{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,1]],"date-time":"2026-04-01T11:08:48Z","timestamp":1775041728627,"version":"3.50.1"},"reference-count":63,"publisher":"Oxford University Press (OUP)","issue":"2","license":[{"start":{"date-parts":[[2021,11,18]],"date-time":"2021-11-18T00:00:00Z","timestamp":1637193600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"funder":[{"name":"MEXT\/JSPS KAKENHI","award":["JP18H03990"],"award-info":[{"award-number":["JP18H03990"]}]},{"name":"AMED-CREST","award":["JP21gm14100003"],"award-info":[{"award-number":["JP21gm14100003"]}]},{"name":"RIKEN Pioneering Research Project"},{"name":"T-CiRA project"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2022,2,21]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Cytosolic peptide:N-glycanase (NGLY1 in mammals), a highly conserved enzyme in eukaryotes, catalyses the deglycosylation of N-glycans that are attached to glycopeptide\/glycoproteins. In 2012, an autosomal recessive disorder related to the NGLY1 gene, which was referred to as NGLY1 deficiency, was reported. Since then, more than 100 patients have been identified. Patients with this disease exhibit various symptoms, including various motor deficits and other neurological problems. Effective therapeutic treatments for this disease, however, have not been established. Most recently, it was demonstrated that the intracerebroventricular administration of an adeno-associated virus 9 vector expressing human NGLY1 during the weaning period allowed some motor functions to be recovered in Ngly1\u2212\/\u2212 rats. This observation led us to hypothesize that a therapeutic intervention for improving these motor deficits or other neurological symptoms found in the patients might be possible. To achieve this, it is critical to establish robust and facile methods for assaying NGLY1 activity in biological samples, for the early diagnosis and evaluation of the therapeutic efficacy for the treatment of NGLY1 deficiency. In this mini review, we summarize progress made in the development of various assay methods for NGLY1 activity, as well as a recent progress in the identification of NGLY1 deficiency-specific biomarkers.<\/jats:p>","DOI":"10.1093\/jb\/mvab127","type":"journal-article","created":{"date-parts":[[2021,11,17]],"date-time":"2021-11-17T12:12:11Z","timestamp":1637151131000},"page":"169-176","source":"Crossref","is-referenced-by-count":11,"title":["Assay for the peptide:<i>N<\/i>-glycanase\/NGLY1 and disease-specific biomarkers for diagnosing NGLY1 deficiency"],"prefix":"10.1093","volume":"171","author":[{"given":"Hiroto","family":"Hirayama","sequence":"first","affiliation":[{"name":"Glycometabolic Biochemistry Laboratory, RIKEN Cluster for Pioneering Research, RIKEN, 2-1 Hirosawa, Wako Saitama 351-0198, Japan"},{"name":"Takeda-CiRA Joint Program, 2-26-1 Muraokahigashi, Fujisawa Kanagawa 251-8555, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tadashi","family":"Suzuki","sequence":"additional","affiliation":[{"name":"Glycometabolic Biochemistry Laboratory, RIKEN Cluster for Pioneering Research, RIKEN, 2-1 Hirosawa, Wako Saitama 351-0198, Japan"},{"name":"Takeda-CiRA Joint Program, 2-26-1 Muraokahigashi, Fujisawa Kanagawa 251-8555, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2021,11,18]]},"reference":[{"key":"2022030107593794200_ref1","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1096\/fj.01-0889rev","article-title":"Cytoplasmic peptide:N-glycanase (PNGase) in eukaryotic cells: occurrence, primary structure, and potential functions","volume":"16","author":"Suzuki","year":"2002","journal-title":"FASEB J."},{"key":"2022030107593794200_ref2","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1080\/09168451.2015.1072464","article-title":"Lack of the evidence for the enzymatic catabolism of Man1GlcNAc2 in Saccharomyces cerevisiae","volume":"80","author":"Hossain","year":"2015","journal-title":"Biosci. 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