Reference on EC 2.7.8.15 - UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gheesling Mullis, K.; Huynh, M.; Kornfeld, R.H.
Purification and kinetic parameters of bovine liver N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
J. Biol. Chem.
269
1718-1726
1994
Bos taurus
Pohlmann, R.; Waheed, A.; Hasilik, A.; von Figura, K.
Synthesis of phosphorylated recognition marker in lysosomal enzymes is located in the cis part of Golgi apparatus
J. Biol. Chem.
257
5323-5325
1982
Rattus
Hiller, A.M.; Koro, L.A.; Marchase, R.B.
Glucose-1-phosphotransferase and N-acetylglucosamine-1-phosphotransferase have distinct acceptor specificities
J. Biol. Chem.
262
4377-4381
1987
Homo sapiens
Ikeda, M.; Wachi, M.; Jung, H.K.; Ishino, F.; Matsuhashi, M.
The Escherichia coli mraY gene encoding UDP-N-acetylmuramoyl-pentapeptide: undecaprenyl-phosphate phospho-N-acetylmuramoyl-pentapeptide transferase
J. Bacteriol.
173
1021-1026
1991
Saccharomyces cerevisiae, Escherichia coli
Sharma, C.B.; Lehle, L.; Tanner, W.
Solubilization and characterization of the initial enzymes of the dolichol pathway from yeast
Eur. J. Biochem.
126
319-325
1982
Saccharomyces cerevisiae, Saccharomyces cerevisiae X2180-1A
Villemez, C.L.; Carlo, P.L.
Properties of a soluble polyprenyl phosphate. UDP-D-N-acetylglucosamine N-acetylglucosamine-1-phosphate transferase
J. Biol. Chem.
255
8174-8178
1980
Acanthamoeba castellanii
Shailubhai, K.; Dong-Yu, B.; Saxena, E.S.; Vijay, I.K.
Purification and characterization of UDP-N-acetyl-D-glucosamine:dolichol phosphate N-acetyl-D-glucosamine-1-phosphate transferase involved in the biosynthesis of asparagine-linked glycoproteins in the mammary gland
J. Biol. Chem.
263
15964-15972
1988
Bos taurus
Kaushal, G.P.; Elbein, A.D.
Purification and properties of UDP-GlcNAc:dolichyl-phosphate GlcNAc-1-phosphate transferase. Activation and inhibition of the enzyme
J. Biol. Chem.
260
16303-16309
1985
Sus scrofa
Plouhar, P.L.; Bretthauer, R.K.
A phospholipid requirement for dolichol pyrophosphate N-acetylglucosamine synthesis in phospholipase A2-treated rat lung microsomes
J. Biol. Chem.
257
8907-8911
1982
BRENDA: Rattus norvegicus
Textmining: Rattus, Bos taurus
Heifetz, A.; Keenan, R.W.; Elbein, A.D.
Mechanism of action of tunicamycin on the UDP-GlcNAc:dolichyl-phosphate Glc-NAc-1-phosphate transferase
Biochemistry
18
2186-2192
1979
Sus scrofa
Kaushal, G.P.; Elbein, A.D.
Properties of solubilized UDP-GlcNAc:dolichyl phosphate-GlcNAc-1-P-transferase from soybean cultured cells
Plant Physiol.
82
748-752
1986
Glycine max
Chandra, N.C.; Doody, M.B.; Bretthauer, R.K.
Specific lipids enhance the activity of UDP-GlcNAc: dolichol phosphate GlcNAc-1-phosphate transferase in rat liver endoplasmic reticulum membrane vesicles
Arch. Biochem. Biophys.
290
345-354
1991
Rattus norvegicus
Zeng, Y.; Elbein, A.D.
UDP-N-acetylglucosamine:dolichyl-phosphate N-acetylglucosamine-1-phosphate transferase is amplified in tunicamycin-resistant soybean cells
Eur. J. Biochem.
233
458-466
1995
Glycine max
Sorensen, T.K.; Dyer, P.S.; Fierro, F.; Laube, U.; Peberdy, J.F.
Characterisation of the gptA gene, encoding UDP N-acetylglucosamine: dolichol phosphate N-acetylglucosaminylphosphoryl transferase, from the filamentous fungus, Aspergillus niger
Biochim. Biophys. Acta
1619
89-97
2003
Aspergillus niger, Aspergillus niger N402
Kukuruzinska, M.A.; Lennon, K.
Diminished activity of the first N-glycosylation enzyme, dolichol-P-dependent N-acetylglucosamine-1-P transferase (GPT), gives rise to mutant phenotypes in yeast
Biochim. Biophys. Acta
1247
51-59
1995
BRENDA: Saccharomyces cerevisiae
Textmining: Xenopus
Mota, O.M.; Huang, G.T.; Kukuruzinska, M.A.
Developmental regulation and tissue-specific expression of hamster dolichol-P-dependent N-acetylglucosamine-1-P transferase (GPT)
Biochem. Biophys. Res. Commun.
204
284-291
1994
BRENDA: Cricetulus griseus
Textmining: eukaryota
Huang, G.T.; Lennon, K.; Kukuruzinska, M.A.
Characterization of multiple transcripts of the hamster dolichol-P-dependent N-acetylglucosamine-1-P transferase suggests functionally complex expression
Mol. Cell. Biochem.
181
97-106
1998
BRENDA: Cricetulus griseus
Textmining: Saccharomyces cerevisiae
Scocca, J.R.; Krag, S.S.
Aspartic acid 252 and asparagine 185 are essential for activity of lipid N-acetylglucosaminylphosphate transferase
Glycobiology
7
1181-1191
1997
BRENDA: Cricetulus griseus
Textmining: Schizosaccharomyces pombe
Wu, X.; Rush, J.S.; Karaoglu, D.; Krasnewich, D.; Lubinsky, M.S.; Waechter, C.J.; Gilmore, R.; Freeze, H.H.
Deficiency of UDP-GlcNAc: dolichol phosphate N-acetylglucosamine-1 phosphate transferase (DPAGT1) causes a novel congenital disorder of glycosylation type Ij
Hum. Mutat.
22
144-150
2003
Homo sapiens
Meissner, J.D.; Naumann, A.; Mueller, W.H.; Scheibe, R.J.
Regulation of UDP-N-acetylglucosamine:dolichyl-phosphate N-acetylglucosamine-1-phosphate transferase by retinoic acid in P19 cells
Biochem. J.
338
561-568
1999
BRENDA: Mus musculus
Textmining: eukaryota
Zara, J.; Lehrman, M.A.
Role of the carboxyl terminus in stable expression of hamster UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase
J. Biol. Chem.
269
19108-19115
1994
Cricetulus griseus
Rajput, B.; Ma, J.; Vijay, I.K.
Structure and organization of mouse GlcNAc-1-phosphate transferase gene
J. Biol. Chem.
269
9590-9597
1994
BRENDA: Mus musculus
Textmining: eukaryota, Saccharomyces cerevisiae, Leishmania
Dan, N.; Middleton, R.B.; Lehrman, M.A.
Hamster UDP-N-acetylglucosamine:dolichol-P N acetylglucosamine-1-P transferase has multiple transmembrane spans and a critical cytosolic loop
J. Biol. Chem.
271
30717-30724
1996
Cricetulus griseus
Dan, N.; Lehrman, M.A.
Oligomerization of hamster UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase, an enzyme with multiple transmembrane spans
J. Biol. Chem.
272
14214-14219
1997
Cricetulus griseus
Waheed, A.; Hasilik, A.; von Figura, K.
UDP-N-acetylglucosamine:lysosomal enzyme precursor N-acetylglucosamine-1-phosphotransferase. Partial purification and characterization of the rat liver Golgi enzyme
J. Biol. Chem.
257
12322-12331
1982
Rattus
Zhao, K.W.; Yeh, R.; Miller, A.L.
Purification and characterization of human lymphoblast N-acetylglucosamine-1-phosphotransferase
Glycobiology
2
119-125
1992
Homo sapiens, Lens culinaris
Bao, M.; Elmendorf, B.J.; Booth, J.L.; Drake, R.R.; Canfield, W.M.
Bovine UDP-N-acetylglucosamine:lysosomal-enzyme N-acetylglucosamine-1-phosphotransferase. II. Enzymatic characterization and identification of the catalytic subunit
J. Biol. Chem.
271
31446-31451
1996
Bos taurus
Bao, M.; Booth, J.L.; Elmendorf, B.J.; Canfield, W.M.
Bovine UDP-N-acetylglucosamine:lysosomal-enzyme N-acetylglucosamine-1-phosphotransferase. I. Purification and subunit structure
J. Biol. Chem.
271
31437-31445
1996
Bos taurus
Mendelsohn, R.D.; Helmerhorst, E.J.; Cipollo, J.F.; Kukuruzinska, M.A.
A hypomorphic allele of the first N-glycosylation gene, ALG7, causes mitochondrial defects in yeast
Biochim. Biophys. Acta
1723
33-44
2005
Saccharomyces cerevisiae
Kudo, M.; Bao, M.; D'Souza, A.; Ying, F.; Pan, H.; Roe, B.A.; Canfield, W.M.
The alpha- and beta-subunits of the human UDP-N-acetylglucosamine:lysosomal enzyme phosphotransferase are encoded by a single cDNA
J. Biol. Chem.
280
36141-36149
2005
Bos taurus
Takahashi, I.; Takahashi, T.; Mikami, T.; Komatsu, M.; Ohura, T.; Schuchman, E.H.; Takada, G.
Acid sphingomyelinase: Relation of 93Lysine residue on the ratio of intracellular to secreted enzyme activity
Tohoku J. Exp. Med.
206
333-340
2005
Homo sapiens
Gao, N.; Shang, J.; Lehrman, M.A.
Unexpected basis for impaired Glc3Man9GlcNAc2-P-P-dolichol biosynthesis by elevated expression of Glcnac-1-p transferase
Glycobiology
18
125-134
2007
Cricetulus griseus, Mesocricetus auratus
Kudo, M.; Canfield, W.M.
Structural requirements for efficient processing and activation of recombinant human UDP-N-acetylglucosamine:lysosomal-enzyme-N-acetylglucosamine-1-phosphotransferase
J. Biol. Chem.
281
11761-11768
2006
Homo sapiens, Homo sapiens (Q3T906), Bos taurus
Salgado, M.; Villagomez-Castro, J.C.; Rocha-Rodriguez, R.; Sabanero-Lopez, M.; Ramos, M.A.; Alagon, A.; Lopez-Romero, E.; Sanchez-Lopez, R.
Entamoeba histolytica: biochemical and molecular insights into the activities within microsomal fractions
Exp. Parasitol.
110
363-373
2005
Entamoeba histolytica, Amoeba
Plante, M.; Claveau, S.; Lepage, P.; Lavoie, E.M.; Brunet, S.; Roquis, D.; Morin, C.; Vezina, H.; Laprise, C.
Mucolipidosis II: a single causal mutation in the N-acetylglucosamine-1-phosphotransferase gene (GNPTAB) in a French Canadian founder population
Clin. Genet.
73
236-244
2008
Homo sapiens
Bretthauer, R.K.
Structure, expression, and regulation of UDP-GlcNAc: dolichol phosphate GlcNAc-1-phosphate transferase (DPAGT1)
Curr. Drug Targets
10
477-482
2009
Bos taurus, Cricetulus griseus, Homo sapiens, Mus musculus, Rattus norvegicus
Cossins, J.; Belaya, K.; Hicks, D.; Salih, M.A.; Finlayson, S.; Carboni, N.; Liu, W.W.; Maxwell, S.; Zoltowska, K.; Farsani, G.T.; Laval, S.; Seidhamed, M.Z.; Seidhamed, M.Z.; Donnelly, P.; Bentley, D.; McGowan, S.J.; Mueller, J.; Palace, J.; Lochmueller, H.; Beeson, D.
Congenital myasthenic syndromes due to mutations in ALG2 and ALG14
Brain
136
944-956
2013
Saccharomyces cerevisiae
Kim, H.S.; Kim, M.S.; Hwang, K.A.; Park, S.W.; Jeon, J.H.
The UDP-N-acetylglucosamine:dolichol phosphate-N-acetylglucosamine-phosphotransferase gene as a new selection marker for potato transformation
Biosci. Biotechnol. Biochem.
77
1589-1592
2013
BRENDA: Solanum tuberosum (G1FCL5), Solanum tuberosum
Textmining: Transformation, Tuber
Xu, L.; Qian, L.; Kang, J.; Sha, S.; Xin, Y.; Lu, S.; Ma, Y.
Down-regulation of N-acetylglucosamine-1-phosphate transferase (WecA) enhanced the sensitivity of Mycobacterium smegmatis against rifampin
J. Appl. Microbiol.
121
966-972
2016
Mycolicibacterium smegmatis, Mycolicibacterium smegmatis (A0R211)
Ko, A.R.; Jin, D.K.; Cho, S.Y.; Park, S.W.; Przybylska, M.; Yew, N.S.; Cheng, S.H.; Kim, J.S.; Kwak, M.J.; Kim, S.J.; Sohn, Y.B.
AAV8-mediated expression of N-acetylglucosamine-1-phosphate transferase attenuates bone loss in a mouse model of mucolipidosis II
Mol. Genet. Metab.
117
447-455
2016
Mus musculus, Mus musculus (Q69ZN6)
Kurosu, M.
Structure-based drug discovery by targeting N-glycan biosynthesis, dolichyl-phosphate N-acetylglucosaminephosphotransferase
Future Med. Chem.
11
927-933
2019
Homo sapiens (Q9H3H5)
Yuste-Checa, P.; Vega, A.I.; Martin-Higueras, C.; Medrano, C.; Gamez, A.; Desviat, L.R.; Ugarte, M.; Perez-Cerda, C.; Perez, B.
DPAGT1-CDG functional analysis of disease-causing pathogenic mutations and role of endoplasmic reticulum stress
PLoS ONE
12
e0179456
2017
Homo sapiens (Q9H3H5), Homo sapiens
Meyer, B.H.; Shams-Eldin, H.; Albers, S.V.
AglH, a thermophilic UDP-N-acetylglucosamine-1-phosphate dolichyl phosphate GlcNAc-1-phosphotransferase initiating protein N-glycosylation pathway in Sulfolobus acidocaldarius, is capable of complementing the eukaryal Alg7
Extremophiles
21
121-134
2017
Sulfolobus acidocaldarius (P39465), Sulfolobus acidocaldarius ATCC 33909 (P39465)
Kanaki, N.; Matsuda, A.; Dejima, K.; Murata, D.; Nomura, K.H.; Ohkura, T.; Gengyo-Ando, K.; Yoshina, S.; Mitani, S.; Nomura, K.
UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase is indispensable for oogenesis, oocyte-to-embryo transition, and larval development of the nematode Caenorhabditis elegans
Glycobiology
29
163-178
2019
BRENDA: Caenorhabditis elegans (Q9U1Z2), Caenorhabditis elegans
Textmining: Nematoda, Homo sapiens, Mus sp., Metazoa
Yoo, J.; Mashalidis, E.H.; Kuk, A.C.Y.; Yamamoto, K.; Kaeser, B.; Ichikawa, S.; Lee, S.Y.
GlcNAc-1-P-transferase-tunicamycin complex structure reveals basis for inhibition of N-glycosylation
Nat. Struct. Mol. Biol.
25
217-224
2018
Homo sapiens (Q9H3H5)
Ohhira, M; Gasa, S; Makita, A; Sekiya, C; Namiki, M
Elevated carbohydrate phosphotransferase activity in human hepatoma and phosphorylation of cathepsin D.
Br J Cancer
63
905-8
1991
Homo sapiens
Boonen, M; Vogel, P; Platt, KA; Dahms, N; Kornfeld, S
Mice lacking mannose 6-phosphate uncovering enzyme activity have a milder phenotype than mice deficient for N-acetylglucosamine-1-phosphotransferase activity.
Mol Biol Cell
20
4381-9
2009
Mus sp.
Criscuolo, BA; Krag, SS
Selection of tunicamycin-resistant Chinese hamster ovary cells with increased N-acetylglucosaminyltransferase activity.
J Cell Biol
94
586-91
1982
Cricetulus griseus
Scocca, JR; Krag, SS
Sequence of a cDNA that specifies the uridine diphosphate N-acetyl-D-glucosamine:dolichol phosphate N-acetylglucosamine-1-phosphate transferase from Chinese hamster ovary cells.
J Biol Chem
265
20621-6
1990
Cricetulus griseus, Saccharomyces cerevisiae
Rajput, B; Ma, J; Muniappa, N; Schantz, L; Naylor, SL; Lalley, PA; Vijay, IK
Mouse UDP-GlcNAc: dolichyl-phosphate N-acetylglucosaminephosphotransferase. Molecular cloning of the cDNA, generation of anti-peptide antibodies and chromosomal localization.
Biochem J
285 ( Pt 3)
985-92
1992
Mus musculus, Saccharomyces cerevisiae, Bos taurus
Liu, X; Chang, KP
The 63-kilobase circular amplicon of tunicamycin-resistant Leishmania amazonensis contains a functional N-acetylglucosamine-1-phosphate transferase gene that can be used as a dominant selectable marker in transfection.
Mol Cell Biol
12
4112-22
1992
Leishmania amazonensis, Leishmania
Uehara, Y; Gasa, S; Makita, A; Sakurada, K; Miyazaki, T
Increased N-acetylglucosamine-1-phosphotransferase activity in sera from patients with leukemia.
Jpn J Cancer Res
82
82-5
1991
Homo sapiens
Madiyalakan, R; Mueller, OT; Shows, TB; Matta, KL
UDP-N-acetylglucosamine: lysosomal enzyme precursor N-acetylglucosamine-1-phosphate transferase activities in human ovarian tumor tissue and some transformed cell lines.
Cancer Invest
5
553-8
1987
Homo sapiens
Lehrman, MA; Zhu, XY; Khounlo, S
Amplification and molecular cloning of the hamster tunicamycin-sensitive N-acetylglucosamine-1-phosphate transferase gene. The hamster and yeast enzymes share a common peptide sequence.
J Biol Chem
263
19796-803
1988
Saccharomyces cerevisiae, eukaryota, Cricetulus griseus
Lang, L; Takahashi, T; Tang, J; Kornfeld, S
Lysosomal enzyme phosphorylation in human fibroblasts. Kinetic parameters offer a biochemical rationale for two distinct defects in the uridine diphospho-N-acetylglucosamine:lysosomal enzyme precursor N-acetylglucosamine-1-phosphotransferase.
J Clin Invest
76
2191-5
1985
Homo sapiens
Waheed, A; Hasilik, A; Cantz, M; von Figura, K
Phosphorylation of lysosomal enzymes in fibroblasts. Marked deficiency of N-acetylglucosamine-1-phosphotransferase in fibroblasts of patients with mucolipidosis III.
Hoppe Seylers Z Physiol Chem
363
169-78
1982
Homo sapiens
Merello, S; Parodi, AJ; Couso, R
Characterization and partial purification of a novel enzymatic activity. UDP-GlcNAc:Ser-protein N-acetylglucosamine-1-phosphotransferase from the cellular slime mold Dictyostelium discoideum.
J Biol Chem
270
7281-7
1995
Dictyostelium, Dictyostelium discoideum
Rajput, B; Muniappa, N; Vijay, IK
Developmental and hormonal regulation of UDP-GlcNAc:dolichol phosphate GlcNAc-1-P transferase in mouse mammary gland.
J Biol Chem
269
16054-61
1994
Mus musculus, Metazoa
Liu, X; Chang, KP
N-acetylglucosamine-1-phosphate transferase gene is conserved in five Leishmania spp. and overexpressed due to its amplification in their tunicamycin-resistant variants.
Mol Biochem Parasitol
59
177-9
1993
Leishmania
Ma, J; Saito, H; Oka, T; Vijay, IK
Negative regulatory element involved in the hormonal regulation of GlcNAc-1-P transferase gene in mouse mammary gland.
J Biol Chem
271
11197-203
1996
Mus musculus
Ma, J; Saito, H; Oka, T; Vijay, IK
Further characterization of negative regulatory element involved in the hormonal regulation of GlcNAc-1-P transferase gene in mouse mammary gland.
Indian J Biochem Biophys
34
110-7
0
Mus musculus
Mehta, DP; Etchison, JR; Wu, R; Freeze, HH
UDP-GlcNAc:Ser-protein N-acetylglucosamine-1-phosphotransferase from Dictyostelium discoideum recognizes serine-containing peptides and eukaryotic cysteine proteinases.
J Biol Chem
272
28638-45
1997
Dictyostelium discoideum
Eckert, V; Blank, M; Mazhari-Tabrizi, R; Mumberg, D; Funk, M; Schwarz, RT
Cloning and functional expression of the human GlcNAc-1-P transferase, the enzyme for the committed step of the dolichol cycle, by heterologous complementation in Saccharomyces cerevisiae.
Glycobiology
8
77-85
1998
Saccharomyces cerevisiae, Homo sapiens, Schizosaccharomyces pombe, Leishmania amazonensis
Stewart, PL
Activity of N-acetylglucosamine-1-phosphate transferase in sheep liver microsomes: in vivo and in vitro inhibition by tunicamycin.
Res Vet Sci
64
31-5
0
Ovis aries, Metazoa
Stewart, PL; May, C; Jago, MV
Reduction and recovery of N-acetylglucosamine-1-phosphate transferase activity in the liver of sheep and rats after a single subcutaneous dose of tunicamycin.
Aust Vet J
76
287-8
1998
Ovis aries, Rattus
Chen, DQ; Lu, H; Chang, KP
Replacement of Leishmania N-acetylglucosamine-1-phosphate transferase gene requires episomal rescue.
Mol Biochem Parasitol
100
223-7
1999
Leishmania
Regis, S; Dagnino, F; Caroli, F; Filocamo, M
Genomic structure of the human UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase gene.
DNA Seq
13
245-50
2002
Homo sapiens, Mus musculus
Paik, KH; Song, SM; Ki, CS; Yu, HW; Kim, JS; Min, KH; Chang, SH; Yoo, EJ; Lee, IJ; Kwan, EK; Han, SJ; Jin, DK
Identification of mutations in the GNPTA (MGC4170) gene coding for GlcNAc-phosphotransferase alpha/beta subunits in Korean patients with mucolipidosis type II or type IIIA.
Hum Mutat
26
308-14
2005
Homo sapiens
Bargal, R; Zeigler, M; Abu-Libdeh, B; Zuri, V; Mandel, H; Ben Neriah, Z; Stewart, F; Elcioglu, N; Hindi, T; Le Merrer, M; Bach, G; Raas-Rothschild, A
When Mucolipidosis III meets Mucolipidosis II: GNPTA gene mutations in 24 patients.
Mol Genet Metab
88
359-63
2006
Homo sapiens, insertion sequences, Meleagris gallopavo
Hajjaran, H; Mohebali, M; Teimouri, A; Oshaghi, MA; Mirjalali, H; Kazemi-Rad, E; Shiee, MR; Naddaf, SR
Identification and phylogenetic relationship of Iranian strains of various Leishmania species isolated from cutaneous and visceral cases of leishmaniasis based on N-acetylglucosamine-1-phosphate transferase gene.
Infect Genet Evol
26
203-12
2014
Canis lupus familiaris, Homo sapiens, Leishmania, Leishmania gerbilli, Leishmania infantum, Leishmania major, Leishmania tropica, Leishmania turanica, Meleagris gallopavo, Rhombomys opimus, Rodentia
Huszár, S; Singh, V; Pol?icová, A; Baráth, P; Barrio, MB; Lagrange, S; Leblanc, V; Nacy, CA; Mizrahi, V; Mikušová, K
N-Acetylglucosamine-1-phosphate transferase, WecA, as a validated drug target in Mycobacterium tuberculosis.
Antimicrob Agents Chemother
2017
Mycobacterium tuberculosis
Ming, SA; Cottman-Thomas, E; Black, NC; Chen, Y; Veeramachineni, V; Peterson, DC; Chen, X; Tedaldi, LM; Wagner, GK; Cai, C; Linhardt, RJ; Vann, WF
Interaction of Neisseria meningitidis Group X N-acetylglucosamine-1-phosphotransferase with its donor substrate.
Glycobiology
28
100-107
2018
Neisseria meningitidis
Saberi, R; Moin-Vaziri, V; Hajjaran, H; Niyyati, M; Taghipour, N; Kheirandish, F; Abadi, A
Identification of Leishmania species using N-acetylglucosamine-1-phosphate transferase gene in a zoonotic cutaneous leishmaniasis focus of Iran.
J Vector Borne Dis
55
14-19
0
Leishmania, Homo sapiens
Ng, BG; Underhill, HR; Palm, L; Bengtson, P; Rozet, JM; Gerber, S; Munnich, A; Zanlonghi, X; Stevens, CA; Kircher, M; Nickerson, DA; Buckingham, KJ; Josephson, KD; Shendure, J; Bamshad, MJ; , ; Freeze, HH; Eklund, EA
DPAGT1 Deficiency with Encephalopathy (DPAGT1-CDG): Clinical and Genetic Description of 11 New Patients.
JIMD Rep
2018
Homo sapiens
Flint, M; Chatterjee, P; Lin, DL; McMullan, LK; Shrivastava-Ranjan, P; Bergeron, É; Lo, MK; Welch, SR; Nichol, ST; Tai, AW; Spiropoulou, CF
A genome-wide CRISPR screen identifies N-acetylglucosamine-1-phosphate transferase as a potential antiviral target for Ebola virus.
Nat Commun
10
285
2019
Ebola virus
Ketcham, CM; Kornfeld, S
Characterization of UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase from Acanthamoeba castellanii.
J Biol Chem
267
11654-9
1992
Acanthamoeba castellanii, Amoeba
Encarnação, M; Lacerda, L; Costa, R; Prata, MJ; Coutinho, MF; Ribeiro, H; Lopes, L; Pineda, M; Ignatius, J; Galvez, H; Mustonen, A; Vieira, P; Lima, MR; Alves, S
Molecular analysis of the GNPTAB and GNPTG genes in 13 patients with mucolipidosis type II or type III - identification of eight novel mutations.
Clin Genet
76
76-84
2009
Homo sapiens
Han, TU; Root, J; Reyes, LD; Huchinson, EB; Hoffmann, JD; Lee, WS; Barnes, TD; Drayna, D
Human GNPTAB stuttering mutations engineered into mice cause vocalization deficits and astrocyte pathology in the corpus callosum.
Proc Natl Acad Sci U S A
116
17515-17524
2019
Homo sapiens, Mus musculus
Chaouch, M; Fathallah-Mili, A; Driss, M; Lahmadi, R; Ayari, C; Guizani, I; Ben Said, M; Benabderrazak, S
Identification of Tunisian Leishmania spp. by PCR amplification of cysteine proteinase B (cpb) genes and phylogenetic analysis.
Acta Trop
125
357-65
2013
Leishmania, Leishmania donovani, Leishmania major, Leishmania tropica, Leishmania infantum, Leishmania killicki
Huo, X; Zhou, X; Peng, P; Yu, M; Zhang, Y; Yang, J; Cao, D; Sun, H; Shen, K
Identification of a Six-Gene Signature for Predicting the Overall Survival of Cervical Cancer Patients.
Onco Targets Ther
14
809-822
2021
Homo sapiens
Detke, S; Chaudhuri, G; Kink, JA; Chang, KP
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Schizosaccharomyces pombe, Cricetulus griseus
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Homo sapiens
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Homo sapiens
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Homo sapiens
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Homo sapiens
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eukaryota
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Homo sapiens
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Homo sapiens, Mus sp.
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Homo sapiens
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Homo sapiens
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Flexor
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Homo sapiens
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2021
Human immunodeficiency virus 1
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