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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
The target gene/protein in this report is human MAN1B1, encoding endoplasmic reticulum α-1,2-mannosidase I (ERManI), a type II membrane class I α1,2-mannosidase of the glycosyl hydrolase 47 (GH47) family. This identity (MAN1B1 ⇔ ERManI) and architecture (N-terminal cytosolic tail, TM helix, luminal catalytic domain) are explicitly described in mechanistic studies on human Man1b1/ERManI. (pan2011golgilocalizationof pages 1-2, sun2020thecytoplasmictail pages 1-3)
Key canonical references used for gene/protein verification and function:
- Pan et al., Molecular Biology of the Cell (2011-08). https://doi.org/10.1091/mbc.e11-02-0118 (pan2011golgilocalizationof pages 1-2)
- Benyair et al., Molecular Biology of the Cell (2015-01). https://doi.org/10.1091/mbc.e14-06-1152 (benyair2015mammalianermannosidase pages 1-2)
- Sun et al., PNAS (2020-09). https://doi.org/10.1073/pnas.1919013117 (sun2020thecytoplasmictail pages 1-1)
- Rymen et al., PLoS Genetics (2013-12). https://doi.org/10.1371/journal.pgen.1003989 (rymen2013man1b1deficiencyan pages 1-2)
MAN1B1/ERManI is a class I α1,2-mannosidase that cleaves α1,2-linked mannose residues from high-mannose N-glycans. In the context of N-glycan processing and quality control, it is widely implicated in generating demannosylated glycan structures that can serve as sorting signals for misfolded glycoprotein disposal. (pan2011golgilocalizationof pages 2-3, benyair2015mammalianermannosidase pages 1-2)
A central and clinically relevant activity attributed to MAN1B1 is trimming Man9GlcNAc2 → Man8GlcNAc2 isomer B by removing the terminal mannose on the middle (B) branch, which has been described as a recognized degradation-related signal. (rymen2013man1b1deficiencyan pages 1-2, benyair2015mammalianermannosidase pages 1-2)
Benyair et al. further report that ERManI trims α1,2-linked mannose residues with preference for the B-branch terminal mannose, supporting a branch preference relevant to ER quality control timing. (benyair2015mammalianermannosidase pages 1-2, benyair2015mammalianermannosidase pages 2-4)
MAN1B1 is mechanistically linked to N-glycan-dependent ER quality control (ERQC) and ERAD. In this model, progressive demannosylation helps drive misfolded glycoproteins away from productive folding cycles and toward degradative pathways. Pan et al. describe ERManI as being capable of cleaving α1,2-mannose residues from Man9GlcNAc2 and show that wild-type ERManI can accelerate degradation of a model misfolded substrate (NHK), supporting its ERAD role. (pan2011golgilocalizationof pages 2-3, pan2011golgilocalizationof pages 9-10)
A key area of expert discussion is where MAN1B1 resides at steady state and where it encounters substrates.
Golgi/cis-Golgi model: Pan et al. report endogenous ERManI as predominantly Golgi-localized, proposing spatial separation between folding/retention steps and later quality control tagging steps. In this view, Golgi localization is apparently important for its functional impact on ERAD, and forced redistribution can change trimming without necessarily increasing degradation. (pan2011golgilocalizationof pages 1-2, pan2011golgilocalizationof pages 9-10)
ER-derived QCV/ERQC model: Benyair et al. provide evidence that ERManI resides in quality control vesicles (QCVs) with ER-like density, separated from Golgi fractions, and localizes to a perinuclear ERQC region under stress. They note that fixation/immunofluorescence artifacts can make ERManI appear Golgi-localized, arguing that QCV/ERQC localization better explains substrate encounter. (benyair2015mammalianermannosidase pages 1-2, benyair2015mammalianermannosidase pages 2-4)
Taken together, these studies support a trafficking- and stress-sensitive compartmentalization model: MAN1B1 likely operates at the interface of ER and early secretory compartments, with localization influenced by cycling/vesicular organization, and its functional coupling to ERAD can depend on that compartmentalization. (pan2011golgilocalizationof pages 9-10, benyair2015mammalianermannosidase pages 2-4)
The classical role is that the luminal catalytic domain trims mannose residues on N-glycans to create or promote degradative glycan signatures. Pan et al. show that ERManI expression can accelerate NHK degradation, consistent with a catalytic contribution to ERAD. (pan2011golgilocalizationof pages 2-3, pan2011golgilocalizationof pages 9-10)
Sun et al. (PNAS, 2020-09-29) provide strong evidence that MAN1B1 has a second separable role: an unconventional, catalysis-independent pathway controlled by the evolutionarily extended N-terminal cytoplasmic tail.
Key experimental findings include:
- Tail involvement: deletion of residues 1–54 impairs Man1b1’s ability to accelerate degradation of misfolded AAT variants. (sun2020thecytoplasmictail pages 1-3, sun2020thecytoplasmictail pages 5-7)
- Independence from catalytic activity: the catalytic-dead mutant D463N still supports aspects of the unconventional clearance pathway, and combined tail deletion + catalytic inactivation strongly reduces clearance, consistent with two partially independent contributions. (sun2020thecytoplasmictail pages 3-4)
- Independence from substrate N-glycans: tail-mediated elimination of misfolded AAT was reported to be independent of the client’s glycosylation status, indicating this pathway does not require glycan trimming on the substrate. (sun2020thecytoplasmictail pages 1-1, sun2020thecytoplasmictail pages 5-7)
- Endpoint: proteasomal degradation is a key endpoint for Man1b1-promoted NHK degradation, supported by proteasome inhibitor effects. (sun2020thecytoplasmictail pages 5-7)
This tail-mediated function is an important modern refinement of MAN1B1 functional annotation because it implies MAN1B1 can contribute to proteostasis beyond direct substrate demannosylation. (sun2020thecytoplasmictail pages 9-11, sun2020thecytoplasmictail pages 1-1)
Rymen et al. (PLoS Genetics, 2013-12-05) identified biallelic MAN1B1 mutations causing a CDG-II phenotype (often referred to as MAN1B1-CDG and clinically associated with Rafiq syndrome). The phenotype described includes developmental delay/psychomotor retardation, facial dysmorphism, and truncal obesity, and patient fibroblasts showed markedly dilated and fragmented Golgi morphology, supporting secretory-pathway involvement. (rymen2013man1b1deficiencyan pages 1-2, rymen2013man1b1deficiencyan pages 2-3)
Rymen et al. provide quantitative and structural biomarker evidence:
- Transferrin pattern: serum transferrin isoelectrofocusing showed a type 2 pattern with markedly increased trisialotransferrin (31–41%) versus normal (1–8%). (rymen2013man1b1deficiencyan pages 3-4)
- Hybrid N-glycans: N-glycan mass spectrometry revealed accumulation of hybrid-type glycans, including NeuAc1Hex6HexNAc3 (m/z 2390) and NeuAc1Hex5HexNAc3 (m/z 2186), often with fucosylated counterparts; these species were reported absent in controls. (rymen2013man1b1deficiencyan pages 3-4)
- Processing delay: metabolic labeling/pulse-chase in patient fibroblasts showed delayed trimming of Man9GlcNAc2 to Man8GlcNAc2 with accumulation of Man9GlcNAc2 and Glc1Man9GlcNAc2 species. (rymen2013man1b1deficiencyan pages 4-7)
Visual evidence supporting these diagnostic findings (transferrin profiles and MALDI-TOF N-glycan profiles) was retrieved from the paper’s figures. (rymen2013man1b1deficiencyan media f357a49a, rymen2013man1b1deficiencyan media 50a6e23d, rymen2013man1b1deficiencyan media 194a2f89)
A later diagnostic review emphasizes that the presence of hybrid glycans on transferrin may be indicative of MAN1B1-CDG, underscoring that this remains a clinically actionable glycan signature. (Wada, 2025-02-14; https://doi.org/10.5702/massspectrometry.a0169) (wada2025massspectrometryas pages 5-6)
A 2023 study developed a targeted glyco/deglycoproteomics workflow using kifunensine (a class I mannosidase inhibitor) to delineate oligomannosidic glycoproteins and glycosites in the early secretory pathway. Although not MAN1B1-specific, this work operationalizes how MAN1B1-class trimming is perturbed and quantified at scale (lectin enrichment + Endo H digestion + high-resolution MS), enabling identification of class I mannosidase-dependent substrate candidates relevant to ERQC/ERAD biology. (Munteanu et al., 2023-01-10; https://doi.org/10.3389/fmolb.2022.1064868) (munteanu2023definingthealtered pages 1-2, munteanu2023definingthealtered pages 2-3)
This paper also explicitly states that class I mannosidases cleave only α1,2-linked mannose residues and that kifunensine leads to accumulation of unprocessed oligomannose (e.g., Man9) glycoforms—important experimental context for functional studies of MAN1B1. (munteanu2023definingthealtered pages 7-8)
Baz et al. (Frontiers in Pediatrics, 2024-04-25) provide real-world evidence that clinical exome sequencing ordered by general pediatricians can identify MAN1B1-related disease. They report a patient homozygous for MAN1B1 NM_016219.5:c.2072A>G p.(His691Arg) diagnosed with Rafiq syndrome (OMIM #614202) (in a dual molecular diagnosis). (https://doi.org/10.3389/fped.2024.1392444) (baz2024clinicalexomesequencing pages 5-6, baz2024clinicalexomesequencing pages 4-5)
Quantitatively, their cohort (n=30) had:
- Diagnostic yield: 11/30 (36.7%) positive; 3/30 (10%) VUS; 16/30 (53%) negative. (baz2024clinicalexomesequencing pages 1-2, baz2024clinicalexomesequencing pages 2-3)
- Reported clinical utility in all 11/11 positive cases (100%), with several downstream impacts (e.g., subsequent testing, targeted therapy). (baz2024clinicalexomesequencing pages 1-2, baz2024clinicalexomesequencing pages 2-3)
These 2024 data primarily advance MAN1B1’s clinical implementation context (diagnostic workflows and utility), rather than revising its enzymology.
Current diagnostic practice supported by the cited literature combines:
1) Genetic diagnosis (exome sequencing) for suspected syndromic neurodevelopmental phenotypes (e.g., Rafiq syndrome diagnosis via homozygous MAN1B1 variant). (baz2024clinicalexomesequencing pages 5-6, yalcintepe2023clinicalexomesequencing pages 5-8)
2) Biochemical confirmation / pathway localization using:
- Transferrin isoelectrofocusing/capillary zone electrophoresis to detect CDG-II patterns and quantify abnormal trisialotransferrin. (rymen2013man1b1deficiencyan pages 3-4)
- Serum N-glycan MS (e.g., MALDI-TOF of permethylated N-glycans) identifying hybrid glycan accumulation, including specific m/z species. (rymen2013man1b1deficiencyan pages 3-4)
Primary papers provide conflicting steady-state localizations (Golgi vs ER-derived QCV/ERQC). Pan et al. propose a Golgi-localized ERManI model linked to ERAD regulation, whereas Benyair et al. argue Golgi appearance can be artifactual and support QCV localization using fractionation and optimized imaging. (pan2011golgilocalizationof pages 1-2, benyair2015mammalianermannosidase pages 1-2)
A reasonable synthesis of these authoritative sources is that MAN1B1 is part of a distributed quality-control network whose functional output depends on dynamic trafficking and compartment convergence under stress, rather than being restricted to a single static organelle address. (pan2011golgilocalizationof pages 9-10, benyair2015mammalianermannosidase pages 2-4)
Sun et al. add a conceptually important refinement: MAN1B1 is not solely a glycan-trimming timer but can also participate in catalysis-independent, glycan-independent degradation promotion via its cytosolic tail. This creates a framework where pathogenic MAN1B1 variants could impair one or both functional axes (enzymatic trimming and/or trafficking/recruitment functions), potentially contributing to variable phenotypes. (sun2020thecytoplasmictail pages 1-1, sun2020thecytoplasmictail pages 3-4)
The following table consolidates the major functional and clinical claims with supporting evidence.
| Topic | Key points | Representative evidence/source | Citation IDs |
|---|---|---|---|
| Identity/domains | • Human MAN1B1 encodes ERManI/ER α1,2-mannosidase I linked to UniProt Q9UKM7. • It is a type II membrane glycosidase in the GH47/class I α1,2-mannosidase family. • Protein architecture includes an N-terminal cytosolic tail, TM segment, and luminal catalytic domain. |
Pan 2011; Sun 2020 | (pan2011golgilocalizationof pages 1-2, sun2020thecytoplasmictail pages 1-3) |
| Catalytic reaction | • Catalyzes removal of α1,2-linked mannose residues from high-mannose N-glycans. • Canonical reaction highlighted for MAN1B1 is Man9GlcNAc2 → Man8GlcNAc2 isomer B. • Overexpression studies also support further trimming toward Man5-7GlcNAc2 in cells. |
Rymen 2013; Pan 2011; Zhang 2021 review | (rymen2013man1b1deficiencyan pages 1-2, pan2011golgilocalizationof pages 2-3, zhang2021thecrucialrole pages 14-15) |
| Substrate specificity | • Shows preference for the B-branch terminal mannose of Man9GlcNAc2. • Substrates are mainly N-glycosylated secretory pathway glycoproteins, especially misfolded ERAD clients. • Class I mannosidases cleave only α1,2-linked mannose residues; kifunensine blocks this processing and causes Man9 accumulation. |
Benyair 2015; Munteanu 2023 | (benyair2015mammalianermannosidase pages 1-2, benyair2015mammalianermannosidase pages 2-4, munteanu2023definingthealtered pages 7-8) |
| Localization | • Localization is debated/dynamic: endogenous MAN1B1 was reported in the Golgi/cis-Golgi by some studies. • Other work places it in ER-derived quality control vesicles (QCVs) and the ER quality control compartment (ERQC), distinct from Golgi under optimized imaging/fractionation. • Trafficking/localization may be stress-sensitive and influenced by COPI/COPII-related cycling. |
Pan 2011; Rymen 2013; Benyair 2015 | (pan2011golgilocalizationof pages 1-2, rymen2013man1b1deficiencyan pages 2-3, benyair2015mammalianermannosidase pages 1-2, benyair2015mammalianermannosidase pages 2-4) |
| ERAD roles | • Mannose trimming by MAN1B1 helps generate the glycan timer/sorting signal that routes terminally misfolded glycoproteins from folding cycles to ER-associated degradation (ERAD). • WT MAN1B1 accelerates degradation of model ERAD substrates such as NHK and influences degradation of ATZ/PIZ-related clients. • Inhibition or knockdown of class I mannosidase activity impairs ERAD, supporting a causal role. |
Pan 2011; Zhang 2021 review; Munteanu 2023 | (pan2011golgilocalizationof pages 9-10, pan2011golgilocalizationof pages 2-3, zhang2021thecrucialrole pages 14-15, munteanu2023definingthealtered pages 1-2) |
| Catalysis-independent role | • MAN1B1 has a second, catalysis-independent quality-control activity mediated by the N-terminal cytoplasmic tail (aa 1-54). • This pathway can promote proteasomal degradation of misfolded AAT variants even when MAN1B1 catalytic activity is disabled. • Tail-dependent activity is independent of N-glycans on the client substrate, implying a noncanonical recruitment/sorting role. |
Sun 2020 | (sun2020thecytoplasmictail pages 9-11, sun2020thecytoplasmictail pages 1-1, sun2020thecytoplasmictail pages 5-7, sun2020thecytoplasmictail pages 3-4) |
| Disease association | • Biallelic MAN1B1 variants cause MAN1B1-CDG / Rafiq syndrome, a CDG-II processing defect. • Core phenotype includes developmental delay/intellectual disability, facial dysmorphism, and often truncal obesity. • Patient cells also show Golgi fragmentation/dilatation, linking enzyme deficiency to secretory-pathway dysfunction. |
Rymen 2013; Baz 2024; Yalcintepe 2023 | (rymen2013man1b1deficiencyan pages 1-2, rymen2013man1b1deficiencyan pages 2-3, baz2024clinicalexomesequencing pages 5-6, yalcintepe2023clinicalexomesequencing pages 5-8) |
| Diagnostic biomarkers | • Serum transferrin testing shows a type II pattern with markedly increased trisialotransferrin. • Serum N-glycan MS reveals distinctive hybrid glycans, including NeuAc1Hex6HexNAc3 and NeuAc1Hex5HexNAc3, often with fucosylated counterparts. • A 2025 diagnostic review highlights hybrid glycans on transferrin as a characteristic clue for MAN1B1-CDG. |
Rymen 2013; Wada 2025 | (rymen2013man1b1deficiencyan pages 3-4, rymen2013man1b1deficiencyan pages 4-7, wada2025massspectrometryas pages 5-6) |
| Experimental tools/applications | • Kifunensine is a widely used class I mannosidase inhibitor to probe MAN1B1-class trimming and ERQC/ERAD function. • Modern workflows combine lectin enrichment, Endo H digestion, and LC-MS/MS glycoproteomics to identify class I mannosidase-dependent substrates. • Clinical implementation includes exome sequencing plus transferrin glycoform/MS glycan profiling for diagnosis. |
Munteanu 2023; Wada 2025; Baz 2024 | (munteanu2023definingthealtered pages 2-3, munteanu2023definingthealtered pages 1-2, munteanu2023definingthealtered pages 7-8, wada2025massspectrometryas pages 5-6, baz2024clinicalexomesequencing pages 1-2) |
| Recent (2023-2024) developments | • 2023 glycoproteomics work expanded practical mapping of class I mannosidase-sensitive glycoproteins and early secretory pathway cargo under kifunensine perturbation. • 2024 clinical exome data show real-world diagnostic utility, including a patient diagnosed with Rafiq syndrome due to homozygous MAN1B1 p.His691Arg. • Recent disease-focused literature emphasizes improved molecular diagnostics and phenotypic recognition of glycosylation disorders, including MAN1B1-CDG. |
Munteanu 2023; Baz 2024 | (munteanu2023definingthealtered pages 2-3, munteanu2023definingthealtered pages 1-2, baz2024clinicalexomesequencing pages 5-6, baz2024clinicalexomesequencing pages 4-5) |
Table: This table summarizes the core functional annotation of human MAN1B1/ERManI, including catalytic activity, localization, ERAD roles, disease links, and recent diagnostic/experimental developments. It is useful as a compact evidence map for interpreting the gene’s molecular function and clinical relevance.
References
(pan2011golgilocalizationof pages 1-2): Shujuan Pan, Shufang Wang, Budi Utama, Lu Huang, Neil Blok, Mary K. Estes, Kelley W. Moremen, and Richard N. Sifers. Golgi localization of ermani defines spatial separation of the mammalian glycoprotein quality control system. Molecular Biology of the Cell, 22:2810-2822, Aug 2011. URL: https://doi.org/10.1091/mbc.e11-02-0118, doi:10.1091/mbc.e11-02-0118. This article has 95 citations and is from a domain leading peer-reviewed journal.
(sun2020thecytoplasmictail pages 1-3): Ashlee H. Sun, John R. Collette, and Richard N. Sifers. The cytoplasmic tail of human mannosidase man1b1 contributes to catalysis-independent quality control of misfolded alpha1-antitrypsin. Proceedings of the National Academy of Sciences, 117:24825-24836, Sep 2020. URL: https://doi.org/10.1073/pnas.1919013117, doi:10.1073/pnas.1919013117. This article has 23 citations and is from a highest quality peer-reviewed journal.
(benyair2015mammalianermannosidase pages 1-2): Ron Benyair, Navit Ogen-Shtern, Niv Mazkereth, Ben Shai, Marcelo Ehrlich, and Gerardo Z. Lederkremer. Mammalian er mannosidase i resides in quality control vesicles, where it encounters its glycoprotein substrates. Molecular Biology of the Cell, 26:172-184, Jan 2015. URL: https://doi.org/10.1091/mbc.e14-06-1152, doi:10.1091/mbc.e14-06-1152. This article has 74 citations and is from a domain leading peer-reviewed journal.
(sun2020thecytoplasmictail pages 1-1): Ashlee H. Sun, John R. Collette, and Richard N. Sifers. The cytoplasmic tail of human mannosidase man1b1 contributes to catalysis-independent quality control of misfolded alpha1-antitrypsin. Proceedings of the National Academy of Sciences, 117:24825-24836, Sep 2020. URL: https://doi.org/10.1073/pnas.1919013117, doi:10.1073/pnas.1919013117. This article has 23 citations and is from a highest quality peer-reviewed journal.
(rymen2013man1b1deficiencyan pages 1-2): Daisy Rymen, Romain Peanne, María B. Millón, Valérie Race, Luisa Sturiale, Domenico Garozzo, Philippa Mills, Peter Clayton, Carla G. Asteggiano, Dulce Quelhas, Ali Cansu, Esmeralda Martins, Marie-Cécile Nassogne, Miguel Gonçalves-Rocha, Haluk Topaloglu, Jaak Jaeken, François Foulquier, and Gert Matthijs. Man1b1 deficiency: an unexpected cdg-ii. PLoS Genetics, 9:e1003989, Dec 2013. URL: https://doi.org/10.1371/journal.pgen.1003989, doi:10.1371/journal.pgen.1003989. This article has 102 citations and is from a domain leading peer-reviewed journal.
(pan2011golgilocalizationof pages 2-3): Shujuan Pan, Shufang Wang, Budi Utama, Lu Huang, Neil Blok, Mary K. Estes, Kelley W. Moremen, and Richard N. Sifers. Golgi localization of ermani defines spatial separation of the mammalian glycoprotein quality control system. Molecular Biology of the Cell, 22:2810-2822, Aug 2011. URL: https://doi.org/10.1091/mbc.e11-02-0118, doi:10.1091/mbc.e11-02-0118. This article has 95 citations and is from a domain leading peer-reviewed journal.
(benyair2015mammalianermannosidase pages 2-4): Ron Benyair, Navit Ogen-Shtern, Niv Mazkereth, Ben Shai, Marcelo Ehrlich, and Gerardo Z. Lederkremer. Mammalian er mannosidase i resides in quality control vesicles, where it encounters its glycoprotein substrates. Molecular Biology of the Cell, 26:172-184, Jan 2015. URL: https://doi.org/10.1091/mbc.e14-06-1152, doi:10.1091/mbc.e14-06-1152. This article has 74 citations and is from a domain leading peer-reviewed journal.
(pan2011golgilocalizationof pages 9-10): Shujuan Pan, Shufang Wang, Budi Utama, Lu Huang, Neil Blok, Mary K. Estes, Kelley W. Moremen, and Richard N. Sifers. Golgi localization of ermani defines spatial separation of the mammalian glycoprotein quality control system. Molecular Biology of the Cell, 22:2810-2822, Aug 2011. URL: https://doi.org/10.1091/mbc.e11-02-0118, doi:10.1091/mbc.e11-02-0118. This article has 95 citations and is from a domain leading peer-reviewed journal.
(sun2020thecytoplasmictail pages 5-7): Ashlee H. Sun, John R. Collette, and Richard N. Sifers. The cytoplasmic tail of human mannosidase man1b1 contributes to catalysis-independent quality control of misfolded alpha1-antitrypsin. Proceedings of the National Academy of Sciences, 117:24825-24836, Sep 2020. URL: https://doi.org/10.1073/pnas.1919013117, doi:10.1073/pnas.1919013117. This article has 23 citations and is from a highest quality peer-reviewed journal.
(sun2020thecytoplasmictail pages 3-4): Ashlee H. Sun, John R. Collette, and Richard N. Sifers. The cytoplasmic tail of human mannosidase man1b1 contributes to catalysis-independent quality control of misfolded alpha1-antitrypsin. Proceedings of the National Academy of Sciences, 117:24825-24836, Sep 2020. URL: https://doi.org/10.1073/pnas.1919013117, doi:10.1073/pnas.1919013117. This article has 23 citations and is from a highest quality peer-reviewed journal.
(sun2020thecytoplasmictail pages 9-11): Ashlee H. Sun, John R. Collette, and Richard N. Sifers. The cytoplasmic tail of human mannosidase man1b1 contributes to catalysis-independent quality control of misfolded alpha1-antitrypsin. Proceedings of the National Academy of Sciences, 117:24825-24836, Sep 2020. URL: https://doi.org/10.1073/pnas.1919013117, doi:10.1073/pnas.1919013117. This article has 23 citations and is from a highest quality peer-reviewed journal.
(rymen2013man1b1deficiencyan pages 2-3): Daisy Rymen, Romain Peanne, María B. Millón, Valérie Race, Luisa Sturiale, Domenico Garozzo, Philippa Mills, Peter Clayton, Carla G. Asteggiano, Dulce Quelhas, Ali Cansu, Esmeralda Martins, Marie-Cécile Nassogne, Miguel Gonçalves-Rocha, Haluk Topaloglu, Jaak Jaeken, François Foulquier, and Gert Matthijs. Man1b1 deficiency: an unexpected cdg-ii. PLoS Genetics, 9:e1003989, Dec 2013. URL: https://doi.org/10.1371/journal.pgen.1003989, doi:10.1371/journal.pgen.1003989. This article has 102 citations and is from a domain leading peer-reviewed journal.
(rymen2013man1b1deficiencyan pages 3-4): Daisy Rymen, Romain Peanne, María B. Millón, Valérie Race, Luisa Sturiale, Domenico Garozzo, Philippa Mills, Peter Clayton, Carla G. Asteggiano, Dulce Quelhas, Ali Cansu, Esmeralda Martins, Marie-Cécile Nassogne, Miguel Gonçalves-Rocha, Haluk Topaloglu, Jaak Jaeken, François Foulquier, and Gert Matthijs. Man1b1 deficiency: an unexpected cdg-ii. PLoS Genetics, 9:e1003989, Dec 2013. URL: https://doi.org/10.1371/journal.pgen.1003989, doi:10.1371/journal.pgen.1003989. This article has 102 citations and is from a domain leading peer-reviewed journal.
(rymen2013man1b1deficiencyan pages 4-7): Daisy Rymen, Romain Peanne, María B. Millón, Valérie Race, Luisa Sturiale, Domenico Garozzo, Philippa Mills, Peter Clayton, Carla G. Asteggiano, Dulce Quelhas, Ali Cansu, Esmeralda Martins, Marie-Cécile Nassogne, Miguel Gonçalves-Rocha, Haluk Topaloglu, Jaak Jaeken, François Foulquier, and Gert Matthijs. Man1b1 deficiency: an unexpected cdg-ii. PLoS Genetics, 9:e1003989, Dec 2013. URL: https://doi.org/10.1371/journal.pgen.1003989, doi:10.1371/journal.pgen.1003989. This article has 102 citations and is from a domain leading peer-reviewed journal.
(rymen2013man1b1deficiencyan media f357a49a): Daisy Rymen, Romain Peanne, María B. Millón, Valérie Race, Luisa Sturiale, Domenico Garozzo, Philippa Mills, Peter Clayton, Carla G. Asteggiano, Dulce Quelhas, Ali Cansu, Esmeralda Martins, Marie-Cécile Nassogne, Miguel Gonçalves-Rocha, Haluk Topaloglu, Jaak Jaeken, François Foulquier, and Gert Matthijs. Man1b1 deficiency: an unexpected cdg-ii. PLoS Genetics, 9:e1003989, Dec 2013. URL: https://doi.org/10.1371/journal.pgen.1003989, doi:10.1371/journal.pgen.1003989. This article has 102 citations and is from a domain leading peer-reviewed journal.
(rymen2013man1b1deficiencyan media 50a6e23d): Daisy Rymen, Romain Peanne, María B. Millón, Valérie Race, Luisa Sturiale, Domenico Garozzo, Philippa Mills, Peter Clayton, Carla G. Asteggiano, Dulce Quelhas, Ali Cansu, Esmeralda Martins, Marie-Cécile Nassogne, Miguel Gonçalves-Rocha, Haluk Topaloglu, Jaak Jaeken, François Foulquier, and Gert Matthijs. Man1b1 deficiency: an unexpected cdg-ii. PLoS Genetics, 9:e1003989, Dec 2013. URL: https://doi.org/10.1371/journal.pgen.1003989, doi:10.1371/journal.pgen.1003989. This article has 102 citations and is from a domain leading peer-reviewed journal.
(rymen2013man1b1deficiencyan media 194a2f89): Daisy Rymen, Romain Peanne, María B. Millón, Valérie Race, Luisa Sturiale, Domenico Garozzo, Philippa Mills, Peter Clayton, Carla G. Asteggiano, Dulce Quelhas, Ali Cansu, Esmeralda Martins, Marie-Cécile Nassogne, Miguel Gonçalves-Rocha, Haluk Topaloglu, Jaak Jaeken, François Foulquier, and Gert Matthijs. Man1b1 deficiency: an unexpected cdg-ii. PLoS Genetics, 9:e1003989, Dec 2013. URL: https://doi.org/10.1371/journal.pgen.1003989, doi:10.1371/journal.pgen.1003989. This article has 102 citations and is from a domain leading peer-reviewed journal.
(wada2025massspectrometryas pages 5-6): Yoshinao Wada. Mass spectrometry as a first-line diagnostic aid for congenital disorders of glycosylation. Mass Spectrometry, 14:A0169-A0169, Feb 2025. URL: https://doi.org/10.5702/massspectrometry.a0169, doi:10.5702/massspectrometry.a0169. This article has 4 citations.
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