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biochemistry & molecular biology (21) 21
glycosylation (18) 18
pngase (16) 16
animals (15) 15
endoplasmic-reticulum (12) 12
index medicus (11) 11
humans (10) 10
molecular sequence data (10) 10
peptide-n4- asparagine amidase - metabolism (10) 10
amino acid sequence (9) 9
mice (8) 8
endoplasmic reticulum - metabolism (7) 7
glycoproteins - chemistry (7) 7
peptide-n-glycanase (7) 7
substrate specificity (7) 7
cell biology (6) 6
cell line (6) 6
enzymes (6) 6
identification (6) 6
proteins (6) 6
alpha-mannosidase (5) 5
biophysics (5) 5
carbohydrate sequence (5) 5
cytoplasmic peptide (5) 5
cytosol - metabolism (5) 5
glycoproteins - metabolism (5) 5
glycoside hydrolases - metabolism (5) 5
multidisciplinary sciences (5) 5
n-glycan (5) 5
peptide (5) 5
polysaccharides - analysis (5) 5
saccharomyces cerevisiae - metabolism (5) 5
yeast (5) 5
deglycosylation (4) 4
erad (4) 4
expression (4) 4
glycopeptides - metabolism (4) 4
glycoproteins (4) 4
mannosidases - metabolism (4) 4
molecular-cloning (4) 4
n-linked glycosylation (4) 4
peptide-n4- asparagine amidase (4) 4
peptide-n4- asparagine amidase - chemistry (4) 4
peptide-n4- asparagine amidase - genetics (4) 4
peptides (4) 4
polysaccharides - metabolism (4) 4
protein structure, tertiary (4) 4
quality-control (4) 4
research article (4) 4
spectrometry, mass, matrix-assisted laser desorption-ionization (4) 4
unfertilized eggs (4) 4
alpha-mannosidase - metabolism (3) 3
amidase (3) 3
amidohydrolases - isolation & purification (3) 3
analysis (3) 3
base sequence (3) 3
biological sciences (3) 3
cells (3) 3
chromatography, high pressure liquid (3) 3
complex (3) 3
core fucosylation (3) 3
cytosol (3) 3
de-n-glycosylation (3) 3
degradation (3) 3
flavobacterium-meningosepticum (3) 3
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hela cells (3) 3
i heavy-chains (3) 3
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medaka fish (3) 3
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peptide : n-glycanase (3) 3
peptide:n-glycanase (3) 3
peptides - metabolism (3) 3
polymannose-type oligosaccharides (3) 3
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proteasome (3) 3
protein folding (3) 3
recombinant proteins - genetics (3) 3
recombinant proteins - metabolism (3) 3
reticulum-associated degradation (3) 3
saccharomyces cerevisiae proteins - metabolism (3) 3
1st demonstration (2) 2
acetylglucosaminidase (2) 2
activation (2) 2
adenosine triphosphatases (2) 2
amidohydrolases - metabolism (2) 2
animal-cells (2) 2
binding sites (2) 2
biochemistry (2) 2
biochemistry - methods (2) 2
blotting, western (2) 2
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Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2005, Volume 102, Issue 26, pp. 9144 - 9149
In eukaryotes, misfolded proteins must be distinguished from correctly folded proteins during folding and transport processes by quality control systems. Yeast... 
Proteins | Molecules | Yeasts | Biological Sciences | Polysaccharides | Active sites | Atomic interactions | Crystals | Atoms | Glycoproteins | Structural homology | Zinc-metalloenzyme | Deep cleft | PNGase | MECHANISM | CRYSTAL-STRUCTURE | CYTOPLASMIC PEPTIDE | MULTIDISCIPLINARY SCIENCES | YEAST PEPTIDE | PROTEIN-DEGRADATION | deep cleft | ENDOPLASMIC-RETICULUM | N-GLYCANASE | DNA-REPAIR | zinc-metalloenzyme | REVEALS | Humans | Molecular Sequence Data | Substrate Specificity | Crystallography, X-Ray | Cytoplasm - metabolism | Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase - chemistry | Zinc - chemistry | DNA-Binding Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Amino Acid Chloromethyl Ketones - pharmacology | DNA Mutational Analysis | Protein Denaturation | Glycoproteins - chemistry | Binding Sites | Circular Dichroism | Protein Structure, Tertiary | Amino Acid Sequence | Biophysical Phenomena | Protein Structure, Secondary | Enzyme Inhibitors - pharmacology | Models, Molecular | Recombinant Proteins - chemistry | Glycosylation | Biophysics | Caspase Inhibitors | DNA-Binding Proteins - chemistry | Protein Folding | Sequence Homology, Amino Acid | Spectrophotometry, Atomic | Animals | Mutagenesis | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Protein Conformation | Proteasome Endopeptidase Complex - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Research | Peptides | Metalloenzymes | Structure | Proteolysis
Journal Article
Journal of the Chinese Chemical Society, ISSN 0009-4536, 03/2012, Volume 59, Issue 3, pp. 269 - 272
A clickable alkyne tagged chloroacetamidyl chitobiose derivative was synthesized as a potential inhibitor of cytoplasmic peptide‐N‐glycanase (PNGase).... 
Click coupling | PNGase | Inhibitor | Synthesis | ACETONYLTRIPHENYLPHOSPHONIUM BROMIDE | ORGANIC-SYNTHESIS | TURNOVER | PROTECTION | STRATEGY | ALKYL VINYL ETHERS | TERMINAL ALKYNES | DEPROTECTION | CHEMISTRY, MULTIDISCIPLINARY | CYCLOADDITIONS
Journal Article
Journal Article
Biochemical Journal, ISSN 0264-6021, 11/2006, Volume 400, Issue 1, pp. 33 - 41
The endoplasmic-reticulum-associated degradation of misfolded (glyco)proteins ensures that only functional, correctly folded proteins exit from the endoplasmic... 
Peptide:N-glycanase (PNGase) | N-glycan | Non-lysosomal degradation | α-mannosidase | Cytosol | Free oligosaccharide | RAT-LIVER | non-lysosomal degradation | cytosol | BIOCHEMISTRY & MOLECULAR BIOLOGY | FULL-LENGTH CDNA | alpha-mannosidase | SUBSTRATE-SPECIFICITY | free oligosaccharide | peptide : N-glycanase (PNGase) | PEPTIDE-N-GLYCANASE | HEPG2 CELLS | POLYMANNOSE-TYPE OLIGOSACCHARIDES | ENDOPLASMIC-RETICULUM | HEN OVIDUCT | EXPRESSION | JAPANESE-QUAIL OVIDUCT | Immunohistochemistry | Membrane Glycoproteins - metabolism | Oligopeptides | Humans | alpha-Mannosidase - metabolism | Cytosol - drug effects | Peptides - genetics | alpha-Mannosidase - antagonists & inhibitors | Green Fluorescent Proteins - genetics | Mannosidases - metabolism | Chromatography, High Pressure Liquid | Recombinant Fusion Proteins - metabolism | Cytosol - enzymology | Peptides - metabolism | Transfection | Cobalt - pharmacology | RNA Interference | Oligosaccharides - chemistry | Mannosidases - genetics | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Swainsonine - pharmacology | Cell Line | Green Fluorescent Proteins - metabolism | Alkaloids - pharmacology | Mannosidases - antagonists & inhibitors | Oligosaccharides - metabolism | Blotting, Western | Gene Expression Regulation, Enzymologic | Recombinant Fusion Proteins - genetics | Cytosol - metabolism | alpha-Mannosidase - genetics | EGFP, enhanced green fluorescent protein | KIF, kifunensine | RNAi, RNA interference | 2-AA, 2-aminobenzoic acid | PNGase, peptide:N-glycanase | DMM, deoxymannojirimycin | siRNA, small interfering RNA | pNP-α-Man, p-nitrophenyl-α-D-mannoside | peptide:N-glycanase (PNGase) | PA, pyridylamino | MALDI–TOF MS, matrix-assisted laser desorption ionization–time-of-flight MS | ERAD, ER-associated degradation | RNase B, ribonuclease B | ENGase, endo-β-N-acetylglucosaminidase | SW, swainsonine | ER, endoplasmic reticulum | PDI, protein disulfide-isomerase | GAPDH, glyceraldehyde-3-phosphate dehydrogenase | TFA, trifluoroacetic acid
Journal Article
Biochemical Journal, ISSN 0264-6021, 01/2006, Volume 393, Issue 1, pp. 1 - 6
The identification of all the substrates of every protein kinase is one of the major challenges of post-genomic research. Here we review a powerful method for... 
Mitogen-activated-protein-kinase-activated protein kinase-2 (MAPKAP-K2) | Protein kinase B (PKB) | Glycogen synthase kinase 3 (GSK3) | Serum- and glucocorticoid-induced protein kinase (SGK) | Kinase substrate tracking and elucidation (KESTREL) | CELLS | glycogen synthase kinase 3 (GSK3) | DOMAIN | SPECIFICITY | PHOSPHORYLATION | PKB | BIOCHEMISTRY & MOLECULAR BIOLOGY | SERUM | IDENTIFICATION | IN-VITRO | protein kinase B (PKB) | kinase substrate tracking and elucidation (KESTREL) | mitogen-activated-protein-kinase-activated protein kinase-2 (MAPKAP-K2) | TRANSFER-RNA | STRESS | serum- and glucocorticoid-induced protein kinase (SGK) | Protein Kinases - metabolism | Phosphorylation | Protein Kinases - genetics | Reproducibility of Results | Animals | Peptide Mapping | Biochemistry - methods | Substrate Specificity | Protein Kinases - deficiency | CRMP, collapsin-response mediator protein | PI3K, phosphoinositide 3-kinase | SAKS1, SAPK-substrate 1 | TNF, tumour necrosis factor | hnRNP, heterogeneous nuclear ribonucleoprotein | PNGase, peptide N-glycanase | PDK1, 3-phosphoinositide-dependent kinase 1 | HEK, human embryonic kidney | Review | JNK, c-Jun N-terminal kinase | EF2, elongation factor 2 | UBA, ubiquitin-associated | KSHV, Kaposi sarcoma-associated herpesvirus | UBX, ubiquitin-like | ERK, extracellular-signal-regulated kinase | PKB, protein kinase B | SAPK, stress-activated protein kinase | MKK1, MAPK kinase-1 | EF2K, EF2 kinase | HSP27, heat-shock protein of 27 kDa | METTL1, methyltransferase-like protein 1 | FLNc, filamin C | NDRG, N-myc downstream-regulated gene product | VCP, valosin-containing protein | GSK3, glycogen synthase kinase 3 | SGK, serum- and glucocorticoid-induced protein kinase | IGF-1, insulin-like growth factor 1 | KESTREL, kinasesubstrate tracking and elucidation | MAPKAP-K2, MAPK-activated protein kinase-2 | CDK, cyclin-dependent protein kinase | CRHSP24, calcium-regulated heatshock protein of 24 kDa | PIC, pro-inflammatory cytokine | LPS, lipopolysaccharide | ARE, AU-rich element | CapZIP, CapZ-interacting protein | MAPK, mitogen-activated protein kinase
Journal Article
Biochemical Journal, ISSN 0264-6021, 12/2004, Volume 384, Issue 2, pp. 391 - 400
A widely expressed protein containing UBA (ubiquitin-associated) and UBX (ubiquitin-like) domains was identified as a substrate of SAPKs (stress-activated... 
Peptide N-glycanase (PNGase) | Stress-activated protein kinase (SAPK) | Ubiquitin-like domain (UBX domain) | Valosin-containing protein (VCP) | p97 | Ubiquitin-associated domain (UBA domain) | VALOSIN-CONTAINING PROTEIN | ACTIVATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELLULAR STRESSES | IDENTIFICATION | ubiquitin-associated domain (UBA domain) | P38 MAP KINASE | FAMILY | UNNATURAL NUCLEOTIDE SPECIFICITY | ubiquitin-like domain (UBX domain) | valosin-containing protein (VCP) | PATHWAY | PROTEASOME | DEGRADATION | stress-activated protein kinase (SAPK) | peptide N-glycanase (PNGase) | Arsenites - pharmacology | Osmotic Pressure | Fibroblasts - enzymology | Protein Subunits - immunology | Kidney - embryology | Humans | Kidney - enzymology | Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase - metabolism | Valosin Containing Protein | Molecular Sequence Data | Substrate Specificity | Protein Subunits - metabolism | Cell Cycle Proteins - immunology | Peptides - metabolism | Protein Binding - drug effects | Mitogen-Activated Protein Kinases - immunology | p38 Mitogen-Activated Protein Kinases - metabolism | Polyubiquitin - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | Immunoprecipitation - methods | Cell Cycle Proteins - metabolism | Cells, Cultured | Cell Extracts - chemistry | Kidney - cytology | Sodium Compounds - pharmacology | Mice, Knockout | Multienzyme Complexes - chemistry | Mitogen-Activated Protein Kinases - deficiency | Leupeptins - pharmacology | Animals | Adenosine Triphosphatases | Mice | Mitogen-Activated Protein Kinases - metabolism | GST, glutathione S-transferase | EGF, epidermal growth factor | PNGase, peptide N-glycanase | ORF, open reading frame | VCP, valosin-containing protein | JNK, c-Jun N-terminal kinase | DTT, dithiothreitol | HEK-293, human embryonic kidney | UBA, ubiquitin-associated | KESTREL, kinasesubstrate tracking and elucidation | UBX, ubiquitin-like | ERK, extracellular-signal-regulated kinase | SAPK, stress-activated protein kinase | SAKS1, stress-activated protein kinase substrate-1 | MAP kinase, mitogen-activated protein kinase | MGP, misfolded glycoprotein | PEG, poly(ethylene glycol)
Journal Article
Trends in Glycoscience and Glycotechnology, ISSN 0915-7352, 07/2009, Volume 21, Issue 120, pp. 219 - 227
N-glycosylation is now recognized as one of the most important modification reactions in eukaryotic cells, and it has been demonstrated that N-glycans on... 
Pngase | Catabolism | N-glycans | Cytosol | Lysosome | ACETYLGLUCOSAMINIDASE | cytosol | CYTOPLASMIC PEPTIDE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROTEIN-PROTEIN INTERACTION | EUKARYOTIC CELLS | catabolism | GENE ENCODES | CATABOLIC PATHWAY | ENDO-BETA-MANNOSIDASE | PEPTIDE-N-GLYCANASE | POLYMANNOSE-TYPE OLIGOSACCHARIDES | PNGase | lysosome
Journal Article
Biochemical Journal, ISSN 0264-6021, 08/2004, Volume 381, Issue 3, pp. 629 - 634
Journal Article
FEBS Letters, ISSN 0014-5793, 05/2001, Volume 496, Issue 2-3, pp. 152 - 160
Journal Article
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