{"id":45304,"date":"2025-07-29T14:49:14","date_gmt":"2025-07-29T14:49:14","guid":{"rendered":"https:\/\/www.newsbeep.com\/us\/45304\/"},"modified":"2025-07-29T14:49:14","modified_gmt":"2025-07-29T14:49:14","slug":"ngly1-deficiency-clinical-features-and-therapeutic-strategy","status":"publish","type":"post","link":"https:\/\/www.newsbeep.com\/us\/45304\/","title":{"rendered":"NGLY1 deficiency – clinical features and therapeutic strategy"},"content":{"rendered":"

Suzuki T. Catabolism of N-glycoproteins in mammalian cells: molecular mechanisms and genetic disorders related to the processes. Mol Asp Med. 2016;51:89\u2013103.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Lehrbach NJ, Breen PC, Ruvkun G. Protein sequence editing of SKN-1A\/Nrf1 by peptide:N-glycanase controls proteasome gene expression. Cell. 2019;177:737\u201350.e15.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Kim HM, Han JW, Chan JY. Nuclear factor erythroid-2 like 1 (NFE2L1): structure, function and regulation. Gene. 2016;584:17\u201325.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Suzuki T, Park H, Hollingsworth NM, Sternglanz R, Lennarz WJ. PNG1, a yeast gene encoding a highly conserved peptide:N-glycanase. J Cell Biol. 2000;149:1039\u201352.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Serafini-Fracassini D, Della Mea M, Parrotta L, Faleri C, Cai G, Del Duca S, et al. AtPng1 knockout mutant of Arabidopsis thaliana shows a juvenile phenotype, morpho-functional changes, altered stress response and cell wall modifications. Plant Physiol Biochem. 2021;167:11\u201321.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Maerz S, Funakoshi Y, Negishi Y, Suzuki T, Seiler S. The Neurospora peptide:N-glycanase ortholog PNG1 is essential for cell polarity despite its lack of enzymatic activity. J Biol Chem. 2010;285:2326\u201332.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Seiler S, Plamann M. The genetic basis of cellular morphogenesis in the filamentous fungus Neurospora crassa. Mol Biol Cell. 2003;14:4352\u201364.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Habibi-Babadi N, Su A, de Carvalho CE, Colavita A. The N-glycanase png-1 acts to limit axon branching during organ formation in Caenorhabditis elegans. J Neurosci. 2010;30:1766\u201376.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Kong J, Peng M, Ostrovsky J, Kwon YJ, Oretsky O, McCormick EM, et al. Mitochondrial function requires NGLY1. Mitochondrion. 2018;38:6\u201316.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Lehrbach NJ, Ruvkun G. Endoplasmic reticulum-associated SKN-1A\/Nrf1 mediates a cytoplasmic unfolded protein response and promotes longevity. Elife. 2019;8:e44425.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Iyer S, Mast JD, Tsang H, Rodriguez TP, DiPrimio N, Prangley M, et al. Drug screens of NGLY1 deficiency in worm and fly models reveal catecholamine, NRF2 and anti-inflammatory-pathway activation as potential clinical approaches. Dis Model Mech. 2019;12:dmm040576.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Lehrbach NJ, Ruvkun G. Proteasome dysfunction triggers activation of SKN-1A\/Nrf1 by the aspartic protease DDI-1. Elife. 2016;5:e17721.<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Yanagi KS, Jochim B, Kunjo SO, Breen P, Ruvkun G, Lehrbach N. Mutations in nucleotide metabolism genes bypass proteasome defects in png-1\/NGLY1-deficient Caenorhabditis elegans. PLoS Biol. 2024;22:e3002720.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Funakoshi Y, Negishi Y, Gergen JP, Seino J, Ishii K, Lennarz WJ, et al. Evidence for an essential deglycosylation-independent activity of PNGase in Drosophila melanogaster. PLoS One. 2010;5:e10545.<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Galeone A, Adams JM, Matsuda S, Presa MF, Pandey A, Han SY, et al. Tissue-specific regulation of BMP signaling by Drosophila N-glycanase 1. Elife. 2017;6:e27612.<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Han SY, Pandey A, Moore T, Galeone A, Duraine L, Cowan TM, et al. A conserved role for AMP-activated protein kinase in NGLY1 deficiency. PLoS Genet. 2020;16:e1009258.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Pandey A, Galeone A, Han SY, Story BA, Consonni G, Mueller WF, et al. Gut barrier defects, intestinal immune hyperactivation and enhanced lipid catabolism drive lethality in NGLY1-deficient Drosophila. Nat Commun. 2023;14:5667.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Galeone A, Adams JM, Matsuda S, Presa MF, Pandey A, Han SY, et al. Regulation of BMP4\/Dpp retrotranslocation and signaling by deglycosylation. Elife. 2020;9:e55596.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Pandey A, Jafar-Nejad H. Tracing the NGLY1 footprints: insights from Drosophila. J Biochem. 2022;171:153\u201360.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Fujihira H, Masahara-Negishi Y, Tamura M, Huang C, Harada Y, Wakana S, et al. Lethality of mice bearing a knockout of the Ngly1-gene is partially rescued by the additional deletion of the Engase gene. PLoS Genet. 2017;13:e1006696.<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Asahina M, Fujinawa R, Fujihira H, Masahara-Negishi Y, Andou T, Tozawa R, et al. JF1\/B6F1 Ngly1(-\/-) mouse as an isogenic animal model of NGLY1 deficiency. Proc Jpn Acad Ser B Phys Biol Sci. 2021;97:89\u2013102.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Need AC, Shashi V, Hitomi Y, Schoch K, Shianna KV, McDonald MT, et al. Clinical application of exome sequencing in undiagnosed genetic conditions. J Med Genet. 2012;49:353\u201361.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Abuduxikuer K, Zou L, Wang L, Chen L, Wang JS. Novel NGLY1 gene variants in Chinese children with global developmental delay, microcephaly, hypotonia, hypertransaminasemia, alacrimia, and feeding difficulty. J Hum Genet. 2020;65:387\u201396.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Bosch DG, Boonstra FN, de Leeuw N, Pfundt R, Nillesen WM, de Ligt J, et al. Novel genetic causes for cerebral visual impairment. Eur J Hum Genet. 2016;24:660\u20135.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Caglayan AO, Comu S, Baranoski JF, Parman Y, Kaymak\u00e7alan H, Akgumus GT, et al. NGLY1 mutation causes neuromotor impairment, intellectual disability, and neuropathy. Eur J Med Genet. 2015;58:39\u201343.<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Chang CA, Wei XC, Martin SR, Sinasac DS, Al-Hertani W. Transiently elevated plasma methionine, S-adenosylmethionine and S-adenosylhomocysteine: unreported laboratory findings in a patient with NGLY1 deficiency, a congenital disorder of deglycosylation. JIMD Rep. 2019;49:21\u201329.<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Dabaj I, Sudri\u00e9-Arnaud B, Lecoquierre F, Raymond K, Ducatez F, Guerrot AM, et al. NGLY1 deficiency: a rare newly described condition with a typical presentation. Life. 2021;11:187.<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Enns GM, Shashi V, Bainbridge M, Gambello MJ, Zahir FR, Bast T, et al. Mutations in NGLY1 cause an inherited disorder of the endoplasmic reticulum-associated degradation pathway. Genet Med. 2014;16:751\u20138.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Frater CH, Ruzhnikov M, Beres S, Alcorn D, Shue A, Levy RJ. Ocular features of NGLY1 deficiency from a prospective longitudinal cohort. J AAPOS. 2024;28:103925.<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Ge H, Wu Q, Lu H, Huang Y, Zhou T, Tan D, et al. Two novel compound heterozygous mutations in NGLY1as a cause of congenital disorder of deglycosylation: a case presentation. BMC Med Genet. 2020;21:135.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Heeley J, Shinawi M. Multi-systemic involvement in NGLY1-related disorder caused by two novel mutations. Am J Med Genet A. 2015;167A:816\u201320.<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Kalfon L, Baydany M, Samra N, Heno N, Segal Z, Eran A, et al. Congenital hypotonia: cracking a SAGA of consanguineous kindred harboring four genetic variants. Mol Genet Genom Med. 2022;10:e1849.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Kariminejad A, Shakiba M, Shams M, Namiranian P, Eghbali M, Talebi S, et al. NGLY1 deficiency: novel variants and literature review. Eur J Med Genet. 2021;64:104146.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Lam C, Ferreira C, Krasnewich D, Toro C, Latham L, Zein WM, et al. Prospective phenotyping of NGLY1-CDDG, the first congenital disorder of deglycosylation. Genet Med. 2017;19:160\u20138.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Levy RJ, Frater CH, Gallentine WB, Phillips JM, Ruzhnikov MR. Delineating the epilepsy phenotype of NGLY1 deficiency. J Inherit Metab Dis. 2022;45:571\u201383.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Lipari Pinto P, Machado C, Janeiro P, Dupont J, Quintas S, Sousa AB, et al. NGLY1 deficiency-A rare congenital disorder of deglycosylation. JIMD Rep. 2020;53:2\u20139.<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Lipi\u0144ski P, Bogda\u0144ska A, R\u00f3\u017cd\u017cy\u0144ska-\u015awi\u0105tkowska A, Wierzbicka-Ruci\u0144ska A, Tylki-Szyma\u0144ska A. NGLY1 deficiency: Novel patient, review of the literature and diagnostic algorithm. JIMD Rep. 2020;51:82\u201388.<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Lipi\u0144ski P, Bogda\u0144ska A, Socha P, Tylki-Szyma\u0144ska A. Liver involvement in congenital disorders of glycosylation and deglycosylation. Front Pediatr. 2021;9:696918.<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Lipi\u0144ski P, Cielecka-Kuszyk J, Socha P, Tylki-Szyma\u0144ska A. Liver involvement in NGLY1 congenital disorder of deglycosylation. Pol J Pathol. 2020;71:66\u201368.<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Nolan DK, Pastore MT, McBride KL. Expanding the NGLY1 deficiency phenotype: case report of an atypical patient. Eur J Med Genet. 2022;65:104558.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Pandey A, Adams JM, Han SY, Jafar-Nejad H. NGLY1 deficiency, a congenital disorder of deglycosylation: from disease gene function to pathophysiology. Cells. 2022;11:1155.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Panneman DM, Wortmann SB, Haaxma CA, van Hasselt PM, Wolf NI, Hendriks Y, et al. Variants in NGLY1 lead to intellectual disability, myoclonus epilepsy, sensorimotor axonal polyneuropathy and mitochondrial dysfunction. Clin Genet. 2020;97:556\u201366.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Rios-Flores IM, Bonal-P\u00e9rez M\u00c1, Castellanos-Gonz\u00e1lez A, Velez-G\u00f3mez E, Bertoli-Avella AM, Bobadilla-Morales L, et al. Acute liver failure in a male patient with NGLY1-congenital disorder of deglycosylation. Eur J Med Genet. 2020;63:103952.<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Sonoda Y, Fujita A, Torio M, Mukaino T, Sakata A, Matsukura M, et al. Progressive myoclonic epilepsy as an expanding phenotype of NGLY1-associated congenital deglycosylation disorder: a case report and review of the literature. Eur J Med Genet. 2024;67:104895.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Stanclift CR, Dwight SS, Lee K, Eijkenboom QL, Wilsey M, Wilsey K, et al. NGLY1 deficiency: estimated incidence, clinical features, and genotypic spectrum from the NGLY1 Registry. Orphanet J Rare Dis. 2022;17:440.<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Stuut T, Popescu O, Oviedo A. N-Glycanase 1 deficiency is a rare cause of pediatric neurodegeneration with neuronal inclusions and liver steatosis. Cureus. 2021;13:e19126.<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Tong S, Ventola P, Frater CH, Klotz J, Phillips JM, Muppidi S, et al. NGLY1 deficiency: a prospective natural history study. Hum Mol Genet. 2023;32:2787\u201396.<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Ullah A, Shah AA, Alluqmani M, Haider N, Aman H, Alfadhli F, et al. Clinical and genetic characterization of patients segregating variants in KPTN, MINPP1, NGLY1, AP4B1, and SON underlying neurodevelopmental disorders: genetic and phenotypic expansion. Int J Dev Neurosci. 2022;82:789\u2013805.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

van Keulen BJ, Rotteveel J, Finken MJJ. Unexplained death in patients with NGLY1 mutations may be explained by adrenal insufficiency. Physiol Rep. 2019;7:e13979.<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Zidoune H, Martinerie L, Tan DS, Askari M, Rezgoune D, Ladjouze A, et al. Expanding DSD phenotypes associated with variants in the DEAH-Box RNA helicase DHX37. Sex Dev. 2021;15:244\u201352.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Hirayama H, Tachida Y, Seino J, Suzuki T. A method for assaying peptide: N-glycanase\/N-glycanase 1 activities in crude extracts using an N-glycosylated cyclopeptide. Glycobiology. 2022;32:110\u201322.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Fujihira H, Sato K, Nishiuchi Y, Murase T, Matsuda Y, Yoshida Y, et al. ELISA-based highly sensitive assay system for the detection of endogenous NGLY1 activity. Biochem Biophys Res Commun. 2024;710:149826.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Achouitar S, Mohamed M, Gardeitchik T, Wortmann SB, Sykut-Cegielska J, Ensenauer R, et al. Nijmegen paediatric CDG rating scale: a novel tool to assess disease progression. J Inherit Metab Dis. 2011;34:923\u20137.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Melnyk S, Pogribna M, Pogribny IP, Yi P, James SJ. Measurement of plasma and intracellular S-adenosylmethionine and S-adenosylhomocysteine utilizing coulometric electrochemical detection: alterations with plasma homocysteine and pyridoxal 5\u2019-phosphate concentrations. Clin Chem. 2000;46:265\u201372.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Asahina M, Fujinawa R, Hirayama H, Tozawa R, Kajii Y, Suzuki T. Reversibility of motor dysfunction in the rat model of NGLY1 deficiency. Mol Brain. 2021;14:91.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Zhu L, Tan B, Dwight SS, Beahm B, Wilsey M, Crawford BE, et al. AAV9-NGLY1 gene replacement therapy improves phenotypic and biomarker endpoints in a rat model of NGLY1 Deficiency. Mol Ther Methods Clin Dev. 2022;27:259\u201371.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Du A, Yang K, Zhou X, Ren L, Liu N, Zhou C, et al. Systemic gene therapy corrects neurological phenotype in a mouse model of NGLY1 deficiency. JCI Insight. 2024;9:e183189.<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Chan KY, Jang MJ, Yoo BB, Greenbaum A, Ravi N, Wu WL, et al. Engineered AAVs for efficient noninvasive gene delivery to the central and peripheral nervous systems. Nat Neurosci. 2017;20:1172\u20139.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Froemke RC, Young LJ. Oxytocin, neural plasticity, and social behavior. Annu Rev Neurosci. 2021;44:359\u201381.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Makita Y, Asahina M, Fujinawa R, Yukitake H, Suzuki T. Intranasal oxytocin suppresses seizure-like behaviors in a mouse model of NGLY1 deficiency. Commun Biol. 2024;7:460.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Hope KA, Berman AR, Peterson RT, Chow CY. An in vivo drug repurposing screen and transcriptional analyses reveals the serotonin pathway and GSK3 as major therapeutic targets for NGLY1 deficiency. PLoS Genet. 2022;18:e1010228.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Rodriguez TP, Mast JD, Hartl T, Lee T, Sand P, Perlstein EO. Defects in the neuroendocrine axis contribute to global development delay in a drosophila model of NGLY1 deficiency. G3 Bethesda. 2018;8:2193\u2013204.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Yoshida Y, Asahina M, Murakami A, Kawawaki J, Yoshida M, Fujinawa R, et al. Loss of peptide:N-glycanase causes proteasome dysfunction mediated by a sugar-recognizing ubiquitin ligase. Proc Natl Acad Sci USA. 2021;118:e2102902118.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Satoh T, Yagi-Utsumi M, Ishii N, Mizushima T, Yagi H, Kato R, et al. Structural basis of sugar recognition by SCF(FBS2) ubiquitin ligase involved in NGLY1 deficiency. FEBS Lett. 2024;598:2259\u201368.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Yoshida Y, Tokunaga F, Chiba T, Iwai K, Tanaka K, Tai T. Fbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chains. J Biol Chem. 2003;278:43877\u201384.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Yoshida Y, Takahashi T, Ishii N, Matsuo I, Takahashi S, Inoue H, et al. Sugar-mediated non-canonical ubiquitination impairs Nrf1\/NFE2L1 activation. Mol Cell. 2024;84:3115\u201327.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n

Haijes HA, de Sain-van der Velden M, Prinsen H, Willems AP, van der Ham M, Gerrits J, et al. Aspartylglycosamine is a biomarker for NGLY1-CDDG, a congenital disorder of deglycosylation. Mol Genet Metab. 2019;127:368\u201372.<\/p>\n

CAS<\/a>\u00a0
\n
\n Google Scholar<\/a>\u00a0\n <\/p>\n","protected":false},"excerpt":{"rendered":"Suzuki T. Catabolism of N-glycoproteins in mammalian cells: molecular mechanisms and genetic disorders related to the processes. Mol…\n","protected":false},"author":2,"featured_media":45305,"comment_status":"","ping_status":"","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[50],"tags":[35864,8006,3872,13113,13056,200,3870,8872,79],"class_list":{"0":"post-45304","1":"post","2":"type-post","3":"status-publish","4":"format-standard","5":"has-post-thumbnail","7":"category-genetics","8":"tag-chemical-biology","9":"tag-diseases","10":"tag-gene-expression","11":"tag-gene-function","12":"tag-gene-therapy","13":"tag-genetics","14":"tag-human-genetics","15":"tag-molecular-medicine","16":"tag-science"},"_links":{"self":[{"href":"https:\/\/www.newsbeep.com\/us\/wp-json\/wp\/v2\/posts\/45304","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www.newsbeep.com\/us\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/www.newsbeep.com\/us\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/www.newsbeep.com\/us\/wp-json\/wp\/v2\/users\/2"}],"replies":[{"embeddable":true,"href":"https:\/\/www.newsbeep.com\/us\/wp-json\/wp\/v2\/comments?post=45304"}],"version-history":[{"count":0,"href":"https:\/\/www.newsbeep.com\/us\/wp-json\/wp\/v2\/posts\/45304\/revisions"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/www.newsbeep.com\/us\/wp-json\/wp\/v2\/media\/45305"}],"wp:attachment":[{"href":"https:\/\/www.newsbeep.com\/us\/wp-json\/wp\/v2\/media?parent=45304"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/www.newsbeep.com\/us\/wp-json\/wp\/v2\/categories?post=45304"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/www.newsbeep.com\/us\/wp-json\/wp\/v2\/tags?post=45304"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}