-glycoproteins and is considered to be a component of endoplasmic reticulum-associated degradation (ERAD). The 2012 identification of recessive NGLY1 …
N-Glycanase 1 (NGLY1) is a cytosolic enzyme involved in removing N-linked glycans of misfolded N-glycoproteins a …
NGLY1 deficiency: estimated incidence, clinical features, and genotypic spectrum from the NGLY1 Registry.
Stanclift CR, Dwight SS, Lee K, Eijkenboom QL, Wilsey M, Wilsey K, Kobayashi ES, Tong S, Bainbridge MN. Stanclift CR, et al. Orphanet J Rare Dis. 2022 Dec 17;17(1):440. doi: 10.1186/s13023-022-02592-3. Orphanet J Rare Dis. 2022. PMID: 36528660 Free PMC article.
PURPOSE: NGLY1 Deficiency is an ultra-rare, multisystemic disease caused by biallelic pathogenic NGLY1 variants. ...We analyzed NGLY1 variants and clinical features and estimated NGLY1 disease incidence in the United States (U.S.). ...
PURPOSE: NGLY1 Deficiency is an ultra-rare, multisystemic disease caused by biallelic pathogenic NGLY1 variants. ...We analyze …
Comparative proteomics reveals elevated CCN2 in NGLY1-deficient cells.
Hetz R, Magaway C, Everett J, Li L, Willard BB, Freeze HH, He P. Hetz R, et al. Biochem Biophys Res Commun. 2022 Dec 3;632:165-172. doi: 10.1016/j.bbrc.2022.09.100. Epub 2022 Oct 2. Biochem Biophys Res Commun. 2022. PMID: 36209585 Free PMC article.
N-glycanase 1(NGLY1) catalyzes the removal of N-linked glycans from newly synthesized or misfolded protein. ...CCN2 was selected for further analysis due to its significant increase in different cell models of NGLY1 deficiency. Functional assays …
N-glycanase 1(NGLY1) catalyzes the removal of N-linked glycans from newly synthesized or misfolded protein. ...C …
N-Glycanase 1 Transcriptionally Regulates Aquaporins Independent of Its Enzymatic Activity.
Tambe MA, Ng BG, Freeze HH. Tambe MA, et al. Cell Rep. 2019 Dec 24;29(13):4620-4631.e4. doi: 10.1016/j.celrep.2019.11.097. Cell Rep. 2019. PMID: 31875565 Free article.
We demonstrate that Ngly1-null mouse embryonic fibroblasts, NGLY1 knockout human cells, and patient fibroblasts are resistant to hypotonic lysis. ...Ngly1 knockdown and overexpression confirms that Ngly1 regulates aquaporin1 and hypotonic cell lysis. . …
We demonstrate that Ngly1-null mouse embryonic fibroblasts, NGLY1 knockout human cells, and patient fibroblasts are resistant …
50 results