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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 requested target was verified as human ALG5, UniProt Q9Y673, HGNC symbol ALG5, Ensembl ENSG00000120697, and transcript NM_013338.5. Its approved description—dolichyl-phosphate β-glucosyltransferase, also called dolichol-phosphate-glucose synthase—is consistent across the supplied UniProt record, human genetics literature, and Open Targets. No conflicting same-symbol protein was used in this report. Open Targets likewise identifies ALG5 as “ALG5 dolichyl-phosphate beta-glucosyltransferase.” (OpenTargets Search: -ALG5, elhassan2024anovelmonoallelic pages 1-2, elhassan2024anovelmonoallelic pages 4-5)
ALG5 is an integral endoplasmic-reticulum membrane glycosyltransferase that catalyzes:
UDP-glucose + dolichyl phosphate → UDP + dolichyl-phosphate glucose.
Dolichyl-phosphate glucose is subsequently used as the membrane-bound glucose donor for the three terminal glucosylation reactions that complete the lipid-linked N-glycan precursor Glc₃Man₉GlcNAc₂-PP-dolichol in the ER lumen. Thus, ALG5 does not directly glucosylate protein; it generates the lipid-linked donor required to complete the oligosaccharide that is later transferred en bloc to nascent proteins. (takahashi2024analysesofthea pages 18-20, takahashi2024analysesofthe pages 18-20, chang2014biochemicalandbiophysical pages 139-143, elhassan2024anovelmonoallelic pages 14-15)
The most important recent development is a July 2024 human study associating heterozygous ALG5 p.Arg79Trp with a late-onset, atypical autosomal-dominant polycystic-kidney phenotype accompanied by substantial tubulointerstitial fibrosis and abnormal uromodulin trafficking. However, the disease evidence currently centers on one variant in two distantly related pedigrees, and direct evidence that the variant impairs polycystin-1 glycosylation remains incomplete. (elhassan2024anovelmonoallelic pages 1-2, elhassan2024anovelmonoallelic pages 4-5, elhassan2024anovelmonoallelic pages 14-15)
The target is the human gene ALG5, not an unrelated similarly named gene or a microbial protein. The 2024 human study refers to the gene through transcript NM_013338.5 and describes its product as an ER dolichol-phosphoglucose synthase involved in N-linked glycosylation. Open Targets maps ALG5 to ENSG00000120697 and uses the approved name “ALG5 dolichyl-phosphate beta-glucosyltransferase.” These identifiers and functions agree with UniProt Q9Y673 and the supplied HGNC designation. (OpenTargets Search: -ALG5, elhassan2024anovelmonoallelic pages 4-5, elhassan2024anovelmonoallelic pages 14-15)
The supplied annotations place Q9Y673 in glycosyltransferase family 2 and identify DPG_synthase, Glyco_trans_2-like, nucleotide-diphosugar-transferase, and PF00535 Glycos_transf_2 domains. These annotations are biochemically consistent with transfer of glucose from the nucleotide-sugar UDP-glucose to a lipid-phosphate acceptor. Nevertheless, the retrieved primary human literature did not independently dissect each InterPro/Pfam domain, so the domain labels should be regarded principally as curated sequence- and family-based annotations rather than individually validated human structural domains.
ALG5 is assigned EC 2.4.1.117 and transfers the glucosyl moiety of UDP-glucose to dolichyl phosphate, forming dolichyl-phosphate glucose and UDP. The experimentally and evolutionarily supported acceptor class is a long-chain polyisoprenoid phosphate embedded in a membrane; the donor is UDP-glucose. (takahashi2024analysesofthea pages 18-20, takahashi2024analysesofthe pages 18-20, chang2014biochemicalandbiophysical pages 151-155)
This reaction defines ALG5 as a polyprenol/dolichol phosphate glucosyltransferase. It should be distinguished from ALG6, ALG8, and ALG10: those enzymes use dolichyl-phosphate glucose to transfer glucose onto the growing lipid-linked oligosaccharide, whereas ALG5 synthesizes the donor itself. (takahashi2024analysesofthea pages 18-20, takahashi2024analysesofthe pages 18-20)
The core specificity is well established at the pathway level: UDP-glucose is the sugar donor and dolichyl phosphate is the lipid acceptor. Homolog experiments have used radiolabeled UDP-glucose and C55–60 dolichyl phosphate and achieved up to 30% acceptor turnover under optimized cell-free conditions, but these are yeast Alg5 experiments and should not be interpreted as kinetic measurements for Q9Y673. (chang2014biochemicalandbiophysical pages 151-155)
No rigorous human Q9Y673 substrate panel, Michaelis constants, turnover number, alternative nucleotide-sugar testing, or dolichol-chain-length preference was identified in the retrieved literature. Therefore, annotation of strict exclusion of related donors or acceptors would exceed the direct evidence.
Human ALG5 is an ER-resident membrane protein. Its use of cytosolic UDP-glucose and synthesis of dolichyl-phosphate glucose place the catalytic reaction on the cytosolic face of the ER membrane. The lipid-linked product must then become available to luminal glucosyltransferases, although the molecular mechanism by which Dol-P-Glc crosses or is presented across the membrane is not established by the retrieved ALG5 studies. (chang2014biochemicalandbiophysical pages 139-143, elhassan2024anovelmonoallelic pages 14-15)
Human kidney tissue provides direct localization evidence. Control tissue showed ER localization, whereas tissue from p.Arg79Trp carriers showed abnormal coarse cytoplasmic staining and ALG5 deposition in both ER and Golgi compartments. The authors interpreted this as disturbed maturation, folding, recycling, or trafficking rather than evidence that Golgi localization is the normal site of catalysis. (elhassan2024anovelmonoallelic pages 1-2, elhassan2024anovelmonoallelic pages 14-15, elhassan2024anovelmonoallelic pages 7-8)
A topology model with two transmembrane segments and cytosolic N- and C-termini is plausible. However, the clearest retrieved topology experiments concern Saccharomyces cerevisiae Alg5p. The investigators reported that yeast topology corresponded broadly to an earlier human model, but exact human topology should therefore be described as supported by orthology and limited topology studies, not as definitively resolved by current high-resolution human structural data. (takahashi2024analysesofthea pages 18-20, takahashi2024analysesofthea pages 23-25, takahashi2024analysesofthe pages 23-25)
N-linked glycosylation begins on the cytosolic ER face, where GlcNAc and mannose residues are assembled on dolichyl diphosphate. After an intermediate is moved to the lumenal side, additional mannose and glucose residues are added. ALG5 supplies the Dol-P-Glc used for the final three glucose additions, producing Glc₃Man₉GlcNAc₂-PP-dolichol. Oligosaccharyltransferase then transfers this oligosaccharide en bloc to suitable Asn-X-Ser/Thr sequons of nascent secretory and membrane proteins. (chang2014biochemicalandbiophysical pages 139-143)
The glucoses supplied through ALG5 are consequently important not only for precursor completion but also for downstream glycoprotein maturation and ER quality-control processes. A defect in ALG5 can therefore affect selected glycoproteins through altered glycan assembly, folding, ER retention, degradation, or trafficking rather than through a conventional receptor-mediated signaling pathway.
Yeast Alg5p reportedly interacts with enzymes involved in the dolichol cycle and early oligosaccharide assembly, including Dpm1p, Sec59p, Cwh8p, and Alg7p. These interactions support the concept of spatially coordinated ER glycosylation machinery, but they are homolog evidence and should not be automatically assigned as experimentally validated human ALG5 interactions. (takahashi2024analysesofthea pages 23-25, takahashi2024analysesofthe pages 23-25)
Elhassan and colleagues reported the heterozygous variant GRCh37 g.37569565G>A; NM_013338.5:c.235C>T; p.Arg79Trp in two Irish multiplex families found to be distantly related by identity by descent. The variant affects a conserved residue near the proposed activity-regulating A-loop and was absent from population databases. It was discovered by exome sequencing after an established kidney-gene panel and MUC1 testing had been unrevealing. The study was published in Kidney International Reports in July 2024: https://doi.org/10.1016/j.ekir.2024.04.031. (elhassan2024anovelmonoallelic pages 1-2, elhassan2024anovelmonoallelic pages 4-5, elhassan2024anovelmonoallelic pages 11-14, elhassan2024anovelmonoallelic pages 2-4)
Across the extended pedigrees, 23 individuals carried p.Arg79Trp and 18 were clinically affected. Fourteen of 23 carriers had CKD, compared with 1 of 15 noncarriers—60.9% versus 6.7%, P=0.002. No carrier had an eGFR below 60 ml/min/1.73 m² before age 50, demonstrating a generally late-onset course. Five carriers reached end-stage kidney disease at a mean age of 73 ± 8.6 years, range 63–87 years. (elhassan2024anovelmonoallelic pages 4-5, elhassan2024anovelmonoallelic pages 5-7, elhassan2024anovelmonoallelic pages 7-8)
The renal phenotype differed from classic severe PKD1-associated ADPKD. Kidneys were generally not enlarged; mean height-adjusted total kidney volume was 156 ± 122 ml/m at a mean age of 70.4 ± 9 years. Cyst burden correlated inversely with eGFR (r=−0.539, P=0.009), but biopsies also showed substantial chronic injury, including cystically dilated tubules, secondary glomerulosclerosis, and 25–50% tubulointerstitial fibrosis/tubular atrophy. Liver cyst expression varied widely and was sometimes substantial despite modest kidney enlargement. (elhassan2024anovelmonoallelic pages 5-7, elhassan2024anovelmonoallelic pages 7-8)
Affected kidney tissue showed ER accumulation of uromodulin, an N-glycosylated GPI-anchored protein produced by tubular cells. Quantitative localization was approximately 34% ER and 66% plasma membrane in affected tissue, compared with 0% ER and 92% plasma membrane in controls. Plasma and urinary uromodulin were reduced. This provides human tissue evidence that abnormal ALG5 function can disrupt processing or trafficking of a physiologically important renal glycoprotein. (elhassan2024anovelmonoallelic pages 1-2, elhassan2024anovelmonoallelic pages 11-14)
Residual urinary uromodulin did not exhibit an abnormal electrophoretic mobility indicative of a gross glycosylation defect. Transferrin processing was apparently normal, and O-glycosylated MUC1 did not show comparable retention. Thus, p.Arg79Trp did not produce an obvious generalized systemic glycosylation phenotype; the findings instead suggest partial, tissue-selective, or client-selective impairment. No ALG5-specific plasma proteomic or glycoproteomic biomarker was identified. (elhassan2024anovelmonoallelic pages 14-15, elhassan2024anovelmonoallelic pages 11-14)
The authors proposed that reduced or mislocalized ALG5 activity could alter N-glycosylation, maturation, and cell-surface delivery of polycystin-1 and possibly polycystin-2, thereby lowering functional polycystin dosage and promoting cystogenesis. In parallel, ER retention of uromodulin could drive organelle stress, tubular-cell loss, nephron attrition, and fibrosis. This two-component model explains why cystic burden was relatively modest while tubulointerstitial damage was substantial. (elhassan2024anovelmonoallelic pages 1-2, elhassan2024anovelmonoallelic pages 14-15)
This remains a mechanistic model rather than complete proof: the study did not report direct quantitative demonstration of abnormal polycystin-1 glycosylation or trafficking in carrier kidneys. Likewise, p.Arg79Trp-specific catalytic activity was not directly measured with purified human enzyme.
The immediate application is molecular diagnosis. ALG5 is a reasonable candidate for inclusion in cystic-kidney gene panels and exome/genome interpretation when PKD1, PKD2, and other established genes are negative, especially when the presentation includes late onset, scattered cysts, nonenlarged kidneys, and fibrosis disproportionate to cyst burden. Segregation testing can support variant interpretation and inform surveillance and family counseling. (elhassan2024anovelmonoallelic pages 4-5, elhassan2024anovelmonoallelic pages 2-4)
Open Targets records associations between ALG5 and autosomal-dominant polycystic kidney disease and “polycystic kidney disease 7,” with association scores of approximately 0.657 and 0.602, respectively. These scores summarize aggregated database evidence; they are not penetrance estimates or measures of therapeutic tractability. Other low-to-moderate database associations, such as insomnia or neurodegenerative disease, should not be interpreted as established ALG5 monogenic phenotypes without targeted validation. (OpenTargets Search: -ALG5)
No ALG5-directed therapy, validated ALG5-specific biochemical biomarker, or clinical trial was identified. Current care therefore remains phenotype-based rather than enzyme-replacement or pathway-targeted treatment. The 2024 findings are most actionable for diagnosis, renal monitoring, and counseling rather than for selecting an ALG5-specific drug.
High-confidence annotation: ALG5/Q9Y673 is the human ER dolichyl-phosphate β-glucosyltransferase that uses UDP-glucose and dolichyl phosphate to generate Dol-P-Glc for lipid-linked oligosaccharide glucosylation. This conclusion is supported by consistent nomenclature, conserved biochemical-pathway evidence, and human genetic/pathology literature. (OpenTargets Search: -ALG5, takahashi2024analysesofthe pages 18-20, chang2014biochemicalandbiophysical pages 139-143, elhassan2024anovelmonoallelic pages 14-15)
Moderate-confidence structural annotation: A compact, polytopic ER-membrane topology—often modeled with two membrane spans and cytosolic termini—is consistent with homolog experiments and prior human comparison, but no high-resolution human structure or comprehensive human topology map was retrieved. (takahashi2024analysesofthea pages 18-20, takahashi2024analysesofthea pages 23-25, takahashi2024analysesofthe pages 23-25)
Strong but variant-limited disease evidence: p.Arg79Trp showed extensive segregation, late-onset clinical expression, abnormal human-tissue localization, fibrosis, and selective UMOD-trafficking abnormalities. Nevertheless, the two pedigrees appear to form one founder lineage, so independent variants and unrelated populations are required to define the full ALG5 disease spectrum. (elhassan2024anovelmonoallelic pages 1-2, elhassan2024anovelmonoallelic pages 4-5, elhassan2024anovelmonoallelic pages 5-7, elhassan2024anovelmonoallelic pages 11-14)
Mechanistically plausible but incomplete: Impaired polycystin maturation provides a credible bridge between N-glycosylation and cystogenesis, while UMOD retention plausibly explains tubulointerstitial injury. Direct human evidence for defective polycystin glycosylation and direct enzymology of p.Arg79Trp remain priorities for future work. (elhassan2024anovelmonoallelic pages 14-15)
The principal evidence and its limitations are summarized below.
| Topic | Conclusion | Evidence type/strength | Key quantitative detail | Source/date/URL |
|---|---|---|---|---|
| Target identity | The target is human ALG5 (UniProt Q9Y673; HGNC ALG5; ENSG00000120697), the dolichyl-phosphate β-glucosyltransferase—not a similarly named protein from another organism. | Strong database identity plus direct human genetic/biological study | Human disease study used transcript NM_013338.5; Open Targets approved name is “ALG5 dolichyl-phosphate beta-glucosyltransferase.” | Open Targets, accessed 2026 (OpenTargets Search: -ALG5); Elhassan et al., published July 2024, DOI (elhassan2024anovelmonoallelic pages 1-2, elhassan2024anovelmonoallelic pages 4-5) |
| Catalytic reaction and specificity | ALG5 transfers glucose from UDP-glucose to dolichyl phosphate: UDP-glucose + dolichyl-P → UDP + dolichyl-P-glucose (Dol-P-Glc). It is therefore a lipid-phosphate glucosyltransferase, not one of the enzymes that directly glucosylates the growing oligosaccharide. | Established biochemical/pathway assignment; human-specific kinetic and substrate-panel data remain limited | EC 2.4.1.117; recombinant homolog assays used UDP-[³H]glucose and Dol-P, reaching up to 30% Dol-P turnover under optimized cell-free conditions—supportive homolog evidence only. | Elhassan et al., July 2024 (elhassan2024anovelmonoallelic pages 14-15); Chang, 2014, homolog experiment (chang2014biochemicalandbiophysical pages 151-155) |
| Cellular site and reaction orientation | Human ALG5 is an ER-resident integral membrane enzyme. Its nucleotide-sugar-dependent synthesis of Dol-P-Glc occurs on the cytosolic face of the ER, consistent with cytosolic UDP-glucose availability. | Human ER localization supported directly; precise orientation derives partly from pathway logic and homolog topology | Patient kidney showed aberrant ALG5 staining in both ER and Golgi, whereas control localization was ER-restricted. | Elhassan et al., July 2024 (elhassan2024anovelmonoallelic pages 1-2, elhassan2024anovelmonoallelic pages 7-8) |
| Membrane topology | A model with two transmembrane segments and cytosolic N- and C-termini is plausible for human ALG5, but the clearest retrieved experimental topology data are from S. cerevisiae Alg5p. | Homolog inference—not direct human proof; confidence moderate for the general architecture but lower for exact human topology | Yeast Alg5p was modeled with 2 transmembrane domains and both termini cytosolic; authors report broad correspondence with the human ortholog. | Takahashi et al., 2024; yeast study/comparison (takahashi2024analysesofthea pages 18-20, takahashi2024analysesofthea pages 23-25, takahashi2024analysesofthe pages 23-25) |
| N-glycosylation pathway role | ALG5 makes Dol-P-Glc, the membrane lipid glucose donor required for adding the three terminal glucose residues to the luminal lipid-linked precursor, completing Glc₃Man₉GlcNAc₂-PP-dolichol before oligosaccharyltransferase transfers the glycan en bloc to Asn-X-Ser/Thr sites. | Strong conserved-pathway evidence; detailed donor-use sequence is best established in yeast and general eukaryotic N-glycosylation | One ALG5 product pool supplies three glucosylation steps, mediated by ALG6, ALG8 and ALG10 homologs after the precursor enters the ER lumen. | Chang, 2014 (chang2014biochemicalandbiophysical pages 139-143); Takahashi et al., 2024 (takahashi2024analysesofthea pages 18-20, takahashi2024analysesofthe pages 18-20) |
| 2024 disease variant and segregation | Heterozygous ALG5 c.235C>T (p.Arg79Trp; R79W) segregated with a late-onset, atypical autosomal-dominant polycystic-kidney/tubulointerstitial phenotype in two distantly related Irish pedigrees. The conserved residue lies near the proposed activity-regulating A-loop and the variant was absent from population databases. | Strong family segregation and human tissue evidence, but presently centered on one variant/founder lineage | 23 carriers, of whom 18 were clinically affected; two pedigrees were related by identity by descent. | Elhassan et al., July 2024, DOI (elhassan2024anovelmonoallelic pages 1-2, elhassan2024anovelmonoallelic pages 4-5, elhassan2024anovelmonoallelic pages 11-14) |
| Kidney-disease penetrance and progression | Disease was usually mild or unapparent before age 50, followed by slowly progressive CKD; cyst burden alone appeared insufficient to explain late kidney failure, implicating tubulointerstitial injury as an additional mechanism. | Direct cohort evidence | CKD occurred in 14/23 carriers (60.9%) versus 1/15 noncarriers (6.7%), P=0.002. No carrier had eGFR <60 ml/min/1.73 m² before age 50. Five reached ESKD; mean ESKD age 73 ± 8.6 years (range 63–87). | Elhassan et al., July 2024 (elhassan2024anovelmonoallelic pages 4-5, elhassan2024anovelmonoallelic pages 5-7, elhassan2024anovelmonoallelic pages 7-8) |
| Imaging and pathology | The phenotype differs from classic PKD1-associated ADPKD: kidneys were generally nonenlarged, with scattered cysts, variable liver cysts and substantial chronic tubulointerstitial damage. | Direct imaging and biopsy evidence | Mean height-adjusted total kidney volume 156 ± 122 ml/m at mean age 70.4 ± 9 years; cyst burden correlated inversely with eGFR (r=−0.539, P=0.009). Biopsies showed 25–50% interstitial fibrosis/tubular atrophy. | Elhassan et al., July 2024 (elhassan2024anovelmonoallelic pages 5-7) |
| UMOD trafficking phenotype | Mutant kidneys accumulated the N-glycosylated, GPI-anchored protein uromodulin (UMOD) in the ER and had reduced urinary/plasma UMOD, supporting selective glycoprotein-processing/trafficking disruption and tubular stress rather than an overt systemic glycosylation failure. | Direct patient-tissue localization and biochemical evidence; mechanism remains associative | In affected tissue, UMOD localization was 34% ER/66% plasma membrane, compared with 0% ER/92% plasma membrane in controls. Residual urinary UMOD had no abnormal electrophoretic mobility; transferrin processing was apparently normal. | Elhassan et al., July 2024 (elhassan2024anovelmonoallelic pages 1-2, elhassan2024anovelmonoallelic pages 11-14) |
| Proposed cystogenic mechanism | Reduced or abnormal ALG5 activity may impair N-glycosylation, maturation and trafficking of polycystin-1 and related glycoproteins; ER retention of UMOD may add organelle stress, apoptosis, nephron loss and fibrosis. Direct quantitative demonstration of defective polycystin-1 glycosylation in carriers was not reported. | Biologically plausible expert interpretation supported by human pathology, but partly mechanistic inference | Abnormal ALG5 Golgi deposition and UMOD ER retention were observed; no ALG5-specific plasma proteomic or glycoproteomic biomarker emerged. | Elhassan et al., July 2024 (elhassan2024anovelmonoallelic pages 1-2, elhassan2024anovelmonoallelic pages 14-15) |
| Current clinical application | ALG5 should be considered on genetic panels or exome/genome analysis for PKD1/PKD2-negative, late-onset cystic kidney disease—especially nonenlarged kidneys with disproportionate tubulointerstitial fibrosis. Results can inform segregation testing, surveillance and family counseling. | Emerging diagnostic implementation based on a peer-reviewed family study; not yet a broadly validated clinical standard | The causal variant was found by exome sequencing after a kidney-gene panel and MUC1 testing were negative. | Elhassan et al., July 2024 (elhassan2024anovelmonoallelic pages 4-5, elhassan2024anovelmonoallelic pages 2-4) |
| Major limitations | Human ALG5 literature remains sparse. Disease evidence is dominated by p.Arg79Trp in one extended founder lineage; exact human topology, catalytic kinetics, alternative-substrate specificity, direct polycystin effects and variant-general disease penetrance require independent validation. No ALG5-targeted treatment, validated biomarker or clinical trial was identified. | Critical evidence-gap assessment | Open Targets records ALG5–ADPKD/PKD7 associations but does not establish a therapy; retrieved topology/interaction work is substantially yeast-based. | Open Targets, accessed 2026 (OpenTargets Search: -ALG5); Takahashi et al., 2024 (takahashi2024analysesofthea pages 18-20, takahashi2024analysesofthe pages 23-25); Elhassan et al., July 2024 (elhassan2024anovelmonoallelic pages 14-15) |
Table: Concise evidence matrix covering ALG5 identity, enzymatic function, ER pathway position, topology confidence, and the quantitative findings from the 2024 p.Arg79Trp kidney-disease study. It separates direct human observations from conclusions inferred from yeast homolog experiments.
Human ALG5/Q9Y673 is best annotated as an ER membrane enzyme that generates dolichyl-phosphate glucose from UDP-glucose and dolichyl phosphate. Its product is an essential lipid-linked donor for completing the triglucosylated N-glycan precursor in the ER. The strongest new clinical evidence, published in July 2024, links heterozygous p.Arg79Trp to a late-onset, incompletely penetrant cystic and tubulointerstitial kidney disorder with abnormal ALG5 and uromodulin trafficking. The disease association is compelling for that lineage, but the precise catalytic defect, direct impact on polycystins, generalizability to other variants, and therapeutic implications remain unresolved.
References
(OpenTargets Search: -ALG5): Open Targets Query (-ALG5, 5 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.
(elhassan2024anovelmonoallelic pages 1-2): Elhussein A.E. Elhassan, Tereza Kmochová, Katherine A. Benson, Neil K. Fennelly, Veronika Barešová, Kendrah Kidd, Brendan Doyle, Anthony Dorman, Martina M. Morrin, Niamh C. Kyne, Petr Vyleťal, Hana Hartmannová, Kateřina Hodaňová, Jana Sovová, Dita Mušálková, Alena Vrbacká, Anna Přistoupilová, Jan Živný, Klára Svojšová, Martin Radina, Viktor Stránecký, Dmitry Loginov, Petr Pompach, Petr Novák, Zdislava Vaníčková, Hana Hansíková, Silvie Rajnochová-Bloudíčková, Ondřej Viklický, Helena Hůlková, Gianpiero L. Cavalleri, Aleš Hnízda, Anthony J. Bleyer, Stanislav Kmoch, Peter J. Conlon, and Martina Živná. A novel monoallelic alg5 variant causing late-onset adpkd and tubulointerstitial fibrosis. Jul 2024. URL: https://doi.org/10.1016/j.ekir.2024.04.031, doi:10.1016/j.ekir.2024.04.031. This article has 14 citations and is from a peer-reviewed journal.
(elhassan2024anovelmonoallelic pages 4-5): Elhussein A.E. Elhassan, Tereza Kmochová, Katherine A. Benson, Neil K. Fennelly, Veronika Barešová, Kendrah Kidd, Brendan Doyle, Anthony Dorman, Martina M. Morrin, Niamh C. Kyne, Petr Vyleťal, Hana Hartmannová, Kateřina Hodaňová, Jana Sovová, Dita Mušálková, Alena Vrbacká, Anna Přistoupilová, Jan Živný, Klára Svojšová, Martin Radina, Viktor Stránecký, Dmitry Loginov, Petr Pompach, Petr Novák, Zdislava Vaníčková, Hana Hansíková, Silvie Rajnochová-Bloudíčková, Ondřej Viklický, Helena Hůlková, Gianpiero L. Cavalleri, Aleš Hnízda, Anthony J. Bleyer, Stanislav Kmoch, Peter J. Conlon, and Martina Živná. A novel monoallelic alg5 variant causing late-onset adpkd and tubulointerstitial fibrosis. Jul 2024. URL: https://doi.org/10.1016/j.ekir.2024.04.031, doi:10.1016/j.ekir.2024.04.031. This article has 14 citations and is from a peer-reviewed journal.
(takahashi2024analysesofthea pages 18-20): T TAKAHASHI, E HORIGOME, and T YAMAMOTO. Analyses of the membrane topology and physical interaction of human dolichol kinase. Unknown journal, 2024.
(takahashi2024analysesofthe pages 18-20): T TAKAHASHI, E HORIGOME, and T YAMAMOTO. Analyses of the membrane topology and physical interaction of human dolichol kinase. Unknown journal, 2024.
(chang2014biochemicalandbiophysical pages 139-143): MM Chang. Biochemical and biophysical investigations of n-linked glycosylation pathways in archaea. Unknown journal, 2014.
(elhassan2024anovelmonoallelic pages 14-15): Elhussein A.E. Elhassan, Tereza Kmochová, Katherine A. Benson, Neil K. Fennelly, Veronika Barešová, Kendrah Kidd, Brendan Doyle, Anthony Dorman, Martina M. Morrin, Niamh C. Kyne, Petr Vyleťal, Hana Hartmannová, Kateřina Hodaňová, Jana Sovová, Dita Mušálková, Alena Vrbacká, Anna Přistoupilová, Jan Živný, Klára Svojšová, Martin Radina, Viktor Stránecký, Dmitry Loginov, Petr Pompach, Petr Novák, Zdislava Vaníčková, Hana Hansíková, Silvie Rajnochová-Bloudíčková, Ondřej Viklický, Helena Hůlková, Gianpiero L. Cavalleri, Aleš Hnízda, Anthony J. Bleyer, Stanislav Kmoch, Peter J. Conlon, and Martina Živná. A novel monoallelic alg5 variant causing late-onset adpkd and tubulointerstitial fibrosis. Jul 2024. URL: https://doi.org/10.1016/j.ekir.2024.04.031, doi:10.1016/j.ekir.2024.04.031. This article has 14 citations and is from a peer-reviewed journal.
(chang2014biochemicalandbiophysical pages 151-155): MM Chang. Biochemical and biophysical investigations of n-linked glycosylation pathways in archaea. Unknown journal, 2014.
(elhassan2024anovelmonoallelic pages 7-8): Elhussein A.E. Elhassan, Tereza Kmochová, Katherine A. Benson, Neil K. Fennelly, Veronika Barešová, Kendrah Kidd, Brendan Doyle, Anthony Dorman, Martina M. Morrin, Niamh C. Kyne, Petr Vyleťal, Hana Hartmannová, Kateřina Hodaňová, Jana Sovová, Dita Mušálková, Alena Vrbacká, Anna Přistoupilová, Jan Živný, Klára Svojšová, Martin Radina, Viktor Stránecký, Dmitry Loginov, Petr Pompach, Petr Novák, Zdislava Vaníčková, Hana Hansíková, Silvie Rajnochová-Bloudíčková, Ondřej Viklický, Helena Hůlková, Gianpiero L. Cavalleri, Aleš Hnízda, Anthony J. Bleyer, Stanislav Kmoch, Peter J. Conlon, and Martina Živná. A novel monoallelic alg5 variant causing late-onset adpkd and tubulointerstitial fibrosis. Jul 2024. URL: https://doi.org/10.1016/j.ekir.2024.04.031, doi:10.1016/j.ekir.2024.04.031. This article has 14 citations and is from a peer-reviewed journal.
(takahashi2024analysesofthea pages 23-25): T TAKAHASHI, E HORIGOME, and T YAMAMOTO. Analyses of the membrane topology and physical interaction of human dolichol kinase. Unknown journal, 2024.
(takahashi2024analysesofthe pages 23-25): T TAKAHASHI, E HORIGOME, and T YAMAMOTO. Analyses of the membrane topology and physical interaction of human dolichol kinase. Unknown journal, 2024.
(elhassan2024anovelmonoallelic pages 11-14): Elhussein A.E. Elhassan, Tereza Kmochová, Katherine A. Benson, Neil K. Fennelly, Veronika Barešová, Kendrah Kidd, Brendan Doyle, Anthony Dorman, Martina M. Morrin, Niamh C. Kyne, Petr Vyleťal, Hana Hartmannová, Kateřina Hodaňová, Jana Sovová, Dita Mušálková, Alena Vrbacká, Anna Přistoupilová, Jan Živný, Klára Svojšová, Martin Radina, Viktor Stránecký, Dmitry Loginov, Petr Pompach, Petr Novák, Zdislava Vaníčková, Hana Hansíková, Silvie Rajnochová-Bloudíčková, Ondřej Viklický, Helena Hůlková, Gianpiero L. Cavalleri, Aleš Hnízda, Anthony J. Bleyer, Stanislav Kmoch, Peter J. Conlon, and Martina Živná. A novel monoallelic alg5 variant causing late-onset adpkd and tubulointerstitial fibrosis. Jul 2024. URL: https://doi.org/10.1016/j.ekir.2024.04.031, doi:10.1016/j.ekir.2024.04.031. This article has 14 citations and is from a peer-reviewed journal.
(elhassan2024anovelmonoallelic pages 2-4): Elhussein A.E. Elhassan, Tereza Kmochová, Katherine A. Benson, Neil K. Fennelly, Veronika Barešová, Kendrah Kidd, Brendan Doyle, Anthony Dorman, Martina M. Morrin, Niamh C. Kyne, Petr Vyleťal, Hana Hartmannová, Kateřina Hodaňová, Jana Sovová, Dita Mušálková, Alena Vrbacká, Anna Přistoupilová, Jan Živný, Klára Svojšová, Martin Radina, Viktor Stránecký, Dmitry Loginov, Petr Pompach, Petr Novák, Zdislava Vaníčková, Hana Hansíková, Silvie Rajnochová-Bloudíčková, Ondřej Viklický, Helena Hůlková, Gianpiero L. Cavalleri, Aleš Hnízda, Anthony J. Bleyer, Stanislav Kmoch, Peter J. Conlon, and Martina Živná. A novel monoallelic alg5 variant causing late-onset adpkd and tubulointerstitial fibrosis. Jul 2024. URL: https://doi.org/10.1016/j.ekir.2024.04.031, doi:10.1016/j.ekir.2024.04.031. This article has 14 citations and is from a peer-reviewed journal.
(elhassan2024anovelmonoallelic pages 5-7): Elhussein A.E. Elhassan, Tereza Kmochová, Katherine A. Benson, Neil K. Fennelly, Veronika Barešová, Kendrah Kidd, Brendan Doyle, Anthony Dorman, Martina M. Morrin, Niamh C. Kyne, Petr Vyleťal, Hana Hartmannová, Kateřina Hodaňová, Jana Sovová, Dita Mušálková, Alena Vrbacká, Anna Přistoupilová, Jan Živný, Klára Svojšová, Martin Radina, Viktor Stránecký, Dmitry Loginov, Petr Pompach, Petr Novák, Zdislava Vaníčková, Hana Hansíková, Silvie Rajnochová-Bloudíčková, Ondřej Viklický, Helena Hůlková, Gianpiero L. Cavalleri, Aleš Hnízda, Anthony J. Bleyer, Stanislav Kmoch, Peter J. Conlon, and Martina Živná. A novel monoallelic alg5 variant causing late-onset adpkd and tubulointerstitial fibrosis. Jul 2024. URL: https://doi.org/10.1016/j.ekir.2024.04.031, doi:10.1016/j.ekir.2024.04.031. This article has 14 citations and is from a peer-reviewed journal.