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TunicamycinGlycosylationLipidsGlucosamineGlycoproteinsPolysaccharidesMolecular Sequence DataProtein BindingProtein Interaction MappingDolichol PhosphatesAmino Acid SequenceCongenital Disorders of GlycosylationDolicholOligosaccharidesProtein Modification, TranslationalGuanosine Diphosphate MannoseMannoseUridine Diphosphate N-AcetylglucosamineAcetylglucosamineTwo-Hybrid System TechniquesProtein Processing, Post-TranslationalCell LineGlycomicsLipid MetabolismGlycosyltransferasesGlycopeptidesCampylobacter jejuniBinding SitesProtein Structure, TertiaryCarbohydrate Metabolism, Inborn ErrorsCarbohydrate SequenceMannosyltransferasesModels, MolecularLipid AHexosaminesEndoplasmic ReticulumBase SequenceProtein ConformationAsparagineN-AcetylglucosaminyltransferasesPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidaseMannose-6-Phosphate IsomeraseUridine Diphosphate GlucoseCarbohydrate ConformationHexosyltransferasesPhosphotransferases (Phosphomutases)LectinsLipid BilayersTranscription FactorsPolyisoprenyl Phosphate OligosaccharidesGolgi ApparatusPolyisoprenyl Phosphate MonosaccharidesMembrane ProteinsPolyisoprenyl Phosphate SugarsMass SpectrometryMutationFucoseDolichol Monophosphate MannoseGlycoside HydrolasesSwainsonineTransferases (Other Substituted Phosphate Groups)Electrophoresis, Polyacrylamide GelMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseUridine Diphosphate GalactoseN-AcetylgalactosaminyltransferasesCricetinaeNeisseriaKineticsLipid PeroxidationMannosidasesN-Acetylneuraminic AcidBrefeldin ACarbohydrate MetabolismCell MembraneCarbohydratesIndolizinesMembrane GlycoproteinsRecombinant ProteinsHygromycin BNucleoside Diphosphate SugarsConcanavalin ACells, CulturedProteinsBacterial ProteinsSaccharomyces cerevisiaeSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationViral Envelope ProteinsWheat Germ AgglutininsMucinsMolecular WeightPolyisoprenyl PhosphatesGlycosidesIntracellular MembranesProteomicsLipid PeroxidesGalactose1-DeoxynojirimycinProtein FoldingGenetic Complementation TestSpectrometry, Mass, Electrospray Ionization

Endoplasmic reticulumMembraneSubcellularGlycomicsGeneticallyAMINO ACIDSMitochondrial matrixBindResiduesAccumulationStructuralChaperoneAccumulateMoleculeRegulatorApoptosisBiochemicalChemicalsPreventsEmbryonicImportant roleCellsProcessesSiteProductionResponseEssentialHumanFormationGlobalTransportInfluenceStructureSolutionMolecularFunctionsStudyLoadSpecificActivityDirectlyTranslationConditions

Endoplasmic reticulum9

• The unfolded protein response (UPR) is a cellular stress response related to the endoplasmic reticulum (ER) stress. (wikipedia.org)
• The UPR is activated in response to an accumulation of unfolded or misfolded proteins in the lumen of the endoplasmic reticulum. (wikipedia.org)
• In such circumstances the protein is guided through endoplasmic reticulum-associated degradation (ERAD). (wikipedia.org)
• Recent studies indicate that nutrient fluctuations and insulin resistance increase proinsulin synthesis in β cells beyond the capacity for folding of nascent polypeptides within the endoplasmic reticulum (ER) lumen, thereby disrupting ER homeostasis and triggering the unfolded protein response (UPR). (jci.org)
• A high-mannose oligosaccharide precursor is synthesized and transferred to proteins in the endoplasmic reticulum and then processed in the Golgi apparatus ( 4 ). (frontiersin.org)
• For instance, how can cells control the diverse patterns of glycosylation of various secretory proteins in the endoplasmic reticulum and Golgi in an orderly manner with high accuracy? (go.jp)
• Many proteins are made in a compartment within the cell called the endoplasmic reticulum and 'chaperone' proteins help them fold correctly. (elifesciences.org)
• This leads to an increase in the number of unfolded proteins in the endoplasmic reticulum and so the cell increases the levels of chaperone proteins to cope with this. (elifesciences.org)
• used biochemical techniques to study how an Hsp70 protein in the endoplasmic reticulum called BiP forms oligomers. (elifesciences.org)

Membrane2

• This minireview gives an updated and consolidated summary of taxonomic classification correlated with membrane phospholipid, glycolipid, and core lipid structural diversity within the family Halobacteriaceae. (go.jp)
• We also point out that the recently reported diversity in the membrane core lipid structure of a putative strain of Halobacterium ( Halobacterium halobium strain IAM 13167) (Morita et al . (go.jp)

Subcellular2

• Glycosylation of those proteins was proven to influence their subcellular locations. (frontiersin.org)
• notably, integration of proteomics data with in situ subcellular microscopic analyses showed a high abundance of cytoskeleton proteins associated with acidified PBs at the early development stages. (nature.com)

Glycomics1

• Large-scale analysis of glycosylation in organisms includes glycomics (glycan profiling) and glycoproteomics (glycosylation site profiling) ( 5 ). (frontiersin.org)

Genetically2

• A genetically heterogeneous group of heritable disorders resulting from defects in protein N-glycosylation. (lookformedical.com)
• Together our data identified promising targets to be genetically engineered to modulate seed storage protein accumulation that have a growing role in health and nutritional issues. (nature.com)

AMINO ACIDS2

• Any of the enzymatically catalyzed modifications of the individual AMINO ACIDS of PROTEINS, and enzymatic cleavage or crosslinking of peptide chains that occur pre-translationally (on the amino acid component of AMINO ACYL TRNA), co-translationally (during the process of GENETIC TRANSLATION), or after translation is completed (POST-TRANSLATIONAL PROTEIN PROCESSING). (lookformedical.com)
• Proteins are composed of long chains of amino acids that fold on themselves to form three-dimensional structures. (elifesciences.org)

Mitochondrial matrix1

• Here, polymerase-interacting protein 2 (Poldip 2) was found in the endothelial mitochondrial matrix and no effects on Poldip 2 and NADPH oxidase 4 (NOX 4) expression treated by Ang II. (bvsalud.org)

Bind2

• We found that the FERM domain in the tail region, which is known to bind to lipids as well as other proteins, is essential for both nuclear and chloroplast positioning, whereas the proximal MyTH4 domain plays a supporting role in chloroplast transport. (go.jp)
• The presence of the interdomain linker makes it more difficult for unfolded proteins to bind. (elifesciences.org)

Residues2

• The aforementioned sugar molecule remains the means by which the cell monitors protein folding, as the misfolding protein becomes characteristically devoid of glucose residues, targeting it for identification and re-glycosylation by the enzyme UGGT (UDP-glucose:glycoprotein glucosyltransferase). (wikipedia.org)
• If this fails to restore the normal folding process, exposed hydrophobic residues of the misfolded protein are bound by the protein glucose regulate protein 78 (Grp78), a heat shock protein 70kDa family member that prevents the protein from further transit and secretion. (wikipedia.org)

Accumulation1

• Cereal endosperm is a short-lived tissue adapted for nutrient storage, containing specialized organelles, such as protein bodies (PBs) and protein storage vacuoles (PSVs), for the accumulation of storage proteins. (nature.com)

Structural1

• Favoured by the highly oxidizing environment of the ER, protein disulfide isomerases facilitate formation of disulfide bonds, which confer structural stability to the protein in order for it to withstand adverse conditions such as extremes of pH and degradative enzymes. (wikipedia.org)

Chaperone5

• The chaperone EDEM guides the retrotranslocation of the misfolded protein back into the cytosol in transient complexes with PDI and Grp78. (wikipedia.org)
• Cells carefully regulate the levels of chaperone proteins. (elifesciences.org)
• Hsp70 chaperones are one family of chaperone proteins. (elifesciences.org)
• These proteins can be present in a cell as single molecules (monomers) or as a group of several chaperone molecules (oligomers). (elifesciences.org)
• Previous research has suggested that the chaperone proteins in oligomers are inactive, but the oligomers may be rapidly broken down into monomers when the cell needs to fold more proteins. (elifesciences.org)

Accumulate1

• Where circumstances continue to cause a particular protein to misfold, the protein is recognized as posing a threat to the proper functioning of the ER, as they can aggregate to one another and accumulate. (wikipedia.org)

Molecule1

• The experiments show that oligomers form when the interdomain linker of one BiP molecule is bound to the region of an adjacent BiP molecule that is normally reserved for binding to unfolded proteins. (elifesciences.org)

Regulator1

• The PI3K/Akt/mTOR signaling pathway is a key regulator of diverse physiological functions such as proliferation, global protein, and lipid synthesis as well as many metabolic pathways interacting to increase secretory capabilities. (go.jp)

Apoptosis3

• Chronic ER stress promotes apoptosis, at least in part through the UPR-induced transcription factor C/EBP homologous protein (CHOP). (jci.org)
• These findings suggest that CHOP is a fundamental factor that links protein misfolding in the ER to oxidative stress and apoptosis in β cells under conditions of increased insulin demand. (jci.org)
• Bax and Bak play a redundant but essential role in apoptosis initiated by the mitochondrial release of apoptogenic factors. (rupress.org)

Biochemical1

• The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. (lookformedical.com)

Chemicals1

• Further experiments challenged cells with chemicals that caused the number of unfolded proteins in the cells to increase. (elifesciences.org)

Prevents1

• Tunicamycin inhibits bacterial and eukaryote N-acetylglucosamine transferases and prevents formation of N-acetylglucosamine lipid intermediates. (sigmaaldrich.com)

Embryonic1

• In this study, the spatiotemporal expression pattern of FOXG1 was examined during early mouse oocyte and embryonic development and its role during corpora luteum (CL) formation was further elucidated. (bvsalud.org)

Important role2

• Tunicamycin plays an important role in the antitumor activity of trastuzumab on breast cancer in vitro and in vivo . (sigmaaldrich.com)
• Gegen Qinlian Pills (GQP) is a Traditional Chinese Medicine that is included in the Chinese Pharmacopoeia and played an important role in the clinical fight against COVID-19. (bvsalud.org)

Cells4

• Tunicamycin has been used to study the effect of N-linked glycosylation of human proton-coupled folate transporter (HsPCFT) in HeLa cells. (sigmaaldrich.com)
• Tunicamycin has also been used to study the functional effects of coxsackievirus and adenovirus receptor (CAR) glycosylation in COS-7 cells. (sigmaaldrich.com)
• However, when the levels of unfolded proteins rise, cells can rapidly break up these oligomers to make active monomers that help to deal with the excess numbers of unfolded proteins. (elifesciences.org)
• Further work is needed to understand how changes in the number of unfolded proteins in cells leads to the formation and disassembly of BiP oligomers. (elifesciences.org)

Processes4

• better source needed] The term protein folding incorporates all the processes involved in the production of a protein after the nascent polypeptides have become synthesized by the ribosomes. (wikipedia.org)
• These glycoproteins are widely involved in important biological processes, such as antigen presentation, cytokine production and glycosylation progression. (frontiersin.org)
• Glycosylation is an important post-translational modification of proteins, and glycoproteins are widely involved in various important cellular biological processes and diseases ( 1 ). (frontiersin.org)
• If there are too few chaperones in the cell, then newly-made proteins may fold incorrectly and interrupt other processes. (elifesciences.org)

Site2

• Electrophoresis in which a pH gradient is established in a gel medium and proteins migrate until they reach the site (or focus) at which the pH is equal to their isoelectric point. (lookformedical.com)
• The starchy endosperm thereby is characterized as a storage site, accumulating starch and seed storage proteins (SSPs) 2 . (nature.com)

Production2

• In this scenario, the UPR has three aims: initially to restore normal function of the cell by halting protein translation, degrading misfolded proteins, and activating the signalling pathways that lead to increasing the production of molecular chaperones involved in protein folding. (wikipedia.org)
• Thus, endomembrane-modifying proteins within the endomembrane system will have an influence on the final grain quality/yield and recombinant protein production. (nature.com)

Response2

• UPR, unfolded protein response. (rupress.org)
• Thus, equilibration between inactive oligomers and active monomeric BiP is poised to buffer fluctuations in ER unfolded protein load on a rapid timescale attainable neither by inter-conversion of active and covalently-modified BiP nor by the conventional unfolded protein response. (elifesciences.org)

Essential1

• The aleurone layer plays essential roles during seed germination and mobilizes starch and SSP reserves in the starchy endosperm by releasing hydrolytic enzymes that are responsible for the degradation of stored nutrients in the endosperm 2 . (nature.com)

Human3

• In human cell lines, tunicamycin enhances cytotoxicity stimulated by cisplatin. (sigmaaldrich.com)
• human-ABHD12 Homo sapiens (Human) abhydrolase domain-containing protein 12. (inra.fr)
• Vascular endothelial dysfunction plays a central role in the most dreadful human diseases, including stroke, tumor metastasis, and the coronavirus disease 2019 (COVID-19). (bvsalud.org)

Formation2

• Tunicamycin blocks the formation of protein N-glycosidic linkages by inhibiting the transfer of N-acetylglucosamine 1-phosphate to dolichol monophosphate. (sigmaaldrich.com)
• The most important of these to note are N-linked glycosylation and disulfide bond formation. (wikipedia.org)

Global1

• However, where circumstances cause a more global disruption to protein folding that overwhelms the ER's coping mechanisms, the UPR is activated. (wikipedia.org)

Transport2

• It plays a central role in the transport of IRON throughout the circulation. (lookformedical.com)
• Moreover, endosomal sorting complex required for transport (ESCRT)-related proteins and their transcripts are most abundant at early and mid-development. (nature.com)

Influence1

• Consequently, endomembrane-modifying proteins will influence the final grain quality and yield. (nature.com)

Structure1

• Current research shows that the glycan of a protein can directly affect its structure and can also maintain the stability of the protein ( 3 ). (frontiersin.org)

Solution2

• Tunicamycin Ready Made Solution 5mg/mL DMSO, Streptomyces sp. (sigmaaldrich.com)
• Tunicamycin Ready Made Solution contains homologues A,B,C, and D. The composition may vary from lot to lot. (sigmaaldrich.com)

Molecular1

• Protein folding steps involve a range of enzymes and molecular chaperones to coordinate and regulate reactions, in addition to a range of substrates required in order for the reactions to take place. (wikipedia.org)

Functions1

• Different glycans of proteins can result in different immunogenicities and immune functions ( 2 ). (frontiersin.org)

Study1

• Our previous study suggested a crosstalk between extracellular regulated protein kinase (ERK) phosphorylation and CypD expression, and gallic acid (GA) inhibited mitochondrial dysfunction in neurons depending on regulating the ERK-CypD axis. (bvsalud.org)

Load1

• An overwhelming load of misfolded proteins or simply the over-expression of proteins (e.g. (wikipedia.org)

Specific2

• It maintains specific transmembrane receptor proteins involved in initiation of the downstream signalling of the UPR in an inactive state by binding to their luminal domains. (wikipedia.org)
• and most prolamins are finally deposited in specific, ER-derived protein bodies (PBs) or/and in PSVs. (nature.com)

Activity2

• Tunicamycin was first isolated from Streptomyces lysosuperificus based on its antiviral activity. (sigmaaldrich.com)
• The events in signal transduction that govern MMP expression and activity and expression of inhibitory proteins are crucial for understanding wound healing, tumorigenesis, and certain genetic diseases. (stanford.edu)

Directly1

• Once the sequence has "docked", the protein continues translation, with the resultant strand being fed through the polypeptide translocator directly into the ER. (wikipedia.org)

Translation1

• Protein folding commences as soon as the polypeptide enters to the luminal environment, even as translation of the remaining polypeptide continues. (wikipedia.org)

Conditions1

• If a cell experiences stressful conditions, or if there is a sudden demand for more proteins to be made, protein folding can be disrupted. (elifesciences.org)