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Attachment of an oligosaccharide to a nitrogen atom
N-linked glycosylation is the attachment of an oligosaccharide, a carbohydrate consisting of several sugar molecules, sometimes also referred to as glycan
N-linked_glycosylation
Biochemical process
bypass glycosylation. Five classes of glycans are produced: N-linked glycans attached to a nitrogen of asparagine or arginine side-chains. N-linked glycosylation
Glycosylation
Biological molecule
post-translational modification glycosylation, specifically N-linked and O-glycosylation. In N-linked glycosylation, it is the first sugar in the chain
N-Acetylglucosamine
Molecular process that occurs within living cells
O-linked glycosylation is the attachment of a sugar molecule to the oxygen atom of serine (Ser) or threonine (Thr) residues in a protein. O-glycosylation
O-linked_glycosylation
Protein-coding gene in the species Homo sapiens
reticulum (ER) that contains an N-terminal thioredoxin-like domain. Functionally, TUSC3 has roles in N-linked glycosylation and ER quality control. It acts
TUSC3
Protein with oligosaccharide modifications
classical secretory glycosylation can be structurally essential. For example, inhibition of asparagine-linked, i.e. N-linked, glycosylation can prevent proper
Glycoprotein
Flattened membrane disk
N-linked glycosylation, which is a crucial process for the proper folding, stability, and function of many secretory and membrane-bound proteins. N-linked
Cisterna
Protein-coding gene in the species Homo sapiens
on PRR32. These include several N-linked glycosylation sites that were predicted with high confidence. Glycosylation is known to play a part in cell-cell
PRR32
Saccharide polymer
N-Linked glycosylation involves oligosaccharide attachment to asparagine via a beta linkage to the amine nitrogen of the side chain. The process of N-linked
Oligosaccharide
Medical condition
increased susceptibility to Epstein–Barr virus (EBV) infection and N-linked glycosylation defect.” The disease is characterized by CD4 lymphopenia, severe
XMEN_disease
Protein-coding gene in the species Homo sapiens
responses, cytoskeletal assembly, and energy metabolism. There are no N-linked glycosylation sites due to the absence of asparagine residues. LOC101928193 has
LOC101928193
Medical condition
to be causing the glycosylation defect in some CDG patients. Also, defects disturbing other glycosylation pathways than the N-linked one are included in
Congenital disorder of glycosylation
Congenital_disorder_of_glycosylation
Protein-coding gene in the species Homo sapiens
"Cloning and expression of N-acetylglucosaminyltransferase I, the medial Golgi transferase that initiates complex N-linked carbohydrate formation". Proc
MGAT1
Chemical compound
backbone.[citation needed] Asparagine also provides key sites for N-linked glycosylation, modification of the protein chain with the addition of carbohydrate
Asparagine
Assembly of proteins inside biological cells
There are broadly two types of glycosylation, N-linked glycosylation and O-linked glycosylation. N-linked glycosylation starts in the endoplasmic reticulum
Protein_biosynthesis
Chemical compound
the first step of glycoprotein synthesis. Tunicamycin blocks N-linked glycosylation (N-glycans) and treatment of cultured human cells with tunicamycin
Tunicamycin
Protein-coding gene in the species Homo sapiens
S2CID 13576808. Dedera DA, Gu RL, Ratner L (1992). "Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function"
MGAT2
Class of enzymes
This sequence is called a glycosylation sequon. The reaction catalyzed by OST is the central step in the N-linked glycosylation pathway. OST is a component
Oligosaccharyltransferase
Class of enzymes
enzyme is isolated from Campylobacter jejuni. It is important for N-linked glycosylation in this species. The glycosyl motif that the enzymes encoded by
N,N'-diacetylbacillosaminyl-diphospho-undecaprenol alpha-1,3-N-acetylgalactosaminyltransferase
N,N'-diacetylbacillosaminyl-diphospho-undecaprenol_alpha-1,3-N-acetylgalactosaminyltransferase
Chemical compound
body. Mannose is present in numerous glycoconjugates including N-linked glycosylation of proteins. C-Mannosylation is also abundant and can be found in
Mannose
Post-translational carbohydrate modification of proteins
O-GlcNAc (short for O-linked GlcNAc or O-linked β-N-acetylglucosamine) is a reversible enzymatic post-translational modification that is found on serine
O-GlcNAc
Protein-coding gene in the species Homo sapiens
synthesis of dolichol-phosphate-mannose, which is essential for N-linked glycosylation and thus the secretion of several glycoproteins as well as for the
PMM1
Protein-coding gene in humans
UDP-N-acetylglucosamine transferase subunit ALG13 homolog, also known as asparagine-linked glycosylation 13 homolog, is an enzyme that in humans is encoded
ALG13
Post-translational modification
asparagine N-linked glycosylation, differing structurally and functionally from the well-established oligomannosidic-, hybrid-, and complex-type N-glycan
Paucimannosylation
Protein-coding gene in humans
catalyzes a key step in endoplasmic reticulum N-linked glycosylation. Congenital disorder of glycosylation GRCh38: Ensembl release 89: ENSG00000172339 –
ALG14
Protein-coding gene in the species Homo sapiens
addition of the second glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation of proteins. Mutations in this gene are associated
ALG8
Class of enzymes
core GlcNAc (N-acetylglucosamine) sugar as in the case of N-linked glycosylation, or to a protein, as in the case of O-linked glycosylation produced by
Fucosyltransferase
Chemical compound
diphosphate (UDP) and N-acetylglucosamine, the enzyme N-acetylglucosamine-1-phosphate transferase catalyzes the N-linked glycosylation of asparagine residues
Mannose_6-phosphate
Chemical changes in proteins following their translation from mRNA
(O-linked), or histidine (N-linked) adenylylation, the addition of an adenylyl moiety, usually to tyrosine (O-linked), or histidine and lysine (N-linked)
Post-translational modification
Post-translational_modification
Glycoprotein exposed on the surface of the HIV virus
variants. Further studies have shown that variability in potential N-linked glycosylation sites (PNGSs) also result in increased viral fitness. PNGSs allow
Envelope_glycoprotein_GP120
Protein-coding gene in humans
(December 2009). "Congenital disorders of glycosylation: an update on defects affecting the biosynthesis of dolichol-linked oligosaccharides" (PDF). Hum. Mutat
DPM3
Cell organelle that processes proteins
fusion event. Initial glycosylation as assembly continues. This is N-linked (O-linking occurs in the Golgi). N-linked glycosylation: If the protein is properly
Endoplasmic_reticulum
Cellular stress response
most important of these to note are N-linked glycosylation and disulfide bond formation. N-linked glycosylation occurs as soon as the protein sequence
Unfolded_protein_response
Type of enzyme
in the purified enzyme, thus reflecting the essential nature of N-linked glycosylation in eukaryotes. DAD1 has been shown to interact with MCL1. GRCh38:
DAD1
Organic compound that consists only of carbon, hydrogen, and oxygen
acid). Sugars may be linked to other types of biological molecules to form glycoconjugates. The enzymatic process of glycosylation creates sugars that
Carbohydrate
Mammalian protein found in Homo sapiens
Kamerling JP, Vliegenthart JF (January 1999). "Glycosylation sites and site-specific glycosylation in human Tamm–Horsfall glycoprotein". Glycobiology
Uromodulin
Polysaccharides found in animal tissue
via O-linked glycosylation by glycosyltransferases, thus forming proteoglycans. Keratan sulfate which may modify core proteins through N-linked glycosylation
Glycosaminoglycan
Microbial gene found in Klebsiella aerogenes KCTC 2190
Kingella kingae). N-linked glycosylation is an important process, especially in eukaryotes where over half of all proteins have N-linked sugars attached and
N-glycosyltransferase
Protein family
mature protein contains 468 amino acids, and includes six potential N-linked glycosylation sites and twelve cysteines, eight of which are tightly clustered
Glycoside_hydrolase_family_56
Protein-coding gene in humans
lipid-linked oligosaccharide precursor of N-linked glycosylation. Mutations in this gene are associated with congenital disorders of glycosylation type
ALG6
Protein-coding gene in the species Homo sapiens
Beta-1,4 N-acetylgalactosaminyltransferase 2 is an enzyme that in humans is encoded by the B4GALNT2 gene. GRCh38: Ensembl release 89: ENSG00000167080
B4GALNT2
Protein-coding gene in the species Homo sapiens
attention from the scientific community. N-Linked and O-linked glycans are the most abundant forms of protein glycosylation and occur on proteins destined for
DPAGT1
Rod-shaped, gram-negative bacterium
post-translational modification such as glycosylation for stability or function have been expressed using the N-linked glycosylation system of Campylobacter jejuni
Escherichia_coli
Protein-coding gene in the species Homo sapiens
fucosyltransferases. It catalyzes the transfer of fucose from GDP-fucose to N-linked type complex glycopeptides. This enzyme is distinct from other fucosyltransferases
FUT8
Protein found in humans
PMID 8709226. Marin M, Lavillette D, Kelly SM, Kabat D (March 2003). "N-linked glycosylation and sequence changes in a critical negative control region of the
Syncytin-1
Chemical compound
and Maslinic Acid Interfere with Intracellular Trafficking and N-Linked Glycosylation of Intercellular Adhesion Molecule-1". Biological and Pharmaceutical
Corosolic_acid
Protein-coding gene in the species Homo sapiens
PMID 26895716. Tominaga N, Hagiwara K, Kosaka N, Honma K, Nakagama H, Ochiya T (May 2014). "RPN2-mediated glycosylation of tetraspanin CD63 regulates
RPN2
Species of virus
VSIV G gene is expressed and is commonly studied as a model for N-linked glycosylation in the endoplasmic reticulum (ER). It is translated into the rough
Indiana_vesiculovirus
Protein-coding gene in the species Homo sapiens
which is necessary for N-linked glycosylation of proteins and some lipids. SRD5A3-CDG Congenital disorder of glycosylation Kahrizi syndrome, a syndrome
SRD5A3
Class of enzymes
reticulum of eukaryotic cells. Biologically, it functions within the N-glycosylation pathway. MOGS is a glycoside hydrolase enzyme, belonging to Family
Mannosyl-oligosaccharide glucosidase
Mannosyl-oligosaccharide_glucosidase
Low-density lipoprotein containing apolipoprotein(a)
Nassir F, Hausman AM, Davidson NO (August 1998). "Inhibition of N-linked glycosylation results in retention of intracellular apo[a] in hepatoma cells,
Lipoprotein(a)
Protein found in humans
six domains derived from the α and β chains. C3 contains two main N-linked glycosylation sites: Asn-917 on the α-chain and Asn-63 on the β-chain, which together
Complement_component_3
Enzyme-coding gene in humans
protein glycosylation. Mutations in this gene have been associated with congenital disorder of glycosylation type Ig (CDG-Ig) characterized by abnormal N-glycosylation
ALG12
interactions). N-linked glycosylation can be seen in antibodies, on cell surfaces, and on various proteins throughout the matrix. Alterations in glycosylation are
PNGase_F
Reaction of a glycosyl donor and acceptor
A chemical glycosylation reaction involves the coupling of a glycosyl donor, to a glycosyl acceptor forming a glycoside. If both the donor and acceptor
Chemical_glycosylation
Family of transport proteins
specialized structures are embedded. Two of the glycosylation sites, the N-linked glycosylation terminal and C-linked terminal, are located in the cytosolic portion
Vesicular monoamine transporter
Vesicular_monoamine_transporter
Group of transport proteins
Ravell JC, Zheng L, Kanellopoulou C, et al. (September 2019). "N-linked glycosylation and expression of immune-response genes". The Journal of Biological
Magnesium_transporter1_family
PMID 8619474. Sgroi D, Nocks A, Stamenkovic I (1996). "A single N-linked glycosylation site is implicated in the regulation of ligand recognition by the
ST6GAL1
Species of virus
Specificity in the Coronavirus Receptor Aminopeptidase N (CD13): Influence of N-Linked Glycosylation". Journal of Virology. 75 (20): 9741–52. doi:10.1128/JVI
Feline_coronavirus
Protein found in egg whites
There are two recurring types of glycosylation, including O-linked and N-linked glycosylation. O-linked glycosylation occurs when sugars attach to the
Ovomucoid
Transmembrane protein family
dysfunction and neuronal loss in Huntington's disease models. Abnormal N-linked glycosylation of AMPAR subunits has been reported in schizophrenia, suggesting
AMPA_receptor
types of glycosylations include S-linked (via cysteine residues), C-linked (via tryptophan) and O-linked (via serine or threonine). By far, N-linked glycosylation
TRAPP_complex
Biochemical classification for carbohydrates
saccharides are covalently linked with proteins, peptides, lipids. Glycoconjugates are formed in processes termed glycosylation. Glycoconjugates are involved
Glycoconjugate
Enzyme family
Instead, 5α-R3 functions in reduction of polyphenol substrates and N-linked glycosylation pathways. Specific substrates include testosterone, progesterone
5α-Reductase
Protein-coding gene in the species Homo sapiens
first isolated by Yoshida and others. Equipped with three potential N-glycosylation sites and a length of 535 amino acids the structure of the MGAT4A gene
Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A
Alpha-1,3-mannosyl-glycoprotein_4-beta-N-acetylglucosaminyltransferase_A
apparatus. Two types of glycosylation occur in the Golgi apparatus: N-linked and O-linked glycosylation(sci direct). N-linked glycosylation occurs when an oligosaccharide
Conserved oligomeric Golgi complex
Conserved_oligomeric_Golgi_complex
Protein-coding gene in the species Homo sapiens
modification protein glycosylation co-translational protein modification response to unfolded protein protein N-linked glycosylation via asparagine ubiquitin-dependent
STT3B
Group of proteins
by a 123-aa chain region characteristic of the IL-17 family. An N-linked glycosylation site on the protein was first identified after purification of the
Interleukin_17
Protein-coding gene in the species Homo sapiens
1089/088922202320886352. PMID 12487819. Hart ML, Saifuddin M, Spear GT (2003). "Glycosylation inhibitors and neuraminidase enhance human immunodeficiency virus type
LMAN1
Protein found in humans
lysosomal degradation of glycoproteins with exposed terminal galactose or N-acetylgalactosamine residues. The asialoglycoprotein receptor may facilitate
Asialoglycoprotein_receptor_1
Glycoprotein spike on a viral capsid or viral envelope
glycosylated through N-linked glycosylation. Studies of the SARS-CoV-2 spike protein have also reported O-linked glycosylation in the S1 region. The
Coronavirus_spike_protein
Gram-negative gammaproteobacterium
North SJ, Panico M, Morris HR, Dell A, Wren BW, Aebi M (2002). "N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli"
Escherichia coli in molecular biology
Escherichia_coli_in_molecular_biology
Protein found in humans
protein N-linked glycosylation cognition transmembrane transport magnesium ion transmembrane transport neutrophil degranulation protein glycosylation protein
Magnesium transporter protein 1
Magnesium_transporter_protein_1
Glucose being transported from the blood into cells
12 transmembrane segments, a single N-linked glycosylation site, a large central cytoplasmic linker, and both N- and C-termini located in the cytoplasm
Glucose_uptake
Protein-coding gene in the species Homo sapiens
Asparagine-linked glycosylation protein 11 is an enzyme encoded by the ALG11 gene. Congenital disorder of glycosylation GRCh38: Ensembl release 89: ENSG00000253710
ALG11
Instrument in mass spectrometry
This is quite useful in analyzing phosphorylation states, O- or N-linked glycosylation, and sulfating. FTICR-MS are also applied increasingly in study
Fourier-transform ion cyclotron resonance
Fourier-transform_ion_cyclotron_resonance
Biochemistry
protein has been found to result in loss-of-function via affecting N-linked glycosylation and in turn causing proteasomal degradation of the protein. This
Biochemistry_of_body_odor
Protein-coding gene in the species Homo sapiens
carbohydrate derivative metabolic process UDP-N-acetylglucosamine metabolic process protein N-linked glycosylation Sources:Amigo / QuickGO Orthologs Databases
GFPT1
Medical condition
CDG1Q or Congenital disorder of glycosylation type 1q) is a rare, non X-linked congenital disorder of glycosylation (CDG) due to a mutation in the steroid
SRD5A3-CDG
Protein found in egg whites
transferrins found in other species. Ovotransferrin has a single N-linked glycosylation site as asparagine 492. While ovotransferrin identifies with its
Ovotransferrin
Immune system protein
usage through its peptide composition as well as by the degree of N-linked glycosylation." Unlike V1-V2 however, the V3 loop is highly variable and thus
CCR5
Protein-coding gene in the species Homo sapiens
6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548. Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22". Nature
Derlin-3
Mosquito-borne viral disease mainly in the US
single codon coding for amino acids belonging to the hypothesized N-linked glycosylation site of the envelope protein. Nevertheless, the latter can be due
Saint_Louis_encephalitis
Medical condition
X-linked intellectual disability refers to medical disorders associated with X-linked recessive inheritance that result in intellectual disability. As
X-linked intellectual disability
X-linked_intellectual_disability
Species of bacterium
jejuni include the pgl locus, which confers the ability to produce N-linked glycosylation of at least 22 bacterial proteins, at least some of which appear
Campylobacter_jejuni
Human sialoglycoprotein
discovered. There are Glycosylated O-linked events with the amino acid Serine at position 144, and two N-linked glycosylation events with Asparagine at positions
Podocalyxin
transmembrane segment with N terminus in cytoplasmic region. The extracellular domain of the β subunit contains six or seven N-linked glycosylation sites which is
Discovery and development of proton pump inhibitors
Discovery_and_development_of_proton_pump_inhibitors
Family of hormones which regulate calcium and phosphate balance
is characterised by the presence of 11 half-Cys residues and one N-linked glycosylation site. The actual amino acid sequence and total length differ between
Stanniocalcin
Medical condition
of glycosylation events in the Golgi are N-linked glycosylation and O-linked glycosylation. Glycosylation of proteins destined for secretion occurs through
Wrinkly_skin_syndrome
Species of virus
of 1549 amino acids with 8 potential sites for N-linked glycosylation. It contains a unique potential N-gly site in the Gn and Gc glycoprotein regions
Kupe_virus
Protein family
infection. The mannose receptor is heavily glycosylated and its N-linked glycosylation sites are highly conserved between mice and humans, indicating an
Mannose_receptor
Class of enzymes
jejuni N-linked glycosylation pathway". Biochemistry. 46 (50): 14342–8. doi:10.1021/bi701956x. PMC 2585822. PMID 18034500. N-acetylgalactosamine-N,N
N-acetylgalactosamine-N,N'-diacetylbacillosaminyl-diphospho-undecaprenol_4-alpha-N-acetylgalactosaminyltransferase
Enzyme
monomeric enzyme with the isoelectric point at 6.4. Post-translational N-linked glycosylation increases the total mass to approximately 74 kDa. The tertiary structure
Tetrahydrocannabinolic acid synthase
Tetrahydrocannabinolic_acid_synthase
Term in molecular biology
is often modified in a particular way. Modifications may be N- or O- linked glycosylation, phosphorylation, tyrosine sulfation or other. "Reviews glossary"
Consensus_site
Protein-coding gene in the species Homo sapiens
defective surface expression of GPI-anchored proteins, defective N-linked glycosylation and deficient O-mannosylation of α-dystroglycan. Dol-P-Man is synthesized
DPM2
Chemical compound
that connects serine or threonine in particular forms of protein O-glycosylation. N-Acetylgalactosamine is necessary for intercellular communication, and
N-Acetylgalactosamine
Human blood group classification
is still expressed in the other cell types. It has two potential N-linked glycosylation sites at asparagine (Asn) 16 and Asn27. The Duffy antigen has been
Duffy_antigen_system
Protein-coding gene in humans
217–23. doi:10.1016/0003-9861(95)90003-9. PMID 7625827. Nagase T, Miyajima N, Tanaka A, et al. (1995). "Prediction of the coding sequences of unidentified
DDOST
Protein-coding gene in humans
modifications are predicted: Modified Phosphotyrosine Residue Two N-Linked Glycosylation Sites A Signal Peptide and signal peptide cleavage site was predicted
NAXD
Protein-coding gene in the species Homo sapiens
this gene transfers a GlcNAc residue to the beta-linked mannose of the trimannosyl core of N-linked oligosaccharides and produces a bisecting GlcNAc.
MGAT3
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