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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
Plan
Objective 1. Verify identity and resolve ambiguities. Completed by cross-referencing 2024 mechanistic and molecular characterizations that explicitly study human RFT1 and its yeast/human orthology relationships, confirming the human ER protein RFT1 with polytopic topology, and by aligning mechanistic role and domains with RFT1/MOP family features (see Evidence). (hirata2024molecularcharacterizationof pages 1-3, hirata2024molecularcharacterizationof pages 8-10)
Objective 2–5. Curate primary literature, recent developments, disease relevance, and expert analysis; emphasize 2023–2024 sources. Achieved via 2024 Nature Communications (direct reconstitution) and 2024 molecular characterization, complemented by clinical/diagnostic primary literature and systematic reviews. (chen2024rft1catalyzeslipidlinked pages 2-3, chen2024rft1catalyzeslipidlinked pages 4-4, chen2024rft1catalyzeslipidlinked pages 5-6, hirata2024molecularcharacterizationof pages 1-3, vleugels2009rft1deficiencyin pages 1-3, colantuono2021liverinvolvementin pages 6-8, vleugels2009rft1deficiencyin pages 3-4)
Objective 6. Create a concise artifact table summarizing key facts. See embedded artifact.
Objective 7. Synthesize the full research report with citations and URLs. Submitted below.
| Aspect | Key details | Primary sources (year, DOI/URL) |
|---|---|---|
| Identity (gene/protein, organism, family/domain) | Human RFT1 (UniProt Q96AA3), member of the RFT1/MOP transporter family; polytopic membrane protein implicated in LLO translocation. | 2024, Chen et al., DOI: https://doi.org/10.1038/s41467-024-48999-3 (chen2024rft1catalyzeslipidlinked pages 2-3); 2024, Hirata et al., DOI: https://doi.org/10.1101/2024.04.03.587922 (hirata2024molecularcharacterizationof pages 1-3) |
| Subcellular localization & topology | Endoplasmic reticulum (ER) resident; predicted ~14 transmembrane spans with both N- and C-termini cytosolic; not N-glycosylated. | 2024, Hirata et al., DOI: https://doi.org/10.1101/2024.04.03.587922 (hirata2024molecularcharacterizationof pages 8-10, hirata2024molecularcharacterizationof pages 22-26) |
| Primary molecular function & substrate specificity | Catalyzes translocation (flipping) of Man5GlcNAc2-PP-dolichol (M5GN2-PP-Dol/Phy) across the ER membrane; shows selectivity for M5 over M3 intermediates. | 2024, Chen et al., DOI: https://doi.org/10.1038/s41467-024-48999-3 (chen2024rft1catalyzeslipidlinked pages 2-3, chen2024rft1catalyzeslipidlinked pages 4-4, chen2024rft1catalyzeslipidlinked pages 5-6); mechanistic/topology context (hirata2024molecularcharacterizationof pages 1-3) |
| Pathway role (N-glycosylation step/mechanism) | Performs the cytosolic-to-lumenal translocation of the heptasaccharide intermediate (M5GN2-PP-Dol), enabling lumenal extension to Glc3Man9GlcNAc2-PP-Dol and subsequent OST-mediated transfer to nascent proteins. | 2024, Chen et al., DOI: https://doi.org/10.1038/s41467-024-48999-3 (chen2024rft1catalyzeslipidlinked pages 2-3); pathway context and reviews (hirata2024molecularcharacterizationof pages 1-3) |
| 2023–2024 developments resolving flippase controversy | 2024 reconstitution with purified Rft1 (and archaeal orthologue) demonstrated direct M5GN2-PP flipping (Nature Communications), while parallel 2024 molecular work characterized Rft1 topology and noted prior reconstitution assays where removal of Rft1 did not abolish bulk scramblase activity — together they provide direct biochemical proof of activity yet explain earlier discrepant results (differences in assay systems, abundance, suppressor bypass). | 2024, Chen et al., DOI: https://doi.org/10.1038/s41467-024-48999-3 (chen2024rft1catalyzeslipidlinked pages 2-3); 2024, Hirata et al., DOI: https://doi.org/10.1101/2024.04.03.587922 (hirata2024molecularcharacterizationof pages 3-5, hirata2024molecularcharacterizationof pages 7-8, hirata2024molecularcharacterizationof pages 22-26) |
| Experimental evidence types | Genetic complementation (yeast/plasmid-shuffle), patient fibroblast complementation, biochemical reconstitution in proteoliposomes with purified protein and UPLC-MS mannosidase readout, LLO profiling/HPLC, structural modeling (AlphaFold2), yeast functional assays (CPY glycosylation). | 2024, Chen et al., DOI: https://doi.org/10.1038/s41467-024-48999-3 (chen2024rft1catalyzeslipidlinked pages 2-3); 2024, Hirata et al., DOI: https://doi.org/10.1101/2024.04.03.587922; 2009, Vleugels et al., DOI: https://doi.org/10.1002/humu.21085 (vleugels2009rft1deficiencyin pages 1-3) |
| Disease association (RFT1-CDG) & hallmark phenotypes | Autosomal recessive RFT1-CDG (OMIM 612015): early-onset multisystem CDG dominated by severe neurodevelopmental disease (intractable epilepsy/epileptic encephalopathy, developmental delay, hypotonia), sensorineural deafness, feeding/respiratory problems, variable hepatic involvement. | 2009, Vleugels et al., DOI: https://doi.org/10.1002/humu.21085 (vleugels2009rft1deficiencyin pages 1-3); 2021, Colantuono et al., DOI: https://doi.org/10.1097/mpg.0000000000003209 (colantuono2021liverinvolvementin pages 6-8); 2024 review/compilation (hirata2024molecularcharacterizationof pages 40-41) |
| Diagnostics (transferrin IEF, LLO profiling, functional rescue) | Typical diagnostic findings: type I transferrin (serum) pattern; LLO profiling/HPLC or radiolabel shows accumulation of Man5GlcNAc2-PP-dolichol; functional rescue of patient fibroblast defects by expression of WT RFT1 (restores LLO profile and glycoprotein secretion). | 2009, Vleugels et al., DOI: https://doi.org/10.1002/humu.21085 (vleugels2009rft1deficiencyin pages 3-4, vleugels2009rft1deficiencyin pages 11-13, vleugels2009rft1deficiencyin pages 1-3) |
| Epidemiology / reported cases | Rare: initial series described 3 novel patients (2009) plus earlier index cases; later reviews note ~9 patients reported in some compilations — overall case count remains small and heterogeneous across reports. | 2009, Vleugels et al., DOI: https://doi.org/10.1002/humu.21085 (vleugels2009rft1deficiencyin pages 1-3); 2021, Colantuono et al. systematic review (colantuono2021liverinvolvementin pages 6-8); 2024 molecular review (hirata2024molecularcharacterizationof pages 40-41) |
| Applications / implications (diagnostics, biotechnology) | Clinical: inclusion in CDG diagnostic panels, transferrin/LLO testing, genotype-based counseling; Research/biotech: mechanistic model for flippase/MOP family transporters, target for glycoengineering studies and understanding LLO biogenesis; purified Rft1 enables mechanistic assays and potential screening. | 2024, Chen et al., DOI: https://doi.org/10.1038/s41467-024-48999-3 (chen2024rft1catalyzeslipidlinked pages 2-3); 2024, Hirata et al., DOI: https://doi.org/10.1101/2024.04.03.587922 (hirata2024molecularcharacterizationof pages 1-3) |
Table: Concise, cited summary of key properties, function, evidence, disease links, diagnostics, and recent 2024 advances for human RFT1 (UniProt Q96AA3). This table compiles experimental and clinical sources to support functional annotation and translational relevance.
Comprehensive research report: Human RFT1 (UniProt Q96AA3)
1) Key concepts and definitions
• Identity and family: RFT1 (HGNC:30220) encodes a multi-pass ER membrane protein required for lipid-linked oligosaccharide (LLO) biogenesis in the N-glycosylation pathway. Recent structural homology and AlphaFold2 modeling place human RFT1 within the broader MOP (multidrug/oligosaccharidyl-lipid/polysaccharide) transporter superfamily that includes bacterial lipid II flippase MurJ, consistent with a transporter/scaffold for a large amphipathic lipid-linked glycan substrate (predicted ~14 TMs, cytosolic N- and C-termini). (Hirata et al., 2024; URL: https://doi.org/10.1101/2024.04.03.587922) (hirata2024molecularcharacterizationof pages 7-8, hirata2024molecularcharacterizationof pages 8-10)
• Primary substrate: the N-glycosylation intermediate Man5GlcNAc2-PP-dolichol (abbreviated M5GN2-PP-Dol or M5-DLO), which must move from the cytosolic to the luminal leaflet of the ER membrane to complete LLO assembly. (Chen et al., 2024; URL: https://doi.org/10.1038/s41467-024-48999-3) (chen2024rft1catalyzeslipidlinked pages 2-3)
• Pathway context: Synthesis of Glc3Man9GlcNAc2-PP-dolichol proceeds in two stages; the cytosolic heptasaccharide intermediate M5GN2-PP-Dol is flipped to the ER lumen where elongation yields Glc3Man9GlcNAc2-PP-Dol for transfer to nascent polypeptides by the OST complex. (Chen et al., 2024; URL: https://doi.org/10.1038/s41467-024-48999-3) (chen2024rft1catalyzeslipidlinked pages 2-3)
2) Molecular function, mechanism, localization, and topology
• Subcellular localization and topology: Human RFT1 localizes throughout the ER. DeepTMHMM and experimental tagging/topology mapping indicate ~14 transmembrane spans with both N- and C-termini facing the cytosol; the single canonical N-glycosylation sequon lies in an intracellular loop, and the protein is not N-glycosylated. (Hirata et al., 2024; URL: https://doi.org/10.1101/2024.04.03.587922) (hirata2024molecularcharacterizationof pages 7-8, hirata2024molecularcharacterizationof pages 22-26, hirata2024molecularcharacterizationof pages 8-10)
• Primary function and specificity: Purified human RFT1 directly catalyzes the transbilayer movement of M5GN2-PP-Dol (and the analogous phytanyl carrier substrate), with strong selectivity for M5 over shorter M3 intermediates in a fully reconstituted proteoliposome assay using an α-mannosidase/UPLC-MS readout. (Chen et al., 2024; URL: https://doi.org/10.1038/s41467-024-48999-3) (chen2024rft1catalyzeslipidlinked pages 4-4, chen2024rft1catalyzeslipidlinked pages 5-6)
• Mechanistic notes: Structural modeling predicts an inward-open, alternating-access–like transporter cavity containing conserved charged residues (e.g., R37, R63, R290, R442, E260) where many RFT1-CDG mutations map, consistent with a substrate-binding/translocation role for a large pyrophosphoryl-oligosaccharide lipid. (Hirata et al., 2024; URL: https://doi.org/10.1101/2024.04.03.587922) (hirata2024molecularcharacterizationof pages 8-10)
3) Recent developments and latest research (2023–2024)
• Definitive biochemical reconstitution: A major 2024 development resolved the long-standing controversy by demonstrating that purified Rft1 (yeast and human) is sufficient to catalyze M5GN2-PP-Dol translocation across membranes. Archaeal Agl23 also flips the same substrate, showing evolutionary conservation. These assays achieved ~90% conversion of M5GN2 to a diagnostic M3GN2 product accessible to exogenous mannosidase within 2 hours, while control liposomes or membrane fractions from an rft1Δ suppressor strain lacked activity. (Chen et al., 2024; URL: https://doi.org/10.1038/s41467-024-48999-3) (chen2024rft1catalyzeslipidlinked pages 4-4, chen2024rft1catalyzeslipidlinked pages 5-6)
• Molecular/structural characterization: Parallel 2024 work defined human RFT1 ER topology, quantified expression and glycosylation effects in yeast complementation, mapped conserved residues required for viability and N-glycosylation, and placed RFT1 in the MOP transporter superfamily. The same study reconciled prior biochemical observations where bulk M5-DLO scrambling persisted after Rft1 depletion by noting abundance differences and potential bypass/suppressor mechanisms; they emphasized the need for purified protein reconstitution (delivered by Chen et al. 2024). (Hirata et al., 2024; URL: https://doi.org/10.1101/2024.04.03.587922) (hirata2024molecularcharacterizationof pages 7-8, hirata2024molecularcharacterizationof pages 22-26, hirata2024molecularcharacterizationof pages 3-5)
4) Experimental evidence base
• Genetic complementation: Human RFT1 functionally replaces yeast Rft1 in viability and glycosylation assays; disease-residue variants define critical positions for function and growth. (Hirata et al., 2024; URL: https://doi.org/10.1101/2024.04.03.587922) (hirata2024molecularcharacterizationof pages 8-10)
• Biochemical reconstitution (purified protein): Direct flipping of M5GN2-PP-Dol/Phy by purified Rft1 in proteoliposomes with mannosidase-coupled UPLC-MS readout; selectivity for M5 over M3. (Chen et al., 2024; URL: https://doi.org/10.1038/s41467-024-48999-3) (chen2024rft1catalyzeslipidlinked pages 4-4, chen2024rft1catalyzeslipidlinked pages 5-6)
• Patient-cell functional rescue and LLO profiling: In RFT1-CDG fibroblasts, wild-type RFT1 cDNA corrects accumulated M5GN2-PP-Dol and restores secretion of a glycoprotein reporter (DNase I), establishing causality. (Vleugels et al., 2009; URL: https://doi.org/10.1002/humu.21085) (vleugels2009rft1deficiencyin pages 1-3, vleugels2009rft1deficiencyin pages 11-13)
5) Role in the N-glycosylation pathway
• Step: RFT1 flips the cytosolic M5GN2-PP-Dol intermediate into the ER lumen for elongation to Glc3Man9GlcNAc2-PP-Dol and downstream OST-mediated transfer to nascent polypeptides. (Chen et al., 2024; URL: https://doi.org/10.1038/s41467-024-48999-3) (chen2024rft1catalyzeslipidlinked pages 2-3)
• Pathway consequences of deficiency: Patient cells accumulate M5GN2-PP-Dol in the LLO pool with paucity of fully assembled LLO, leading to hypoglycosylation of proteins. (Vleugels et al., 2009; URL: https://doi.org/10.1002/humu.21085) (vleugels2009rft1deficiencyin pages 1-3, vleugels2009rft1deficiencyin pages 3-4)
6) Disease associations, phenotypes, and statistics
• Disorder: RFT1-CDG (OMIM 612015), an autosomal recessive congenital disorder of N-linked glycosylation. (Vleugels et al., 2009; URL: https://doi.org/10.1002/humu.21085) (vleugels2009rft1deficiencyin pages 6-7)
• Clinical spectrum (representative): severe neurodevelopmental disease (global developmental delay, hypotonia), intractable epilepsy including epileptic encephalopathy in infancy, universal sensorineural deafness in early series, feeding difficulties with aspiration, respiratory complications, and variable organ involvement (e.g., hepatomegaly reported; some series noted normal liver function). (Vleugels et al., 2009; URL: https://doi.org/10.1002/humu.21085; Colantuono et al., 2021; URL: https://doi.org/10.1097/mpg.0000000000003209) (vleugels2009rft1deficiencyin pages 4-6, vleugels2009rft1deficiencyin pages 6-7, colantuono2021liverinvolvementin pages 6-8)
• Reported case counts: Early clinical/molecular reports documented four total patients (three novel plus the index case). A later systematic review referenced “some of the nine patients reported” with RFT1-CDG features, indicating a total reported cohort on the order of single digits to low double digits in the literature at that time; overall, RFT1-CDG remains rare with few documented cases. (Vleugels et al., 2009; URL: https://doi.org/10.1002/humu.21085; Colantuono et al., 2021; URL: https://doi.org/10.1097/mpg.0000000000003209) (vleugels2009rft1deficiencyin pages 1-3, colantuono2021liverinvolvementin pages 6-8)
7) Diagnostics and real-world implementations
• Screening and confirmation: A Type I transferrin isoelectric focusing (IEF) pattern is typical of CDG-I defects. In RFT1-CDG, LLO profiling by radiolabel/HPLC demonstrates accumulation of M5GN2-PP-Dol with little fully assembled LLO and absence of M5GN2 on protein-linked glycans. Functional rescue by WT RFT1 in patient fibroblasts restores LLO composition and improves glycoprotein secretion (DNase I), supporting pathogenicity. These approaches inform clinical and research diagnostics. (Vleugels et al., 2009; URL: https://doi.org/10.1002/humu.21085) (vleugels2009rft1deficiencyin pages 3-4, vleugels2009rft1deficiencyin pages 11-13, vleugels2009rft1deficiencyin pages 1-3)
• Organ involvement in practice: Reviews emphasize neurological dominance, with reported hepatomegaly in some cases; phenotypes are heterogeneous, underscoring the utility of combined biochemical and genomic testing in suspected CDG. (Colantuono et al., 2021; URL: https://doi.org/10.1097/mpg.0000000000003209) (colantuono2021liverinvolvementin pages 6-8)
8) Expert analyses and interpretation
• Resolution of the “RFT1 flippase” controversy: 2024 purified-protein reconstitution provides direct biochemical evidence that Rft1 catalyzes M5GN2-PP-Dol flipping across membranes, reconciling earlier results where Rft1 depletion did not abolish bulk flipping in microsomes (likely due to suppressor/bypass and protein abundance issues). Structural/topological mapping supports a transporter mechanism aligned with MOP family principles and locates CDG mutations to a central cavity, strengthening the direct-actor model. (Chen et al., 2024; URL: https://doi.org/10.1038/s41467-024-48999-3; Hirata et al., 2024; URL: https://doi.org/10.1101/2024.04.03.587922) (chen2024rft1catalyzeslipidlinked pages 4-4, chen2024rft1catalyzeslipidlinked pages 5-6, hirata2024molecularcharacterizationof pages 7-8, hirata2024molecularcharacterizationof pages 8-10, hirata2024molecularcharacterizationof pages 22-26)
• Pathophysiology: Failure to flip M5GN2-PP-Dol impairs LLO completion, reducing N-glycosylation efficiency. The hallmark biochemical lesion—M5GN2-PP-Dol accumulation with paucity of mature LLO—correlates with hypoglycosylation-dependent clinical phenotypes in RFT1-CDG. (Vleugels et al., 2009; URL: https://doi.org/10.1002/humu.21085) (vleugels2009rft1deficiencyin pages 1-3, vleugels2009rft1deficiencyin pages 3-4)
9) Applications and implications
• Diagnostics: Incorporate RFT1 into gene panels for CDG; use transferrin IEF as an initial screen, followed by LLO profiling and functional complementation where feasible. (Vleugels et al., 2009; URL: https://doi.org/10.1002/humu.21085) (vleugels2009rft1deficiencyin pages 3-4, vleugels2009rft1deficiencyin pages 11-13)
• Biotechnology and basic science: The availability of purified active Rft1 enables mechanistic biochemistry on substrate recognition and transport, guiding design of reconstituted glycosylation systems and informing glycoengineering strategies that depend on LLO supply and quality. The evolutionary conservation (archaeal suppressor/ortholog activity) invites comparative studies of MOP transporters. (Chen et al., 2024; URL: https://doi.org/10.1038/s41467-024-48999-3) (chen2024rft1catalyzeslipidlinked pages 2-3, chen2024rft1catalyzeslipidlinked pages 5-6)
Mandatory verification summary
• Gene symbol/protein match: Studied protein is human RFT1, consistent with the UniProt Q96AA3 description and the literature (ER polytopic protein that mediates M5GN2-PP-Dol translocation). (Hirata et al., 2024; Chen et al., 2024) (hirata2024molecularcharacterizationof pages 1-3, chen2024rft1catalyzeslipidlinked pages 2-3)
• Organism: Homo sapiens; cross-species complementation confirms orthology with yeast Rft1; human RFT1 rescues yeast rft1 deficiency. (Hirata et al., 2024) (hirata2024molecularcharacterizationof pages 22-26)
• Family/domains: RFT1 shows predicted MOP superfamily features with a central hydrophilic cavity; many pathogenic variants map to conserved residues in this region. (Hirata et al., 2024) (hirata2024molecularcharacterizationof pages 8-10)
• Ambiguity check: No conflicting gene symbol usage impacting humans was identified in the curated sources; where earlier literature questioned direct flippase activity, 2024 purified-protein assays now support a direct catalytic role for RFT1. (Chen et al., 2024; Hirata et al., 2024) (chen2024rft1catalyzeslipidlinked pages 4-4, hirata2024molecularcharacterizationof pages 7-8)
References (URLs and dates)
• Chen S. et al. Rft1 catalyzes lipid-linked oligosaccharide translocation across the ER membrane. Nature Communications. 2024-06. URL: https://doi.org/10.1038/s41467-024-48999-3 (chen2024rft1catalyzeslipidlinked pages 2-3, chen2024rft1catalyzeslipidlinked pages 4-4, chen2024rft1catalyzeslipidlinked pages 5-6)
• Hirata E. et al. Molecular characterization of Rft1, an ER membrane protein associated with congenital disorder of glycosylation RFT1-CDG. 2024-04 (preprint/revised for JBC). URL: https://doi.org/10.1101/2024.04.03.587922 (hirata2024molecularcharacterizationof pages 1-3, hirata2024molecularcharacterizationof pages 7-8, hirata2024molecularcharacterizationof pages 22-26, hirata2024molecularcharacterizationof pages 8-10, hirata2024molecularcharacterizationof pages 40-41)
• Vleugels W. et al. RFT1 deficiency in three novel CDG patients. Human Mutation. 2009-10. URL: https://doi.org/10.1002/humu.21085 (vleugels2009rft1deficiencyin pages 1-3, vleugels2009rft1deficiencyin pages 4-6, vleugels2009rft1deficiencyin pages 6-7, vleugels2009rft1deficiencyin pages 11-13, vleugels2009rft1deficiencyin pages 3-4)
• Colantuono R. et al. Liver involvement in congenital disorders of glycosylation: a systematic review. JPGN. 2021-06. URL: https://doi.org/10.1097/mpg.0000000000003209 (colantuono2021liverinvolvementin pages 6-8)
References
(hirata2024molecularcharacterizationof pages 1-3): Eri Hirata, Ken-taro Sakata, Grace I. Dearden, Faria Noor, Indu Menon, George N. Chiduza, and Anant K. Menon. Molecular characterization of rft1, an er membrane protein associated with congenital disorder of glycosylation rft1-cdg. The Journal of Biological Chemistry, Apr 2024. URL: https://doi.org/10.1101/2024.04.03.587922, doi:10.1101/2024.04.03.587922. This article has 4 citations.
(hirata2024molecularcharacterizationof pages 8-10): Eri Hirata, Ken-taro Sakata, Grace I. Dearden, Faria Noor, Indu Menon, George N. Chiduza, and Anant K. Menon. Molecular characterization of rft1, an er membrane protein associated with congenital disorder of glycosylation rft1-cdg. The Journal of Biological Chemistry, Apr 2024. URL: https://doi.org/10.1101/2024.04.03.587922, doi:10.1101/2024.04.03.587922. This article has 4 citations.
(chen2024rft1catalyzeslipidlinked pages 2-3): Shuai Chen, Cai-Xia Pei, Si Xu, Hanjie Li, Yi-Shi liu, Yicheng Wang, Cheng Jin, Neta Dean, and Xiao-Dong Gao. Rft1 catalyzes lipid-linked oligosaccharide translocation across the er membrane. Nature Communications, Jun 2024. URL: https://doi.org/10.1038/s41467-024-48999-3, doi:10.1038/s41467-024-48999-3. This article has 15 citations and is from a highest quality peer-reviewed journal.
(chen2024rft1catalyzeslipidlinked pages 4-4): Shuai Chen, Cai-Xia Pei, Si Xu, Hanjie Li, Yi-Shi liu, Yicheng Wang, Cheng Jin, Neta Dean, and Xiao-Dong Gao. Rft1 catalyzes lipid-linked oligosaccharide translocation across the er membrane. Nature Communications, Jun 2024. URL: https://doi.org/10.1038/s41467-024-48999-3, doi:10.1038/s41467-024-48999-3. This article has 15 citations and is from a highest quality peer-reviewed journal.
(chen2024rft1catalyzeslipidlinked pages 5-6): Shuai Chen, Cai-Xia Pei, Si Xu, Hanjie Li, Yi-Shi liu, Yicheng Wang, Cheng Jin, Neta Dean, and Xiao-Dong Gao. Rft1 catalyzes lipid-linked oligosaccharide translocation across the er membrane. Nature Communications, Jun 2024. URL: https://doi.org/10.1038/s41467-024-48999-3, doi:10.1038/s41467-024-48999-3. This article has 15 citations and is from a highest quality peer-reviewed journal.
(vleugels2009rft1deficiencyin pages 1-3): Wendy Vleugels, Micha A. Haeuptle, Bobby G. Ng, Jean-Claude Michalski, Roberta Battini, Carlo Dionisi-Vici, Mark D. Ludman, Jaak Jaeken, François Foulquier, Hudson H. Freeze, Gert Matthijs, and Thierry Hennet. Rft1 deficiency in three novel cdg patients. Human Mutation, 30:1428-1434, Oct 2009. URL: https://doi.org/10.1002/humu.21085, doi:10.1002/humu.21085. This article has 44 citations and is from a domain leading peer-reviewed journal.
(colantuono2021liverinvolvementin pages 6-8): Rossella Colantuono, Elisa D’Acunto, Daniela Melis, Pietro Vajro, Hudson H. Freeze, and Claudia Mandato. Liver involvement in congenital disorders of glycosylation: a systematic review. Journal of Pediatric Gastroenterology and Nutrition, 73:444-454, Jun 2021. URL: https://doi.org/10.1097/mpg.0000000000003209, doi:10.1097/mpg.0000000000003209. This article has 12 citations and is from a peer-reviewed journal.
(vleugels2009rft1deficiencyin pages 3-4): Wendy Vleugels, Micha A. Haeuptle, Bobby G. Ng, Jean-Claude Michalski, Roberta Battini, Carlo Dionisi-Vici, Mark D. Ludman, Jaak Jaeken, François Foulquier, Hudson H. Freeze, Gert Matthijs, and Thierry Hennet. Rft1 deficiency in three novel cdg patients. Human Mutation, 30:1428-1434, Oct 2009. URL: https://doi.org/10.1002/humu.21085, doi:10.1002/humu.21085. This article has 44 citations and is from a domain leading peer-reviewed journal.
(hirata2024molecularcharacterizationof pages 22-26): Eri Hirata, Ken-taro Sakata, Grace I. Dearden, Faria Noor, Indu Menon, George N. Chiduza, and Anant K. Menon. Molecular characterization of rft1, an er membrane protein associated with congenital disorder of glycosylation rft1-cdg. The Journal of Biological Chemistry, Apr 2024. URL: https://doi.org/10.1101/2024.04.03.587922, doi:10.1101/2024.04.03.587922. This article has 4 citations.
(hirata2024molecularcharacterizationof pages 3-5): Eri Hirata, Ken-taro Sakata, Grace I. Dearden, Faria Noor, Indu Menon, George N. Chiduza, and Anant K. Menon. Molecular characterization of rft1, an er membrane protein associated with congenital disorder of glycosylation rft1-cdg. The Journal of Biological Chemistry, Apr 2024. URL: https://doi.org/10.1101/2024.04.03.587922, doi:10.1101/2024.04.03.587922. This article has 4 citations.
(hirata2024molecularcharacterizationof pages 7-8): Eri Hirata, Ken-taro Sakata, Grace I. Dearden, Faria Noor, Indu Menon, George N. Chiduza, and Anant K. Menon. Molecular characterization of rft1, an er membrane protein associated with congenital disorder of glycosylation rft1-cdg. The Journal of Biological Chemistry, Apr 2024. URL: https://doi.org/10.1101/2024.04.03.587922, doi:10.1101/2024.04.03.587922. This article has 4 citations.
(hirata2024molecularcharacterizationof pages 40-41): Eri Hirata, Ken-taro Sakata, Grace I. Dearden, Faria Noor, Indu Menon, George N. Chiduza, and Anant K. Menon. Molecular characterization of rft1, an er membrane protein associated with congenital disorder of glycosylation rft1-cdg. The Journal of Biological Chemistry, Apr 2024. URL: https://doi.org/10.1101/2024.04.03.587922, doi:10.1101/2024.04.03.587922. This article has 4 citations.
(vleugels2009rft1deficiencyin pages 11-13): Wendy Vleugels, Micha A. Haeuptle, Bobby G. Ng, Jean-Claude Michalski, Roberta Battini, Carlo Dionisi-Vici, Mark D. Ludman, Jaak Jaeken, François Foulquier, Hudson H. Freeze, Gert Matthijs, and Thierry Hennet. Rft1 deficiency in three novel cdg patients. Human Mutation, 30:1428-1434, Oct 2009. URL: https://doi.org/10.1002/humu.21085, doi:10.1002/humu.21085. This article has 44 citations and is from a domain leading peer-reviewed journal.
(vleugels2009rft1deficiencyin pages 6-7): Wendy Vleugels, Micha A. Haeuptle, Bobby G. Ng, Jean-Claude Michalski, Roberta Battini, Carlo Dionisi-Vici, Mark D. Ludman, Jaak Jaeken, François Foulquier, Hudson H. Freeze, Gert Matthijs, and Thierry Hennet. Rft1 deficiency in three novel cdg patients. Human Mutation, 30:1428-1434, Oct 2009. URL: https://doi.org/10.1002/humu.21085, doi:10.1002/humu.21085. This article has 44 citations and is from a domain leading peer-reviewed journal.
(vleugels2009rft1deficiencyin pages 4-6): Wendy Vleugels, Micha A. Haeuptle, Bobby G. Ng, Jean-Claude Michalski, Roberta Battini, Carlo Dionisi-Vici, Mark D. Ludman, Jaak Jaeken, François Foulquier, Hudson H. Freeze, Gert Matthijs, and Thierry Hennet. Rft1 deficiency in three novel cdg patients. Human Mutation, 30:1428-1434, Oct 2009. URL: https://doi.org/10.1002/humu.21085, doi:10.1002/humu.21085. This article has 44 citations and is from a domain leading peer-reviewed journal.