We are actively tracking the number of publications by the scientific community which reference our structures, whether in the main text, figure captions or supplementary material. Selected articles are manually reviewed. Publications by SSGCID authors are excluded from the manually reviewed list. From our manual curation results, we estimate that the false positive rate might be as high as 50% for some structures.
This list was obtained from Google Scholar searches using an API provided by Christian Kreibich.
| Structure | Year released | #citations |
|---|---|---|
| 5SCM | 2022 | 0 |
| 5SCY | 2022 | 0 |
| 3JS9 | 2009 | 0 |
| 3IPW | 2009 | 0 |
| 5SCX | 2022 | 0 |
| 3GNQ | 2009 | 0 |
| 5SCW | 2022 | 0 |
| 5SCV | 2022 | 0 |
| 5SCU | 2022 | 0 |
| 5SCT | 2022 | 0 |
| # | PDB | Additional SSGCID structures cited | Link | Title | Year | Citation | Highlighted abstract |
|---|---|---|---|---|---|---|---|
| 1 | 7k43 | 7k4n | https://www.nature.com/articles/s41401-021-00851-w | Structure genomics of SARS-CoV-2 and its Omicron variant: drug design templates for COVID-19 | 2022 | C Wu, W Yin, Y Jiang, HE Xu- Acta Pharmacologica Sinica, 2022 - nature.com | on uncovering structures and functions for structural biology of SARS-CoV-2 and discuss important biological issues that remain to be addressed. We present the examples of structure - ... S2E12 (represented as a cyan surface) binds to the “up” conformation of SARS-CoV-2 S RBD (PDB: 7K4N); S2M11 (represented as a brown surface) binds to the “down” conformation of SARS-CoV-2 S RBD (PDB: 7K43); |
| 2 | 5k9f | - | https://www.nature.com/articles/s41419-025-08070-5 | TRIM17 promotes the progression of osteosarcoma by regulating PDK1 m6A modification-mediated AKT/mTOR pathway activation through ubiquitination of FTO | 2025 | W Liu, D Zheng, X Huang, Z Wei, Z Wei, W Guo- Cell death & disease, 2025 - nature.com | Download the three-dimensional structures of TRIM17 (ID: 6Z08) and FTO (ID: 5K9F ) from the PDB database, and remove the ligands and water molecules. The amino acid residues |
| 3 | 7so9 | - | https://www.nature.com/articles/s41421-023-00535-1 | Comprehensive structural analysis reveals broad-spectrum neutralizing antibodies against SARS-CoV-2 Omicron variants | 2023 | X Chi, L Xia, G Zhang, X Chi, B Huang, Y Zhang- Cell Discovery, 2023 - nature.com | with multiple structures , we selected the subcomplex deposited earliest in the PDB database ID: 7SO9 ) were manually refined based on the focused-refined cryo-EM map. Each residue |
| 4 | 6wpt | 7jw0, 7jv6, 7k4n, 7k43, 7jvc | https://www.nature.com/articles/s41422-021-00487-9 | Structural basis for bivalent binding and inhibition of SARS-CoV-2 infection by human potent neutralizing antibodies | 2021 | R Yan, R Wang, B Ju, J Yu, Y Zhang, N Liu, J Wang- Cell research, 2021 - nature.com | Neutralizing monoclonal antibodies (nAbs) to severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) represent promising candidates for clinical intervention against coronavirus disease 2019 (COVID-19). We isolated a large number of nAbs from SARS-CoV-2-infected ... Besides, there are some special antibodies that can compete ACE2 binding while bind to RBD with different patterns. We assigned these antibodies into class IV which contains S309 (PDB code: 6WPT), C110 (PDB code: 7K8V) and C135 (PDB code |
| 5 | 7lxy | 7ly2, 7lxz, 7ly3 | https://www.nature.com/articles/s41423-021-00752-2 | Neutralizing antibodies for the prevention and treatment of COVID-19 | 2021 | L Du, Y Yang, X Zhang- Cellular & Molecular Immunology, 2021 - nature.com | Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) initiates the infection process by binding to the viral cellular receptor angiotensin-converting enzyme 2 through the receptor-binding domain (RBD) in the S1 subunit of the viral spike (S) protein. ... a–e Cryo-EM structures of the SARS-CoV-2 S trimer bound to NTD-targeting nAbs a S2L28 (PDB 7LXZ), b S2M28 (PDB 7LY2), c S2X333 (PDB 7LXY), d 4-8 (PDB 7LQV), and e 4A8 (PDB 7C2L). |
| 6 | 3p0x | - | https://www.nature.com/articles/s41467-019-12614-7 | Acetyl-CoA-mediated activation of Mycobacterium tuberculosis isocitrate lyase 2 | 2019 | RP Bhusal, W Jiao, BXC Kwai, J Reynisson- Nature, 2019 - nature.com | The structural resemblance of the Mtb ICL2 C-terminal domain to members of the GNAT observed in crystal structures of isocitrate-bound ICL1 from Brucella melitensis (Bm ICL1, PDB 3P0X ) of the active site loop are more similar to that found in the crystal structure of substrate |
| 7 | 5k85 | 5ifi | https://www.nature.com/articles/s41467-020-14301-4 | ProtCID: A data resource for structural information on protein interactions | 2020 | Q Xu, RL Dunbrack- Nature communications, 2020 - nature.com | While the structure of full-length activated PAH has not been determined, a recent structure of the ACT domain of J9VFT1_CRYNH, E5XP76_9ACTN) and two common entries ( PDB : 5IFI [https://doi.org/10.2210/pdb5IFI/ pdb ] and 5K85 [https://doi.org/10.2210/pdb5K85/ pdb ]) |
| 8 | 6q05 | - | https://www.nature.com/articles/s41467-020-16876-4 | Cryo-EM structures of HKU2 and SADS-CoV spike glycoproteins provide insights into coronavirus evolution | 2020 | J Yu, S Qiao, R Guo, X Wang- Nature communications, 2020 - nature.com | structures of HKU2 and SADS-CoV spike glycoproteins provide insights into coronavirus evolution. Download PDF. Article; Open Access; Published: 17 June 2020. Cryo-EM structures of HKU2 and SADS-CoV spike glycoproteins provide insights into coronavirus evolution |
| 9 | 6nb6 | - | https://www.nature.com/articles/s41467-020-17371-6 | Cryo-EM analysis of the post-fusion structure of the SARS-CoV spike glycoprotein | 2020 | X Fan, D Cao, L Kong, X Zhang- Nature communications, 2020 - nature.com | However, structural information of the post-fusion S2 from these highly pathogenic human-infecting The structures of pre- and post-fusion SARS-CoV S glycoprotein dramatically differ This structure suggests potential targets for the development of vaccines and therapies against |
| 10 | 6wpt | - | https://www.nature.com/articles/s41467-020-18058-8 | A cross-reactive human IgA monoclonal antibody blocks SARS-CoV-2 spike-ACE2 interaction | 2020 | M Ejemel, Q Li, S Hou, ZA Schiller, JA Tree- Nature, 2020 - nature.com | COVID-19 caused by SARS-CoV-2 has become a global pandemic requiring the development of interventions for the prevention or treatment to curtail mortality and morbidity. No vaccine to boost mucosal immunity, or as a therapeutic, has yet been developed to SARS-CoV-2. ... However, this predicted epitope of MAb362 is different from the other recently reported MAb complexes to the SARS-CoV-2-RBD (Fig. 3c and Supplementary Fig. 5), including: CR302217 (PDB: 6W41); S30916 (PDB: 6WPT); REGN10933 and REGN1098725; |