The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
CryoSeek identification of glycofibrils with diverse compositions and structural assemblies
Open accessPublished version of a preprint
Abstract
CryoSeek is a research strategy that employs cryo-electron microscopy (cryo-EM) to discover bio-entities from accessible sources, supplemented with AI-facilitated data processing and bioinformatic analyses. Here we report CryoSeek-based characterization of more glycofibrils isolated from the Tsinghua Lotus Pond (TLP), named TLP-0/2/3/4b/IPT, with resolutions ranging from 3.0-3.5 Å. These glycofibrils, all covered with dense glycoshells, have various mass percentiles of the central protein components. TLP-0 has no protein at all, TLP-2 and TLP-4b each only have a linear chain of di- or tetra-peptide repeats, respectively; the central stem of TLP-3 is a trimer of linear tripeptide repeats, and IPT (immunoglobulin-like, plexins, and transcription factors) refers to the tandem domain that constitutes the central stem of TLP-IPT. Glycan-mediated interactions determine the structural assembly of the glycofibrils that lack folded protein component. Our previous and current studies reveal the diversity of the structural folds of glycans, advance our understanding of glycan architecture, and further demonstrate CryoSeek as a structure-first paradigm for discovery.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Evolutionary-scale prediction of atomic level protein structure with a language model
Lin, Z., Akin, H., Rao, R., Hie, B., Zhu, Z., Lu, W., Smetanin, N., Verkuil, R., Kabeli, O., Shmueli, Y., et al. (2022) · doi:10.1101/2022.07.20.500902 · Cited by 5,990
Varki, A. (2017) · Glycobiology · doi:10.1093/glycob/cww086 · Cited by 2,635
Automated model building and protein identification in cryo-EM maps
Jamali, K., Käll, L., Zhang, R., Brown, A., Kimanius, D., & Scheres, S. H. W. (2023) · doi:10.1101/2023.05.16.541002 · Cited by 686
Flagged first, then by citations
Research works printed but not linked: 58
- Varki, 1993, Biological roles of oligosaccharides: all of the theories are correct, Glycobiology, 3, 97, 10.1093/glycob/3.2.97 · DOI
- Cosgrove, 2005, Growth of the plant cell wall, Nat. Rev. Mol. Cell Biol., 6, 850, 10.1038/nrm1746 · DOI · Paper page
- Amazaki, 2018, Effects of N-Glycans on Glycoprotein Folding and Protein Dynamics, Adv. Exp. Med. Biol., 1104, 1, 10.1007/978-981-13-2158-0_1 · DOI
- Rabinovich, 2012, Glycobiology of immune responses, Ann. N. Y. Acad. Sci., 1253, 1, 10.1111/j.1749-6632.2012.06492.x · DOI
- Flynn, 2021, Small RNAs are modified with N-glycans and displayed on the surface of living cells, Cell, 184, 3109, 10.1016/j.cell.2021.04.023 · DOI
- Huang, 2024, Structure-guided discovery of protein and glycan components in native mastigonemes, Cell, 187, 1733, 10.1016/j.cell.2024.02.037 · DOI
- Kühlbrandt, 2014, Biochemistry. The resolution revolution, Science, 343, 1443, 10.1126/science.1251652 · DOI · Paper page
- Cheng, 2015, Single-Particle Cryo-EM at Crystallographic Resolution, Cell, 161, 450, 10.1016/j.cell.2015.03.049 · DOI
- Baek, 2021, Accurate prediction of protein structures and interactions using a three-track neural network, Science, 373, 871, 10.1126/science.abj8754 · DOI · Paper page
- Abramson, 2024, Accurate structure prediction of biomolecular interactions with AlphaFold 3, Nature, 630, 493, 10.1038/s41586-024-07487-w · DOI · Paper page
- Liao, 2013, Structure of the TRPV1 ion channel determined by electron cryo-microscopy, Nature, 504, 107, 10.1038/nature12822 · DOI
- Lis, 1993, Protein glycosylation: Structural and functional aspects, Eur. J. Biochem., 218, 1, 10.1111/j.1432-1033.1993.tb18347.x · DOI
- Moremen, 2012, Vertebrate protein glycosylation: diversity, synthesis and function, Nat. Rev. Mol. Cell Biol., 13, 448, 10.1038/nrm3383 · DOI
- Deng, 2014, Crystal structure of the human glucose transporter GLUT1, Nature, 510, 121, 10.1038/nature13306 · DOI · Paper page
- Deng, 2015, Molecular basis of ligand recognition and transport by glucose transporters, Nature, 526, 391, 10.1038/nature14655 · DOI
- Xie, 2014, Crystal structure of the γ-secretase component nicastrin, Proc. Natl. Acad. Sci. USA, 111, 13349, 10.1073/pnas.1414837111 · DOI
- Walls, 2016, Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy, Nat. Struct. Mol. Biol., 23, 899, 10.1038/nsmb.3293 · DOI
- Williams, 2021, Fab-dimerized glycan-reactive antibodies are a structural category of natural antibodies, Cell, 184, 2955, 10.1016/j.cell.2021.04.042 · DOI
- Xiong, 2018, Glycan Shield and Fusion Activation of a Deltacoronavirus Spike Glycoprotein Fine-Tuned for Enteric Infections, J. Virol., 92, 10.1128/JVI.01628-17 · DOI
- Imai, 2003, Geometric phase analysis of lattice images from algal cellulose microfibrils, Polymer, 44, 1871, 10.1016/S0032-3861(02)00861-3 · DOI
- Wang, 2024, CryoSeek: A strategy for bioentity discovery using cryoelectron microscopy, Proc. Natl. Acad. Sci. USA, 121, 10.1073/pnas.2417046121 · DOI
- Wang, 2025, CryoSeek II: Cryo-EM analysis of glycofibrils from freshwater reveals well-structured glycans coating linear tetrapeptide repeats, Proc. Natl. Acad. Sci. USA, 122
- Xu, 2019, A2-net: Molecular structure estimation from cryo-em density volumes, Proc. AAAI Conf. Artif. Intell., 33, 1230
- Pettersen, 2021, UCSF ChimeraX: Structure visualization for researchers, educators, and developers, Protein Sci., 30, 70, 10.1002/pro.3943 · DOI
- Remaut, 2006, Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted beta strand displacement mechanism, Mol. Cell, 22, 831, 10.1016/j.molcel.2006.05.033 · DOI
- Shibata, 2020, Structure of polymerized type V pilin reveals assembly mechanism involving protease-mediated strand exchange, Nat. Microbiol., 5, 830, 10.1038/s41564-020-0705-1 · DOI
- Williams, 1988, The immunoglobulin superfamily--domains for cell surface recognition, Annu. Rev. Immunol., 6, 381, 10.1146/annurev.iy.06.040188.002121 · DOI
- Ma, 2010, Deletion or insertion in the first immunoglobulin-plexin-transcription (IPT) domain differentially regulates expression and tumorigenic activities of RON receptor Tyrosine Kinase, Mol. Cancer, 9, 307, 10.1186/1476-4598-9-307 · DOI
- Bork, 1999, Domains in plexins: links to integrins and transcription factors, Trends Biochem. Sci., 24, 261, 10.1016/S0968-0004(99)01416-4 · DOI
- Kong, 2016, Structural Basis for Plexin Activation and Regulation, Neuron, 91, 548, 10.1016/j.neuron.2016.06.018 · DOI
- Vester-Christensen, 2013, Mining the O-mannose glycoproteome reveals cadherins as major O-mannosylated glycoproteins, Proc. Natl. Acad. Sci. USA, 110, 21018, 10.1073/pnas.1313446110 · DOI
- Ye, 2006, BLAST: improvements for better sequence analysis, Nucleic Acids Res., 34, W6, 10.1093/nar/gkl164 · DOI
- Daugbjerg, 2018, Baffinella frigidus gen. et sp. nov. (Baffinellaceae fam. nov., Cryptophyceae) from Baffin Bay: Morphology, pigment profile, phylogeny, and growth rate response to three abiotic factors, J. Phycol., 54, 665, 10.1111/jpy.12766 · DOI
- Haynes, 1998, Phosphoglycosylation: a new structural class of glycosylation?, Glycobiology, 8, 1, 10.1093/glycob/8.1.1 · DOI
- Gustafson, 1980, Occurrence of N-acetylglucosamine-1-phosphate in proteinase I from Dictyostelium discoideum, J. Biol. Chem., 255, 7208, 10.1016/S0021-9258(20)79687-0 · DOI
- Roach, 2002, Glycogen and its metabolism, Curr. Mol. Med., 2, 101, 10.2174/1566524024605761 · DOI
- Smith, 2020, Starch: A Flexible, Adaptable Carbon Store Coupled to Plant Growth, Annu. Rev. Plant Biol., 71, 217, 10.1146/annurev-arplant-050718-100241 · DOI
- Heredia, 1995, Composition of plant cell walls, Z. Lebensm. Unters. Forsch., 200, 24, 10.1007/BF01192903 · DOI
- Chandel, 2021, Carbohydrate Metabolism, Cold Spring Harb. Perspect. Biol., 13, 10.1101/cshperspect.a040568 · DOI
- Staudinger, 1937, About cellulose, starch and glycogen, Naturwissenschaften, 25, 673, 10.1007/BF01496192 · DOI
- Gessler, 1999, V-amylose at atomic resolution:: X-ray structure of a cycloamylose with 26 glucose residues (cyclomaltohexaicosaose), Proc. Natl. Acad. Sci. USA, 96, 4246, 10.1073/pnas.96.8.4246 · DOI
- Zhang, 2026, Absolute hand determination of glycofibrils from natural sources in cryo-EM, Proc. Natl. Acad. Sci. USA, 123
- Archibald, 2020, Cryptomonads, Curr. Biol., 30, R1114, 10.1016/j.cub.2020.08.101 · DOI
- Higgins, 2002, Characterization of the adhesive mucilages secreted by live diatom cells using atomic force microscopy, Protist, 153, 25, 10.1078/1434-4610-00080 · DOI
- Lachnit, 2019, Identification of proteins in the adhesive trails of the diatom Amphora coffeaeformis, Philos. Trans. R. Soc. Lond. B Biol. Sci., 374, 10.1098/rstb.2019.0196 · DOI
- Zackova Suchanova, 2023, Diatom adhesive trail proteins acquired by horizontal gene transfer from bacteria serve as primers for marine biofilm formation, New Phytol., 240, 770, 10.1111/nph.19145 · DOI
- Flemming, 2016, EPS-Then and Now, Microorganisms, 4, 10.3390/microorganisms4040041 · DOI · Paper page
- Huang, 2023, Discovery of deaminase functions by structure-based protein clustering, Cell, 186, 3182, 10.1016/j.cell.2023.05.041 · DOI
- Altae-Tran, 2023, Uncovering the functional diversity of rare CRISPR-Cas systems with deep terascale clustering, Science, 382, 10.1126/science.adi1910 · DOI
- Zhang, 2024, Pro-CRISPR PcrIIC1-associated Cas9 system for enhanced bacterial immunity, Nature, 630, 484, 10.1038/s41586-024-07486-x · DOI
- Zheng, 2017, MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy, Nat. Methods, 14, 331, 10.1038/nmeth.4193 · DOI
- Punjani, 2017, cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination, Nat. Methods, 14, 290, 10.1038/nmeth.4169 · DOI · Paper page
- Emsley, 2004, Coot: model-building tools for molecular graphics, Acta Crystallogr. D Biol. Crystallogr., 60, 2126, 10.1107/S0907444904019158 · DOI · Paper page
- Adams, 2010, PHENIX: a comprehensive Python-based system for macromolecular structure solution, Acta Crystallogr. D Biol. Crystallogr., 66, 213, 10.1107/S0907444909052925 · DOI · Paper page
- Lei, 2005, Automated acquisition of cryo-electron micrographs for single particle reconstruction on an FEI Tecnai electron microscope, J. Struct. Biol., 150, 69, 10.1016/j.jsb.2005.01.002 · DOI
- Hu, 2025, High-throughput cryo-EM characterization and automated model building of glycofibrils via CryoSeek, LangTaoSha Preprint Server
- Rosenthal, 2003, Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy, J. Mol. Biol., 333, 721, 10.1016/j.jmb.2003.07.013 · DOI · Paper page
- Davis, 2004, MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes, Nucleic Acids Res., 32, W615, 10.1093/nar/gkh398 · DOI
Metadata
- Authors
- Li, Z., Wang, T., Sun, Y., Xu, K., Huang, W., Zhang, Q. C., Yan, C., Hu, M., & Yan, N.
- Affiliations
- Center for Life Sciences (CN)
- Shenzhen Medical Academy of Research and Translation (CN)
- Shenzhen Bay Laboratory (CN)
- Corresponding author
- Li, Zhangqiang
- Wang, Tongtong
- Yan, Nieng
- Venue
- Cell Chemical Biology
- Publisher
- Elsevier BV
- Published
- 2026-05
- Volume
- 33
- Issue
- 5
- Pages
- 699-710.e2
- ISSN
- 2451-9448 (ISSN-L)
- 2451-9456
- OpenAlex
- W4414765436
- Cited by
- 4
- References
- 4
- Citations by year
- 2026: 4
- FWCI
- 7.87
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- Locations
- Cell chemical biology (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (92478205)
- Key Technologies Research and Development Program (2022YFA1206400)
- National Key Research and Development Program of China
- Tsinghua University
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Polysaccharides and Plant Cell Walls
- Keywords
- glycans, plexins, transcription factors
- MeSH terms
- Models, Molecular, Polysaccharides, Cryoelectron Microscopy
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review