The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
Uggt1 (UniProt Q9JLA3) in Rattus norvegicus encodes UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1), a ~170 kDa endoplasmic reticulum (ER) luminal glycoprotein-folding sensor and quality-control enzyme that catalyzes reglucosylation of N-linked glycans on non-native glycoproteins. This function places Uggt1 in the ER glycoprotein folding/quality-control system (the calnexin/calreticulin cycle) and distinguishes it from (i) drug-metabolizing “UGT1A” glucuronosyltransferases and (ii) the paralog UGGT2, which has overlapping but distinct client preferences and lower abundance in some systems. (sagert2023theerfolding pages 1-2, adams2020quantitativeglycoproteomicsreveals pages 1-4, ninagawa2024uggt1mediatedreglucosylationof pages 5-9)
UGGT1 is a reglucosylating glycosyltransferase that transfers a glucose residue from UDP-glucose onto deglucosylated N-linked glycans on glycoproteins that have not reached a native conformation. In a defined antigen-presentation substrate system, UGGT1 converted Man9GlcNAc2 → Glc1Man9GlcNAc2 on MHC I, which is the canonical “tag” for lectin-chaperone binding in the ER. (sagert2023theerfolding pages 1-2, sagert2023theerfolding pages 7-8)
Catalytic requirements: UGGT1 catalytic activity requires Ca2+, coordinated by a DxD motif in the catalytic site; importantly, Ca2+ is necessary for catalysis but not necessarily for client binding in all contexts (see §3.1). (sagert2023theerfolding pages 7-8)
The calnexin (CNX) / calreticulin (CRT) cycle is an ER lectin-chaperone system for folding N-glycosylated proteins. When a glycoprotein carries a monoglucosylated N-glycan it can bind CNX/CRT; after deglucosylation, a protein that is still non-native can be reglucosylated by UGGT1, enabling additional rounds of CNX/CRT-assisted folding and preventing premature ER exit. (ninagawa2024uggt1mediatedreglucosylationof pages 1-5, sagert2023theerfolding pages 1-2)
UGGT1 is a conformation sensor: it preferentially acts on proteins that are non-native and can prefer clients with exposed hydrophobic regions, consistent with recognition of misfolded/partially folded surfaces rather than fully folded proteins. (ninagawa2024uggt1mediatedreglucosylationof pages 1-5, ninagawa2024uggt1mediatedreglucosylationof pages 5-9)
A quantitative glycoproteomics strategy identified 71 endogenous UGGT substrates (in human cell models) and found these clients are biased toward large, multidomain, heavily glycosylated proteins. UGGT1 was the dominant cellular glucosyltransferase in that study and showed preference toward large plasma-membrane proteins, while UGGT2 favored smaller soluble lysosomal proteins. (adams2020quantitativeglycoproteomicsreveals pages 1-4)
A 2023 eLife study reconstituted an in vitro system with purified human proteins and used glycoengineering plus LC–MS to measure UGGT1 activity on MHC I. The work showed that the MHC I chaperone TAPBPR promotes UGGT1-catalyzed reglucosylation of peptide-free MHC I, while high-affinity peptide-loaded MHC I was not glucosylated—supporting a model where UGGT1 edits/folds only non-native states. (Publication: Jan 2023; https://doi.org/10.7554/eLife.85432) (sagert2023theerfolding pages 1-2, sagert2023theerfolding pages 8-9)
Quantitative data: Under their assay conditions, the UGGT1 reaction on the MHC I substrate reached a saturation of ~80%. (sagert2023theerfolding pages 8-9)
Mechanistic refinement (binding vs catalysis): Ca2+ is essential for UGGT1 catalysis, but in pull-down experiments, chelation (EGTA) or a catalytic-site mutant did not reduce binding of UGGT1 to the TAPBPR-associated MHC I complex, indicating that binding determinants can be separable from catalytic metal dependence. (sagert2023theerfolding pages 7-8)
A 2024 eLife study (preprint in 2023) directly tested the long-standing question of whether reglucosylation affects degradation of unstable/misfolded glycoproteins by using genetically disrupted UGGT1/UGGT2 cells. It reported that UGGT1 delays degradation of several misfolded/unstable substrates and framed glycoprotein fate as a “tug-of-war” between UGGT1-driven structure formation (via CNX/CRT re-entry) and degradation driven by mannose trimming/EDEM-mediated pathways. (Publication: Sep 2024; https://doi.org/10.1101/2023.10.18.562958) (ninagawa2024uggt1mediatedreglucosylationof pages 12-16, ninagawa2024uggt1mediatedreglucosylationof pages 1-5)
Pathway-level consequence: The authors further report physiological importance for ER stress signaling, stating ATF6α cannot function properly without UGGTs (UGGT1/2), with reduced induction of ERSE/UPRE reporters in UGGT-deficient contexts while ATF4 reporter activity was unchanged. (ninagawa2024uggt1mediatedreglucosylationof pages 12-16)
Quantitative/statistical notes from the study excerpt: UGGT2 protein abundance was reported as ~6.9% of UGGT1 in HCT116 cells and 29.8% of UGGT1 in HeLa cells, supporting UGGT1 as the dominant paralog in some mammalian systems. (ninagawa2024uggt1mediatedreglucosylationof pages 5-9)
UGGT1 forms a stable complex with the selenoprotein SEP15/SELENOF, which is proposed to act as a redox-active cochaperone in ER folding surveillance.
A 2024 PNAS study used AlphaFold2/AlphaFold-multimer plus mutagenesis and co-immunoprecipitation to refine the UGGT1–SEP15 interface. It proposed a UGGT1 SEP15-binding region (SBR) (a helix–loop–helix insertion) that is present in organisms with SEP15 and absent in organisms lacking SEP15, and it predicted a complex interface with buried surface area of about 1,860 Ų. (Publication: Aug 12, 2024; https://doi.org/10.1073/pnas.2315009121) (williams2024insightsintothe pages 3-4, williams2024insightsintothe pages 1-2)
Experimental validation (quantitative): In cell co-IP experiments summarized in the excerpt, WT interaction was measurable (reported as ~27% of expressed SEP15 detected in complex in that experimental configuration), while UGGT1 interface point mutants sharply reduced binding to ~3.8% and ~6.5%, supporting the model-predicted interface. (williams2024insightsintothe pages 5-6)
Earlier authoritative synthesis: A widely cited 2020 FEBS Journal review reported a high-affinity UGGT1–Sep15 interaction with Kd ≈ 20 nM, and that essentially the entire cellular pool of Sep15 may be UGGT1-bound (whereas UGGT1 can exist both bound and free). (Publication: Apr 2020; https://doi.org/10.1111/febs.15330) (kozlov2020calnexincycle– pages 12-14)
UGGT1 is described across multiple mammalian studies as ER-localized/ER-resident and operating in the ER lumen as part of ER protein quality control and early secretory pathway surveillance. (sagert2023theerfolding pages 1-2, ninagawa2024uggt1mediatedreglucosylationof pages 5-9)
UGGT1’s primary pathway role is within the N-glycan-dependent lectin chaperone system (CNX/CRT cycle) that retains and refolds non-native glycoproteins. (ninagawa2024uggt1mediatedreglucosylationof pages 1-5, sagert2023theerfolding pages 1-2)
Recent evidence expands UGGT1’s functional position to a decision layer that can antagonize premature degradation: UGGT1-mediated reglucosylation can delay entry into gpERAD, competing with EDEM/mannose trimming that promotes degradation. (ninagawa2024uggt1mediatedreglucosylationof pages 12-16, ninagawa2024uggt1mediatedreglucosylationof pages 5-9)
Direct mechanistic studies are largely performed in human or other mammalian cell systems, but there is experimentally grounded rat evidence for Uggt1/UGGT1 regulation at the mRNA/protein/activity levels in metabolic disease models.
A 2020 FEBS Letters study quantified UGGT1 in liver ER fractions from Zucker rat models:
- Zucker fatty (ZF) obesity vs lean controls (ZN): Uggt1 mRNA ~0.6-fold, UGGT1 protein ~0.6-fold, and UGGT1 enzymatic activity was reported as ~60% lower. (Publication: Apr 2020; https://doi.org/10.1002/1873-3468.13780) (kuribara2020metabolicsyndromeperturbs pages 5-7)
- Zucker diabetic fatty (ZDF) obese type 2 diabetes vs obese (ZF): Uggt1 mRNA ~1.7-fold higher and UGGT1 protein ~1.5-fold higher, yet enzymatic activity was ~0.5-fold compared with ZF, showing a marked abundance–activity mismatch under severe metabolic syndrome. (kuribara2020metabolicsyndromeperturbs pages 7-9, kuribara2020metabolicsyndromeperturbs pages 9-10)
Methods and rigor notes: The study measured UGGT1 activity using a fluorescent glycan substrate (M9-BODIPY) and quantified products by HPLC/fluorescence in solubilized liver ER fractions; mRNA was assayed by qPCR with β2-microglobulin normalization and protein by western blot with β-actin loading control. Reported data were mean ± SD (n=3). (kuribara2020metabolicsyndromeperturbs pages 2-5, kuribara2020metabolicsyndromeperturbs pages 7-9)
Antigen presentation quality control: The 2023 reconstitution study demonstrates a concrete immunology application: UGGT1 can be functionally integrated with MHC I peptide editing via TAPBPR, refining how antigen-presenting cells enforce quality control on peptide-receptive MHC I before export. (sagert2023theerfolding pages 8-9, sagert2023theerfolding pages 1-2)
ER proteostasis engineering and glycoprotein manufacturing relevance (mechanism-to-implementation): Quantitative mapping of UGGT1 client selectivity (71 endogenous substrates) and discovery that UGGT1 can antagonize early ERAD provide actionable principles for engineering secretion or stability of difficult-to-fold glycoproteins (e.g., choosing interventions that modulate reglucosylation vs mannose trimming). These represent enabling findings for biotechnology even when not yet deployed as standardized industrial protocols. (adams2020quantitativeglycoproteomicsreveals pages 1-4, ninagawa2024uggt1mediatedreglucosylationof pages 12-16)
Disease-model interpretation and biomolecular phenotyping: Rat metabolic syndrome models show that UGGT1 activity can be strongly decreased even when expression is increased, emphasizing that activity assays (not only transcript/protein quantification) are required to interpret ER quality control capacity in vivo. (kuribara2020metabolicsyndromeperturbs pages 7-9, kuribara2020metabolicsyndromeperturbs pages 5-7)
UGGT1 is widely conceptualized as an ER “gatekeeper” or “folding sensor” that enforces quality control of the secretory proteome via glycan reglucosylation, with SEP15 serving as a redox-active partner. This framing is reinforced by: (i) experimental reconstitution in 2023 demonstrating chaperone-dependent client processing (TAPBPR/MHC I), (ii) 2024 genetic evidence that UGGT1 actively competes with gpERAD rather than acting only as a passive “safety net,” and (iii) 2024 structure-guided mapping of the UGGT1–SEP15 interface with quantitative mutational disruption. (sagert2023theerfolding pages 1-2, ninagawa2024uggt1mediatedreglucosylationof pages 12-16, williams2024insightsintothe pages 1-2, williams2024insightsintothe pages 5-6)
The following table compiles the principal functional annotation points and quantitative findings from the evidence base used here:
| Aspect | Key details | Key sources (with year, venue) | URL |
|---|---|---|---|
| Identity | Target verified as rat Uggt1/UGGT1 (UniProt Q9JLA3), the mammalian UDP-glucose:glycoprotein glucosyltransferase 1, an ER quality-control glucosyltransferase distinct from drug-metabolizing UGT1A enzymes, UGGT2, or ceramide glucosyltransferase. It is described as a central ER folding sensor/gatekeeper for N-glycosylated proteins (sagert2023theerfolding pages 1-2, adams2020quantitativeglycoproteomicsreveals pages 1-4). | Sagert et al., 2023, eLife; Adams et al., 2020, eLife | https://doi.org/10.7554/elife.85432 ; https://doi.org/10.7554/elife.63997 |
| Reaction | UGGT1 catalyzes reglucosylation: transfer of glucose from UDP-glucose onto deglucosylated N-linked glycans, e.g. conversion of Man9GlcNAc2 to Glc1Man9GlcNAc2 on non-native glycoproteins; catalytic activity requires Ca2+ coordinated by a DxD motif (sagert2023theerfolding pages 1-2, sagert2023theerfolding pages 7-8). | Sagert et al., 2023, eLife | https://doi.org/10.7554/elife.85432 |
| Substrate specificity | UGGT1 preferentially acts on non-native/partially folded glycoproteins and prefers proteins with exposed hydrophobic regions over folded proteins. Cellular substrates are enriched for large, multidomain, heavily glycosylated proteins; UGGT1 is the dominant mammalian glucosyltransferase and shows preference toward large plasma-membrane proteins (ninagawa2024uggt1mediatedreglucosylationof pages 1-5, adams2020quantitativeglycoproteomicsreveals pages 1-4, adams2020quantitativeglycoproteomicsreveals pages 4-7). | Ninagawa et al., 2024, eLife; Adams et al., 2020, eLife | https://doi.org/10.1101/2023.10.18.562958 ; https://doi.org/10.7554/elife.63997 |
| Localization | UGGT1 is an ER-resident/ER-localized luminal enzyme in the early secretory pathway; both mammalian UGGT1 and UGGT2 are described as ER-localized glycoproteins with Endo H-sensitive N-glycans (ninagawa2024uggt1mediatedreglucosylationof pages 5-9, sagert2023theerfolding pages 1-2). | Ninagawa et al., 2024, eLife; Sagert et al., 2023, eLife | https://doi.org/10.1101/2023.10.18.562958 ; https://doi.org/10.7554/elife.85432 |
| Pathway role | UGGT1 functions in the calnexin/calreticulin (CNX/CRT) cycle, re-glucosylating misfolded glycoproteins so they can rebind lectin chaperones and avoid premature ER exit. Newer evidence indicates UGGT1 also delays glycoprotein ER-associated degradation (gpERAD), creating a “tug-of-war” between refolding and EDEM/mannose-trimming-driven degradation; proper ATF6α function depends on UGGT activity (ninagawa2024uggt1mediatedreglucosylationof pages 12-16, ninagawa2024uggt1mediatedreglucosylationof pages 1-5, ninagawa2024uggt1mediatedreglucosylationof pages 5-9, sagert2023theerfolding pages 1-2). | Ninagawa et al., 2024, eLife; Sagert et al., 2023, eLife | https://doi.org/10.1101/2023.10.18.562958 ; https://doi.org/10.7554/elife.85432 |
| Binding partners | Supported partners include TAPBPR, which promotes UGGT1-mediated reglucosylation of peptide-free MHC I, and SEP15/SELENOF, a redox-active selenoprotein that forms a stable complex with UGGT1. SEP15 binding maps largely to its N-terminal cysteine-rich domain (CRD) and a predicted SEP15-binding region (SBR) in UGGT1; prior review evidence cites high-affinity binding (Kd ~20 nM) (sagert2023theerfolding pages 8-9, williams2024insightsintothe pages 3-4, williams2024insightsintothe pages 2-3, williams2024insightsintothe pages 1-2, kozlov2020calnexincycle– pages 12-14). | Sagert et al., 2023, eLife; Williams et al., 2024, PNAS; Kozlov & Gehring, 2020, FEBS J. | https://doi.org/10.7554/elife.85432 ; https://doi.org/10.1073/pnas.2315009121 ; https://doi.org/10.1111/febs.15330 |
| Recent 2023-2024 developments | 2023: Reconstituted human-protein system showed TAPBPR is an essential mediator for UGGT1 reglucosylation of peptide-free MHC I in at least some allomorphs; UGGT1-catalyzed conversion reached about 80% saturation in the assay, and Ca2+ was required for catalysis but not for binding to the MHC I–TAPBPR complex (sagert2023theerfolding pages 8-9, sagert2023theerfolding pages 7-8). 2024: UGGT1 was shown to compete with ERAD and inhibit early degradation of unstable/misfolded glycoproteins, including ATF6α (ninagawa2024uggt1mediatedreglucosylationof pages 12-16, ninagawa2024uggt1mediatedreglucosylationof pages 5-9). 2024: AlphaFold2 plus mutagenesis/co-IP refined the UGGT1–SEP15 interface, identifying an interface of about 1,860 Å2 and validating UGGT1 interface mutants that strongly reduced SEP15 binding (williams2024insightsintothe pages 3-4, williams2024insightsintothe pages 5-6, williams2024insightsintothe pages 4-5). | Sagert et al., 2023, eLife; Ninagawa et al., 2024, eLife; Williams et al., 2024, PNAS | https://doi.org/10.7554/elife.85432 ; https://doi.org/10.1101/2023.10.18.562958 ; https://doi.org/10.1073/pnas.2315009121 |
| Rat-specific findings | Direct rat evidence is limited but present in rat liver metabolic-disease models. In Zucker fatty rats, Uggt1 mRNA, UGGT1 protein, and UGGT1 enzymatic activity are all reduced versus lean controls; in Zucker diabetic fatty rats, mRNA/protein rise relative to obese rats but enzymatic activity remains impaired, indicating discordance between abundance and function under severe metabolic stress (kuribara2020metabolicsyndromeperturbs pages 5-7, kuribara2020metabolicsyndromeperturbs pages 9-10, kuribara2020metabolicsyndromeperturbs pages 7-9, kuribara2020metabolicsyndromeperturbs pages 1-2). | Kuribara et al., 2020, FEBS Letters | https://doi.org/10.1002/1873-3468.13780 |
| Quantitative stats | Quantitative values supported by evidence include: 71 endogenous UGGT substrates identified in human cells, with a conservative 3-fold enrichment cutoff for high-confidence substrates (adams2020quantitativeglycoproteomicsreveals pages 1-4, adams2020quantitativeglycoproteomicsreveals pages 4-7); UGGT2 abundance was about 6.9% of UGGT1 in HCT116 cells and 29.8% in HeLa cells (ninagawa2024uggt1mediatedreglucosylationof pages 5-9); in the TAPBPR/MHC I system, UGGT1 reaction saturated at about 80% (sagert2023theerfolding pages 8-9); the UGGT1–SEP15 predicted interface buries about 1,860 Å2, and SEP15 co-IP with WT UGGT1 was about 27%, falling to about 3.8% or 6.5% with UGGT1 interface mutants; SELENOF knockout altered glucosylation of 26 proteins, 7 by at least 50% (williams2024insightsintothe pages 3-4, williams2024insightsintothe pages 5-6, williams2024insightsintothe pages 4-5); in rat ZF liver, Uggt1 mRNA and protein were each about 0.6-fold of lean controls and activity was about 60% lower; in ZDF versus ZF, mRNA was 1.7-fold higher and protein about 1.5-fold higher, yet activity was about 0.5-fold (kuribara2020metabolicsyndromeperturbs pages 5-7, kuribara2020metabolicsyndromeperturbs pages 7-9). | Adams et al., 2020, eLife; Sagert et al., 2023, eLife; Williams et al., 2024, PNAS; Kuribara et al., 2020, FEBS Letters | https://doi.org/10.7554/elife.63997 ; https://doi.org/10.7554/elife.85432 ; https://doi.org/10.1073/pnas.2315009121 ; https://doi.org/10.1002/1873-3468.13780 |
| Applications | Current applications are mainly mechanistic and translational rather than clinical: UGGT1 knowledge is being used to understand antigen presentation quality control (MHC I/TAPBPR), to map ER proteostasis and client selectivity, and to interpret how altered UGGT1 activity affects glycoprotein maturation and metabolic disease-associated ER quality control. These studies also support proteostasis-oriented strategies in biotechnology and disease models, but no direct rat-specific therapeutic implementation was supported in the gathered snippets (sagert2023theerfolding pages 8-9, ninagawa2024uggt1mediatedreglucosylationof pages 12-16, adams2020quantitativeglycoproteomicsreveals pages 1-4, kuribara2020metabolicsyndromeperturbs pages 5-7). | Sagert et al., 2023, eLife; Ninagawa et al., 2024, eLife; Adams et al., 2020, eLife; Kuribara et al., 2020, FEBS Letters | https://doi.org/10.7554/elife.85432 ; https://doi.org/10.1101/2023.10.18.562958 ; https://doi.org/10.7554/elife.63997 ; https://doi.org/10.1002/1873-3468.13780 |
Table: This table summarizes the supported functional annotation of rat Uggt1/UGGT1 (UniProt Q9JLA3), including biochemical function, ER quality-control role, binding partners, recent mechanistic advances, and rat-specific metabolic-disease evidence. It is useful as a compact evidence map before writing the full narrative report.
While rat-specific functional enzymology and regulation are available in liver metabolic disease models, most high-resolution mechanistic studies (client structural states, detailed glycan-product mapping, and interaction-interface mapping) are performed in human or other mammalian systems and are used here as strong, but not exclusively rat-derived, evidence for the conserved function of rat Uggt1/UGGT1. (kuribara2020metabolicsyndromeperturbs pages 5-7, sagert2023theerfolding pages 8-9, williams2024insightsintothe pages 5-6)
References
(sagert2023theerfolding pages 1-2): Lina Sagert, Christian Winter, Ina Ruppert, Maximilian Zehetmaier, Christoph Thomas, and Robert Tampé. The er folding sensor uggt1 acts on tapbpr-chaperoned peptide-free mhc i. eLife, Jan 2023. URL: https://doi.org/10.7554/elife.85432, doi:10.7554/elife.85432. This article has 8 citations and is from a domain leading peer-reviewed journal.
(adams2020quantitativeglycoproteomicsreveals pages 1-4): Benjamin M Adams, Nathan P Canniff, Kevin P Guay, Ida Signe Bohse Larsen, and Daniel N Hebert. Quantitative glycoproteomics reveals cellular substrate selectivity of the er protein quality control sensors uggt1 and uggt2. Dec 2020. URL: https://doi.org/10.7554/elife.63997, doi:10.7554/elife.63997. This article has 70 citations and is from a domain leading peer-reviewed journal.
(ninagawa2024uggt1mediatedreglucosylationof pages 5-9): Satoshi Ninagawa, Masaki Matsuo, Deng Ying, Shuichiro Oshita, Shinya Aso, Kazutoshi Matsushita, Mai Taniguchi, Akane Fueki, Moe Yamashiro, Kaoru Sugasawa, Shunsuke Saito, Koshi Imami, Yasuhiko Kizuka, Tetsushi Sakuma, Takashi Yamamoto, Hirokazu Yagi, Koichi Kato, and Kazutoshi Mori. Uggt1-mediated reglucosylation of n-glycan competes with er-associated degradation of unstable and misfolded glycoproteins. eLife, Sep 2024. URL: https://doi.org/10.1101/2023.10.18.562958, doi:10.1101/2023.10.18.562958. This article has 7 citations and is from a domain leading peer-reviewed journal.
(sagert2023theerfolding pages 7-8): Lina Sagert, Christian Winter, Ina Ruppert, Maximilian Zehetmaier, Christoph Thomas, and Robert Tampé. The er folding sensor uggt1 acts on tapbpr-chaperoned peptide-free mhc i. eLife, Jan 2023. URL: https://doi.org/10.7554/elife.85432, doi:10.7554/elife.85432. This article has 8 citations and is from a domain leading peer-reviewed journal.
(ninagawa2024uggt1mediatedreglucosylationof pages 1-5): Satoshi Ninagawa, Masaki Matsuo, Deng Ying, Shuichiro Oshita, Shinya Aso, Kazutoshi Matsushita, Mai Taniguchi, Akane Fueki, Moe Yamashiro, Kaoru Sugasawa, Shunsuke Saito, Koshi Imami, Yasuhiko Kizuka, Tetsushi Sakuma, Takashi Yamamoto, Hirokazu Yagi, Koichi Kato, and Kazutoshi Mori. Uggt1-mediated reglucosylation of n-glycan competes with er-associated degradation of unstable and misfolded glycoproteins. eLife, Sep 2024. URL: https://doi.org/10.1101/2023.10.18.562958, doi:10.1101/2023.10.18.562958. This article has 7 citations and is from a domain leading peer-reviewed journal.
(sagert2023theerfolding pages 8-9): Lina Sagert, Christian Winter, Ina Ruppert, Maximilian Zehetmaier, Christoph Thomas, and Robert Tampé. The er folding sensor uggt1 acts on tapbpr-chaperoned peptide-free mhc i. eLife, Jan 2023. URL: https://doi.org/10.7554/elife.85432, doi:10.7554/elife.85432. This article has 8 citations and is from a domain leading peer-reviewed journal.
(ninagawa2024uggt1mediatedreglucosylationof pages 12-16): Satoshi Ninagawa, Masaki Matsuo, Deng Ying, Shuichiro Oshita, Shinya Aso, Kazutoshi Matsushita, Mai Taniguchi, Akane Fueki, Moe Yamashiro, Kaoru Sugasawa, Shunsuke Saito, Koshi Imami, Yasuhiko Kizuka, Tetsushi Sakuma, Takashi Yamamoto, Hirokazu Yagi, Koichi Kato, and Kazutoshi Mori. Uggt1-mediated reglucosylation of n-glycan competes with er-associated degradation of unstable and misfolded glycoproteins. eLife, Sep 2024. URL: https://doi.org/10.1101/2023.10.18.562958, doi:10.1101/2023.10.18.562958. This article has 7 citations and is from a domain leading peer-reviewed journal.
(williams2024insightsintothe pages 3-4): Robert V. Williams, Kevin P. Guay, Owen A. Hurlbut Lesk, Eugenia M. Clerico, Daniel N. Hebert, and Lila M. Gierasch. Insights into the interaction between uggt, the gatekeeper of folding in the er, and its partner, the selenoprotein sep15. Proceedings of the National Academy of Sciences of the United States of America, Aug 2024. URL: https://doi.org/10.1073/pnas.2315009121, doi:10.1073/pnas.2315009121. This article has 11 citations and is from a highest quality peer-reviewed journal.
(williams2024insightsintothe pages 1-2): Robert V. Williams, Kevin P. Guay, Owen A. Hurlbut Lesk, Eugenia M. Clerico, Daniel N. Hebert, and Lila M. Gierasch. Insights into the interaction between uggt, the gatekeeper of folding in the er, and its partner, the selenoprotein sep15. Proceedings of the National Academy of Sciences of the United States of America, Aug 2024. URL: https://doi.org/10.1073/pnas.2315009121, doi:10.1073/pnas.2315009121. This article has 11 citations and is from a highest quality peer-reviewed journal.
(williams2024insightsintothe pages 5-6): Robert V. Williams, Kevin P. Guay, Owen A. Hurlbut Lesk, Eugenia M. Clerico, Daniel N. Hebert, and Lila M. Gierasch. Insights into the interaction between uggt, the gatekeeper of folding in the er, and its partner, the selenoprotein sep15. Proceedings of the National Academy of Sciences of the United States of America, Aug 2024. URL: https://doi.org/10.1073/pnas.2315009121, doi:10.1073/pnas.2315009121. This article has 11 citations and is from a highest quality peer-reviewed journal.
(kozlov2020calnexincycle– pages 12-14): Guennadi Kozlov and Kalle Gehring. Calnexin cycle – structural features of the er chaperone system. The FEBS Journal, 287:4322-4340, Apr 2020. URL: https://doi.org/10.1111/febs.15330, doi:10.1111/febs.15330. This article has 233 citations.
(kuribara2020metabolicsyndromeperturbs pages 5-7): Taiki Kuribara, Ayami Imagawa, Makoto Hirano, Yukishige Ito, and Kiichiro Totani. Metabolic syndrome perturbs deglucosylation and reglucosylation in the glycoprotein folding cycle. FEBS Letters, 594:1759-1769, Apr 2020. URL: https://doi.org/10.1002/1873-3468.13780, doi:10.1002/1873-3468.13780. This article has 11 citations and is from a peer-reviewed journal.
(kuribara2020metabolicsyndromeperturbs pages 7-9): Taiki Kuribara, Ayami Imagawa, Makoto Hirano, Yukishige Ito, and Kiichiro Totani. Metabolic syndrome perturbs deglucosylation and reglucosylation in the glycoprotein folding cycle. FEBS Letters, 594:1759-1769, Apr 2020. URL: https://doi.org/10.1002/1873-3468.13780, doi:10.1002/1873-3468.13780. This article has 11 citations and is from a peer-reviewed journal.
(kuribara2020metabolicsyndromeperturbs pages 9-10): Taiki Kuribara, Ayami Imagawa, Makoto Hirano, Yukishige Ito, and Kiichiro Totani. Metabolic syndrome perturbs deglucosylation and reglucosylation in the glycoprotein folding cycle. FEBS Letters, 594:1759-1769, Apr 2020. URL: https://doi.org/10.1002/1873-3468.13780, doi:10.1002/1873-3468.13780. This article has 11 citations and is from a peer-reviewed journal.
(kuribara2020metabolicsyndromeperturbs pages 2-5): Taiki Kuribara, Ayami Imagawa, Makoto Hirano, Yukishige Ito, and Kiichiro Totani. Metabolic syndrome perturbs deglucosylation and reglucosylation in the glycoprotein folding cycle. FEBS Letters, 594:1759-1769, Apr 2020. URL: https://doi.org/10.1002/1873-3468.13780, doi:10.1002/1873-3468.13780. This article has 11 citations and is from a peer-reviewed journal.
(adams2020quantitativeglycoproteomicsreveals pages 4-7): Benjamin M Adams, Nathan P Canniff, Kevin P Guay, Ida Signe Bohse Larsen, and Daniel N Hebert. Quantitative glycoproteomics reveals cellular substrate selectivity of the er protein quality control sensors uggt1 and uggt2. Dec 2020. URL: https://doi.org/10.7554/elife.63997, doi:10.7554/elife.63997. This article has 70 citations and is from a domain leading peer-reviewed journal.
(williams2024insightsintothe pages 2-3): Robert V. Williams, Kevin P. Guay, Owen A. Hurlbut Lesk, Eugenia M. Clerico, Daniel N. Hebert, and Lila M. Gierasch. Insights into the interaction between uggt, the gatekeeper of folding in the er, and its partner, the selenoprotein sep15. Proceedings of the National Academy of Sciences of the United States of America, Aug 2024. URL: https://doi.org/10.1073/pnas.2315009121, doi:10.1073/pnas.2315009121. This article has 11 citations and is from a highest quality peer-reviewed journal.
(williams2024insightsintothe pages 4-5): Robert V. Williams, Kevin P. Guay, Owen A. Hurlbut Lesk, Eugenia M. Clerico, Daniel N. Hebert, and Lila M. Gierasch. Insights into the interaction between uggt, the gatekeeper of folding in the er, and its partner, the selenoprotein sep15. Proceedings of the National Academy of Sciences of the United States of America, Aug 2024. URL: https://doi.org/10.1073/pnas.2315009121, doi:10.1073/pnas.2315009121. This article has 11 citations and is from a highest quality peer-reviewed journal.
(kuribara2020metabolicsyndromeperturbs pages 1-2): Taiki Kuribara, Ayami Imagawa, Makoto Hirano, Yukishige Ito, and Kiichiro Totani. Metabolic syndrome perturbs deglucosylation and reglucosylation in the glycoprotein folding cycle. FEBS Letters, 594:1759-1769, Apr 2020. URL: https://doi.org/10.1002/1873-3468.13780, doi:10.1002/1873-3468.13780. This article has 11 citations and is from a peer-reviewed journal.