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Research report: Danio rerio gnptab (UniProt Q5RGJ8) — functional annotation and pathway context

0) Identity verification (critical disambiguation)

Danio rerio gnptab (UniProt Q5RGJ8) encodes the N-acetylglucosamine-1-phosphotransferase α/β precursor (GlcNAc-1-phosphotransferase; EC 2.7.8.17), the catalytic polypeptide of the mannose-6-phosphate (M6P) lysosomal enzyme-targeting pathway. This is directly verified by a peer-reviewed structural study that crystallized and biochemically characterized a zebrafish GNPTAB minimal construct explicitly annotated as UniProt Q5RGJ8. (gorelik2022structuresofthe pages 2-3, gorelik2022structuresofthe pages 4-5)

A key figure from that work summarizes GNPTAB domain organization, membrane topology/orientation in the Golgi lumen, and the phosphotransfer reaction. (gorelik2022structuresofthe media 67065d55)

1) Key concepts and definitions (current understanding)

1.1 The mannose-6-phosphate (M6P) lysosomal targeting pathway

In vertebrates, many soluble lysosomal hydrolases are sorted away from constitutive secretion by addition of M6P tags to their N-glycans. GNPTAB supplies the initiating enzymatic step by transferring GlcNAc-1-phosphate from UDP-GlcNAc to mannose residues on high-mannose N-glycans, yielding a GlcNAc–phosphate–mannose intermediate that is subsequently processed (“uncovered”) to expose M6P for receptor-mediated trafficking. (qian2013thedmapinteraction pages 1-2, gorelik2022structuresofthe pages 1-2)

1.2 Enzyme nomenclature and reaction chemistry

GlcNAc-1-phosphotransferase (GNPT) is a phosphotransferase (not a glycosyltransferase) that uses UDP-GlcNAc as phosphate-sugar donor; it requires Mg2+ or Mn2+ for activity, consistent with metal coordination of phosphate groups in the active site. (gorelik2022structuresofthe pages 3-4, gorelik2022structuresofthe pages 2-3)

1.3 Subunit organization and maturation

The native GNPT enzyme is commonly described as a heterohexamer α2β2γ2, where:
- GNPTAB encodes an α/β precursor that is proteolytically cleaved in the Golgi/TGN (reported at K928–D929 / after Lys928) to generate mature α and β subunits; cleavage is required for activity in the canonical full-length protein. (qian2013thedmapinteraction pages 1-2, petrey2012investigatingmucolipidosisii pages 25-30, gorelik2022structuresofthe pages 4-5)
- GNPTG encodes the auxiliary γ subunit, which enhances phosphorylation of subsets of substrates and contributes to substrate selection. (gorelik2022structuresofthe pages 1-2, gorelik2022structuresofthe pages 4-5)

1.4 Substrate specificity and recognition determinants

GNPTAB is distinctive in that it does not indiscriminately modify secretory glycoproteins; substrate recognition depends on protein-level determinants:
- A DMAP interaction domain within GNPTAB serves as a substrate-recognition module, experimentally binding lysosomal hydrolases (cathepsin D, α-iduronidase) but not tested non-lysosomal glycoproteins. (qian2013thedmapinteraction pages 1-2)
- Recognition also depends on the cargo’s tertiary structure and can involve appropriately oriented lysine residues near an N-glycan (often described as a determinant for selective phosphorylation). (aarnio2017defectsincarbohydratedependent pages 15-19, petrey2012investigatingmucolipidosisii pages 25-30)
- The γ subunit contains an MRH (mannose receptor homology) domain that binds terminal α1,2/α1,3 mannoses and contributes to substrate choice for a substantial subset of lysosomal hydrolases. (gorelik2022structuresofthe pages 4-5)

2) Molecular function of zebrafish GNPTAB (reaction, substrates, and catalytic determinants)

2.1 Primary molecular function

Zebrafish GNPTAB catalyzes the first step of M6P tag formation by transferring phospho-GlcNAc from UDP-GlcNAc to the 6-hydroxyl of mannose on N-glycans (including high-mannose glycans of lysosomal hydrolases). (gorelik2022structuresofthe pages 3-4, qian2013thedmapinteraction pages 1-2)

Biochemical/structural work indicates GNPT can act on minimal acceptors down to α-methyl-D-mannoside and even single-mannose substrates in vitro, emphasizing that protein-context determinants primarily control physiological selectivity. (gorelik2022structuresofthe pages 4-5, qian2013thedmapinteraction pages 2-3)

2.2 Active-site architecture and key residues (zebrafish structural evidence)

A zebrafish GNPTAB catalytic construct (UniProt Q5RGJ8) was structurally solved with bound UDP-GlcNAc, mapping mechanistic features including:
- A proposed general base His956 to deprotonate the mannose O6,
- Arg986 and a catalytic Mg site stabilizing phosphate,
- Metal coordination involving Asp408/Asp407,
- An activity-critical residue Asn1151. (gorelik2022structuresofthe pages 4-5, gorelik2022structuresofthe pages 3-4)

Quantitatively, mutation of Asp407 reduced activity by ~500-fold, and mutation of Asn1151 reduced activity by ~200-fold in the reported assays. (gorelik2022structuresofthe pages 3-4, gorelik2022structuresofthe pages 4-5)

3) Cellular localization and topology

GNPTAB functions in the cis-Golgi, with its catalytic surfaces oriented toward the Golgi lumen, consistent with both structural topology and colocalization evidence (GM130 marker). (gorelik2022structuresofthe pages 3-4, qian2013thedmapinteraction pages 2-3)

The GNPT complex is membrane-associated; structural work describes GNPTAB anchoring via multiple transmembrane helices, placing luminal active sites in surface cavities oriented away from the membrane. (gorelik2022structuresofthe pages 3-4)

4) Pathway membership and biological processes

4.1 Core pathway role

GNPTAB initiates formation of the M6P sorting signal that enables downstream receptor-based routing of lysosomal enzymes; loss of GNPT activity abolishes M6P labeling and causes missorting/secretion of lysosomal enzymes, with secondary lysosomal dysfunction and storage. (liu2024thehostmannose6phosphate pages 2-4, qian2013thedmapinteraction pages 1-2)

4.2 Mechanistic regulators (2023–2024 emphasis)

Recent work has sharpened the view that GNPTAB function depends on Golgi retention and regulated processing:
- GOLPH3/GOLPH3L → LYSET/TMEM251 → GNPTAB axis: In EMBO J (2024), GOLPH3/GOLPH3L were shown to maintain cis-Golgi localization of LYSET/TMEM251, thereby preserving the integrity of the M6P pathway; LYSET deficiency leads to GNPT mislocalization and degradation in lysosomes and prevents M6P tagging of ~70 lysosomal enzymes (quantitative scale of impact). (brauer2024golph3andgolph3l pages 1-2)
- A 2024 preprint proposes a reconciled mechanism where TMEM251/LYSET stabilizes GNPTAB, promotes its S1P cleavage, and prevents mislocalization of GNPT to lysosomes by Golgi anchoring and recycling machinery (GOLPH3 and retromer). (yang2024molecularinsightsinto pages 1-5, yang2024molecularinsightsinto pages 38-41)
- A 2024 review emphasizes the pathway as a host factor in viral infection and frames GNPT/LYSET acting sequentially with the uncovering enzyme. (liu2024thehostmannose6phosphate pages 2-4)

5) Zebrafish in vivo evidence: functional and mechanistic phenotypes

5.1 Loss-of-function phenotypes and rescue

Zebrafish gnptab depletion (morpholino-based MLII models) causes reduced mannose phosphorylation of lysosomal hydrolases and broad developmental phenotypes (craniofacial cartilage, cardiac edema, otic vesicle/otolith defects, pectoral fin defects, motility defects), with rescue by wild-type GNPTAB mRNA. (flanagansteet2009alteredchondrocytedifferentiation pages 3-4, petrey2012excessiveactivityof pages 1-2)

Quantitatively:
- Wild-type phosphotransferase activity was reported as 35–51 pmol/mg/h during the first 5 days; morpholino knockdown achieved up to 89% inhibition (4 dpf). (flanagansteet2009alteredchondrocytedifferentiation pages 3-4)
- A partial reduction (~58%) could still yield largely normal embryos, suggesting a threshold for developmental sensitivity. (flanagansteet2009alteredchondrocytedifferentiation pages 3-4)
- Morphants showed ~10 ± 3% reduced body length and death within 5–6 days. (flanagansteet2009alteredchondrocytedifferentiation pages 3-4)

5.2 Substrate-recognition domain validated in vivo (DMAP domain)

A human disease-associated mutation K732N (in the GNPTAB DMAP interaction domain) selectively impaired phosphorylation of lysosomal hydrolases while retaining activity toward a simple mannose acceptor. In vitro, phosphorylation of cathepsin D and α-iduronidase was only 12–15% of wild-type. In zebrafish gnptab-depleted embryos, wild-type mRNA rescued the MLII-like phenotype, whereas the K732N mutant mRNA failed to rescue (reported ~76% remaining MLII-like vs ~75% rescue with WT). (qian2013thedmapinteraction pages 2-3, qian2013thedmapinteraction pages 1-2)

5.3 Cartilage/chondrocyte differentiation and ECM homeostasis

Zebrafish MLII gnptab models show chondrocyte and ECM abnormalities:
- Chondrocytes fail to intercalate and are reported ~25% larger than wild-type. (flanagansteet2009alteredchondrocytedifferentiation pages 9-10)
- Chondrocyte-enriched sorting for transcript profiling achieved 99.2% and 99.9% purity at 2 and 3 dpf; GFP+ populations were ~8% (2 dpf) and ~20% (3 dpf) of dissociated cells. (petrey2012excessiveactivityof pages 3-4)
- Transcriptional/ECM markers: reduced aggrecan and sustained/high col2a1/type II collagen transcripts at later stages were reported. (petrey2012excessiveactivityof pages 3-4)

5.4 Protease dysregulation as a downstream mechanism and its correction

In gnptab-deficient embryos, there is increased and sustained activity of cathepsins and MMPs, regionally enriched in the head, linking lysosomal mistargeting to extracellular protease-driven cartilage pathology. (petrey2012excessiveactivityof pages 4-5, petrey2012excessiveactivityof pages 3-4)

Rescue/perturbation evidence:
- WT GNPTAB mRNA normalized cathepsin activity at 3 dpf (with WT n=4 and MLII n=6 in enzyme assays). (petrey2012excessiveactivityof pages 3-4)
- Pharmacologic cathepsin K inhibition (2-day treatment from 2 dpf) partially rescued cartilage: 13.9% rescue at 2.5 μM and 22.2% rescue at 5 μM; morpholino suppression of cathepsin K produced 15.9% full rescue and 69.2% partial rescue. (petrey2012investigatingmucolipidosisii pages 96-101)
- Chondrocyte intercalation improved from 6 ± 4% in MLII toward 60 ± 9% with co-knockdown, compared to 85 ± 5% in WT. (petrey2012investigatingmucolipidosisii pages 96-101)

6) Current applications and real-world implementations

6.1 Human diagnostics and variant interpretation (2024 cohort example)

A 2024 cohort of 20 Chinese probands (6 ML II; 14 ML III α/β) expanded the GNPTAB mutation spectrum and illustrates real-world diagnostic workflows. GNPTAB variants were detected in 35/40 alleles (87.5%); the most prevalent variants were c.2715+1G>A (14.3%) and c.2404C>T / p.Gln802Ter (11.4%). The authors note that increased plasma lysosomal enzyme activities of 10–20× normal support diagnosis; they provide reference ranges including arylsulfatase A (50–140 nmol/mg·17 h) and hexosaminidase A (29.8–63.8 nmol/mg·h). (feng2024clinicalandmolecular pages 1-2)

6.2 Zebrafish models as a discovery and screening platform

Zebrafish gnptab MLII models have enabled mechanistic dissection of early cartilage pathology and demonstrated that targeting downstream pathways (e.g., cathepsin K) can ameliorate structural phenotypes, supporting their utility for pathway-based therapeutic hypothesis testing. (petrey2012excessiveactivityof pages 1-2, petrey2012investigatingmucolipidosisii pages 96-101)

6.3 Biomanufacturing/therapeutic enzyme design (2023 glycoengineering)

A 2023 study described a “Long-Acting-GlycoDesign (LAGD)” glycoengineering approach that eliminates M6P from therapeutic lysosomal enzymes and converts them to homogeneous sialylated glycans, improving circulation time and biodistribution in mouse studies (qualitative in excerpt). This illustrates that manipulating the M6P axis—whose biosynthesis depends on GNPTAB—remains an active area in enzyme-therapy development and bioprocessing. (chen2023auniversalglycodesign pages 1-2)

7) Expert synthesis and interpretation

Collectively, the most precise experimental evidence supports GNPTAB as a cis-Golgi luminal phosphotransferase whose α/β precursor must be correctly processed and retained at the Golgi to provide selective M6P tagging of lysosomal hydrolases. Structural data from a zebrafish Q5RGJ8 catalytic construct resolves the core catalytic mechanism, while zebrafish developmental models show that reduced M6P tagging can drive tissue pathology via altered ECM homeostasis and protease misregulation, a mechanism that is pharmacologically modifiable. (gorelik2022structuresofthe pages 4-5, flanagansteet2009alteredchondrocytedifferentiation pages 3-4, petrey2012investigatingmucolipidosisii pages 96-101)

Recent 2024 work reframes GNPTAB activity as an emergent property of a Golgi retention network (GOLPH3/GOLPH3L–LYSET/TMEM251–GNPT), explaining how defects in trafficking/retention can phenocopy catalytic loss by destabilizing GNPT and collapsing M6P tagging across dozens of lysosomal enzymes. (brauer2024golph3andgolph3l pages 1-2, yang2024molecularinsightsinto pages 38-41)

Summary artifact

The following table consolidates key functional annotation points, zebrafish in vivo evidence, quantitative results, and 2023–2024 developments with URLs.

Table: This table summarizes the core functional annotation of Danio rerio gnptab (UniProt Q5RGJ8), integrating enzyme chemistry, domains, localization, pathway role, and zebrafish-specific experimental evidence. It also highlights quantitative results and key primary citations useful for downstream gene annotation.

Key cited sources (publication date; URL)

• Gorelik et al., Aug 2022, PNAS. “Structures of the mannose-6-phosphate pathway enzyme, GlcNAc-1-phosphotransferase.” https://doi.org/10.1073/pnas.2203518119 (gorelik2022structuresofthe pages 4-5, gorelik2022structuresofthe pages 2-3, gorelik2022structuresofthe pages 3-4, gorelik2022structuresofthe media 67065d55)
• Qian et al., Jun 2013, PNAS. “The DMAP interaction domain … is a substrate recognition module.” https://doi.org/10.1073/pnas.1308453110 (qian2013thedmapinteraction pages 1-2, qian2013thedmapinteraction pages 2-3)
• Flanagan-Steet et al., Nov 2009, Am J Pathol. “Altered Chondrocyte Differentiation … in a Zebrafish Model for Mucolipidosis II.” https://doi.org/10.2353/ajpath.2009.090210 (flanagansteet2009alteredchondrocytedifferentiation pages 3-4, flanagansteet2009alteredchondrocytedifferentiation pages 9-10, flanagansteet2009alteredchondrocytedifferentiation pages 2-3)
• Petrey et al., Mar 2012, Dis Model Mech. “Excessive activity of cathepsin K … in a zebrafish model of mucolipidosis II.” https://doi.org/10.1242/dmm.008219 (petrey2012excessiveactivityof pages 1-2, petrey2012excessiveactivityof pages 3-4, petrey2012excessiveactivityof pages 4-5)
• Liu et al., Jan 2024, Front Cell Infect Microbiol (review). “The host mannose-6-phosphate pathway and viral infection.” https://doi.org/10.3389/fcimb.2024.1349221 (liu2024thehostmannose6phosphate pages 2-4)
• Brauer et al., Nov 2024, EMBO J. “GOLPH3 and GOLPH3L maintain Golgi localization of LYSET …” https://doi.org/10.1038/s44318-024-00305-z (brauer2024golph3andgolph3l pages 1-2)
• Feng et al., Dec 2024, BMC Pediatrics. “Clinical and molecular characteristics of 20 Chinese probands …” https://doi.org/10.1186/s12887-024-05223-x (feng2024clinicalandmolecular pages 1-2)
• Chen et al., Feb 2023, Front Bioeng Biotechnol. “A universal GlycoDesign …” https://doi.org/10.3389/fbioe.2023.1128371 (chen2023auniversalglycodesign pages 1-2)
• Tang et al., May 2023, Trends Glycosci Glycotechnol (review). “Glycoengineering for the Production of Lysosomal Enzymes.” https://doi.org/10.4052/tigg.2204.1e (tang2023glycoengineeringforthe pages 1-2)
• Yang et al., Dec 2024, bioRxiv (preprint). “Molecular Insights into the Regulation of GNPTAB by TMEM251.” https://doi.org/10.1101/2024.12.05.627003 (yang2024molecularinsightsinto pages 1-5, yang2024molecularinsightsinto pages 38-41)

References

1. (gorelik2022structuresofthe pages 2-3): Alexei Gorelik, Katalin Illes, Khanh Huy Bui, and Bhushan Nagar. Structures of the mannose-6-phosphate pathway enzyme, glcnac-1-phosphotransferase. Proceedings of the National Academy of Sciences of the United States of America, Aug 2022. URL: https://doi.org/10.1073/pnas.2203518119, doi:10.1073/pnas.2203518119. This article has 17 citations and is from a highest quality peer-reviewed journal.

2. (gorelik2022structuresofthe pages 4-5): Alexei Gorelik, Katalin Illes, Khanh Huy Bui, and Bhushan Nagar. Structures of the mannose-6-phosphate pathway enzyme, glcnac-1-phosphotransferase. Proceedings of the National Academy of Sciences of the United States of America, Aug 2022. URL: https://doi.org/10.1073/pnas.2203518119, doi:10.1073/pnas.2203518119. This article has 17 citations and is from a highest quality peer-reviewed journal.

3. (gorelik2022structuresofthe media 67065d55): Alexei Gorelik, Katalin Illes, Khanh Huy Bui, and Bhushan Nagar. Structures of the mannose-6-phosphate pathway enzyme, glcnac-1-phosphotransferase. Proceedings of the National Academy of Sciences of the United States of America, Aug 2022. URL: https://doi.org/10.1073/pnas.2203518119, doi:10.1073/pnas.2203518119. This article has 17 citations and is from a highest quality peer-reviewed journal.

4. (qian2013thedmapinteraction pages 1-2): Yi Qian, Heather Flanagan-Steet, Eline van Meel, Richard Steet, and Stuart A. Kornfeld. The dmap interaction domain of udp-glcnac:lysosomal enzyme n-acetylglucosamine-1-phosphotransferase is a substrate recognition module. Proceedings of the National Academy of Sciences, 110:10246-10251, Jun 2013. URL: https://doi.org/10.1073/pnas.1308453110, doi:10.1073/pnas.1308453110. This article has 47 citations and is from a highest quality peer-reviewed journal.

5. (gorelik2022structuresofthe pages 1-2): Alexei Gorelik, Katalin Illes, Khanh Huy Bui, and Bhushan Nagar. Structures of the mannose-6-phosphate pathway enzyme, glcnac-1-phosphotransferase. Proceedings of the National Academy of Sciences of the United States of America, Aug 2022. URL: https://doi.org/10.1073/pnas.2203518119, doi:10.1073/pnas.2203518119. This article has 17 citations and is from a highest quality peer-reviewed journal.

6. (gorelik2022structuresofthe pages 3-4): Alexei Gorelik, Katalin Illes, Khanh Huy Bui, and Bhushan Nagar. Structures of the mannose-6-phosphate pathway enzyme, glcnac-1-phosphotransferase. Proceedings of the National Academy of Sciences of the United States of America, Aug 2022. URL: https://doi.org/10.1073/pnas.2203518119, doi:10.1073/pnas.2203518119. This article has 17 citations and is from a highest quality peer-reviewed journal.

7. (petrey2012investigatingmucolipidosisii pages 25-30): AC Petrey. Investigating mucolipidosis ii: a role for proteases in cartilage pathogenesis. Unknown journal, 2012.

8. (aarnio2017defectsincarbohydratedependent pages 15-19): MC Aarnio. Defects in carbohydrate-dependent lysosomal targeting lead to alterations in growth factor signaling. Unknown journal, 2017.

9. (qian2013thedmapinteraction pages 2-3): Yi Qian, Heather Flanagan-Steet, Eline van Meel, Richard Steet, and Stuart A. Kornfeld. The dmap interaction domain of udp-glcnac:lysosomal enzyme n-acetylglucosamine-1-phosphotransferase is a substrate recognition module. Proceedings of the National Academy of Sciences, 110:10246-10251, Jun 2013. URL: https://doi.org/10.1073/pnas.1308453110, doi:10.1073/pnas.1308453110. This article has 47 citations and is from a highest quality peer-reviewed journal.

10. (liu2024thehostmannose6phosphate pages 2-4): Qincheng Liu, Weiqi Wang, Liwei Xu, Qisheng Zhang, and Hongna Wang. The host mannose-6-phosphate pathway and viral infection. Frontiers in Cellular and Infection Microbiology, Jan 2024. URL: https://doi.org/10.3389/fcimb.2024.1349221, doi:10.3389/fcimb.2024.1349221. This article has 6 citations.

11. (brauer2024golph3andgolph3l pages 1-2): Berit K Brauer, Zilei Chen, Felix Beirow, Jiaran Li, Daniel Meisinger, Emanuela Capriotti, Michaela Schweizer, Lea Wagner, Jascha Wienberg, Laura Hobohm, Lukas Blume, Wenjie Qiao, Yoshiki Narimatsu, Jan E Carette, Henrik Clausen, Dominic Winter, Thomas Braulke, Sabrina Jabs, and Matthias Voss. Golph3 and golph3l maintain golgi localization of lyset and a functional mannose 6-phosphate transport pathway. The EMBO Journal, 43:6264-6290, Nov 2024. URL: https://doi.org/10.1038/s44318-024-00305-z, doi:10.1038/s44318-024-00305-z. This article has 20 citations.

12. (yang2024molecularinsightsinto pages 1-5): Xi Yang, Balraj Doray, Varsha Venkatarangan, Benjamin C. Jennings, Danielle Henn, Jiaxuan Liang, Haikun Zhao, Weichao Zhang, Bokai Zhang, Linchen Yu, Liang Chen, Stuart Kornfeld, and Ming Li. Molecular insights into the regulation of gnptab by tmem251. bioRxiv, Dec 2024. URL: https://doi.org/10.1101/2024.12.05.627003, doi:10.1101/2024.12.05.627003. This article has 2 citations.

13. (yang2024molecularinsightsinto pages 38-41): Xi Yang, Balraj Doray, Varsha Venkatarangan, Benjamin C. Jennings, Danielle Henn, Jiaxuan Liang, Haikun Zhao, Weichao Zhang, Bokai Zhang, Linchen Yu, Liang Chen, Stuart Kornfeld, and Ming Li. Molecular insights into the regulation of gnptab by tmem251. bioRxiv, Dec 2024. URL: https://doi.org/10.1101/2024.12.05.627003, doi:10.1101/2024.12.05.627003. This article has 2 citations.

14. (flanagansteet2009alteredchondrocytedifferentiation pages 3-4): Heather Flanagan-Steet, Christina Sias, and Richard Steet. Altered chondrocyte differentiation and extracellular matrix homeostasis in a zebrafish model for mucolipidosis ii. The American Journal of Pathology, 175:2063-2075, Nov 2009. URL: https://doi.org/10.2353/ajpath.2009.090210, doi:10.2353/ajpath.2009.090210. This article has 56 citations.

15. (petrey2012excessiveactivityof pages 1-2): Aaron C. Petrey, Heather Flanagan-Steet, Steven Johnson, Xiang Fan, Mitche De la Rosa, Mark E. Haskins, Alison V. Nairn, Kelley W. Moremen, and Richard Steet. Excessive activity of cathepsin k is associated with cartilage defects in a zebrafish model of mucolipidosis ii. Mar 2012. URL: https://doi.org/10.1242/dmm.008219, doi:10.1242/dmm.008219. This article has 49 citations and is from a domain leading peer-reviewed journal.

16. (flanagansteet2009alteredchondrocytedifferentiation pages 9-10): Heather Flanagan-Steet, Christina Sias, and Richard Steet. Altered chondrocyte differentiation and extracellular matrix homeostasis in a zebrafish model for mucolipidosis ii. The American Journal of Pathology, 175:2063-2075, Nov 2009. URL: https://doi.org/10.2353/ajpath.2009.090210, doi:10.2353/ajpath.2009.090210. This article has 56 citations.

17. (petrey2012excessiveactivityof pages 3-4): Aaron C. Petrey, Heather Flanagan-Steet, Steven Johnson, Xiang Fan, Mitche De la Rosa, Mark E. Haskins, Alison V. Nairn, Kelley W. Moremen, and Richard Steet. Excessive activity of cathepsin k is associated with cartilage defects in a zebrafish model of mucolipidosis ii. Mar 2012. URL: https://doi.org/10.1242/dmm.008219, doi:10.1242/dmm.008219. This article has 49 citations and is from a domain leading peer-reviewed journal.

18. (petrey2012excessiveactivityof pages 4-5): Aaron C. Petrey, Heather Flanagan-Steet, Steven Johnson, Xiang Fan, Mitche De la Rosa, Mark E. Haskins, Alison V. Nairn, Kelley W. Moremen, and Richard Steet. Excessive activity of cathepsin k is associated with cartilage defects in a zebrafish model of mucolipidosis ii. Mar 2012. URL: https://doi.org/10.1242/dmm.008219, doi:10.1242/dmm.008219. This article has 49 citations and is from a domain leading peer-reviewed journal.

19. (petrey2012investigatingmucolipidosisii pages 96-101): AC Petrey. Investigating mucolipidosis ii: a role for proteases in cartilage pathogenesis. Unknown journal, 2012.

20. (feng2024clinicalandmolecular pages 1-2): Yuyu Feng, Yonglan Huang, Xiaoyuan Zhao, Huiying Sheng, Xueying Su, Xi Yin, Liu Li, and Wen Zhang. Clinical and molecular characteristics of 20 chinese probands with mucolipidosis type ii and iii alpha/beta. BMC Pediatrics, Dec 2024. URL: https://doi.org/10.1186/s12887-024-05223-x, doi:10.1186/s12887-024-05223-x. This article has 1 citations and is from a peer-reviewed journal.

21. (chen2023auniversalglycodesign pages 1-2): Yen-Hsi Chen, Weihua Tian, Makiko Yasuda, Zilu Ye, Ming Song, Ulla Mandel, Claus Kristensen, Lorenzo Povolo, André R. A. Marques, Tomislav Čaval, Albert J. R. Heck, Julio Lopes Sampaio, Ludger Johannes, Takahiro Tsukimura, Robert Desnick, Sergey Y. Vakhrushev, Zhang Yang, and Henrik Clausen. A universal glycodesign for lysosomal replacement enzymes to improve circulation time and biodistribution. Frontiers in Bioengineering and Biotechnology, Feb 2023. URL: https://doi.org/10.3389/fbioe.2023.1128371, doi:10.3389/fbioe.2023.1128371. This article has 7 citations.

22. (flanagansteet2009alteredchondrocytedifferentiation pages 2-3): Heather Flanagan-Steet, Christina Sias, and Richard Steet. Altered chondrocyte differentiation and extracellular matrix homeostasis in a zebrafish model for mucolipidosis ii. The American Journal of Pathology, 175:2063-2075, Nov 2009. URL: https://doi.org/10.2353/ajpath.2009.090210, doi:10.2353/ajpath.2009.090210. This article has 56 citations.

23. (tang2023glycoengineeringforthe pages 1-2): Yu-He Tang, Ganglong Yang, and Morihisa Fujita. Glycoengineering for the production of lysosomal enzymes. Trends in Glycoscience and Glycotechnology, 35:E42-E49, May 2023. URL: https://doi.org/10.4052/tigg.2204.1e, doi:10.4052/tigg.2204.1e. This article has 0 citations and is from a peer-reviewed journal.

Artifacts

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Citations

1. qian2013thedmapinteraction pages 1-2
2. gorelik2022structuresofthe pages 4-5
3. gorelik2022structuresofthe pages 3-4
4. flanagansteet2009alteredchondrocytedifferentiation pages 3-4
5. flanagansteet2009alteredchondrocytedifferentiation pages 9-10
6. petrey2012excessiveactivityof pages 3-4
7. petrey2012investigatingmucolipidosisii pages 96-101
8. feng2024clinicalandmolecular pages 1-2
9. chen2023auniversalglycodesign pages 1-2
10. gorelik2022structuresofthe pages 2-3
11. petrey2012investigatingmucolipidosisii pages 25-30
12. tang2023glycoengineeringforthe pages 1-2
13. gorelik2022structuresofthe pages 1-2
14. aarnio2017defectsincarbohydratedependent pages 15-19
15. qian2013thedmapinteraction pages 2-3
16. yang2024molecularinsightsinto pages 1-5
17. yang2024molecularinsightsinto pages 38-41
18. petrey2012excessiveactivityof pages 1-2
19. petrey2012excessiveactivityof pages 4-5
20. flanagansteet2009alteredchondrocytedifferentiation pages 2-3
21. https://doi.org/10.1073/pnas.2203518119
22. https://doi.org/10.1073/pnas.2203518119;
23. https://doi.org/10.1073/pnas.1308453110
24. https://doi.org/10.1073/pnas.1308453110;
25. https://doi.org/10.3389/fcimb.2024.1349221
26. https://doi.org/10.1038/s44318-024-00305-z
27. https://doi.org/10.3389/fcimb.2024.1349221;
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