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 |
|---|---|---|
| 7TM8 | 2022 | 0 |
| 7TM7 | 2022 | 0 |
| 7TM6 | 2022 | 0 |
| 7TM5 | 2022 | 0 |
| 7TM4 | 2022 | 0 |
| 7TM0 | 2022 | 0 |
| 7TLZ | 2022 | 0 |
| 7TLY | 2022 | 0 |
| 7TJ3 | 2022 | 0 |
| 7TI7 | 2022 | 0 |
| # | PDB | Additional SSGCID structures cited | Link | Title | Year | Citation | Highlighted abstract |
|---|---|---|---|---|---|---|---|
| 1 | 6q04 | 6VXX | https://www.mdpi.com/1999-4915/12/9/909 | The sialoside-binding pocket of SARS-CoV-2 spike glycoprotein structurally resembles MERS-CoV | 2020 | M Awasthi, S Gulati, DP Sarkar, S Tiwari, S Kateriya- Viruses, 2020 - mdpi.com | Multiple sequence alignment of the NTD domains was performed with the Clustal W program [15]. 2.2. Structure Prediction. The cryo-EM structures of SARS-CoV-2 ( PDB ID: 6VXX) [8] and MERS-CoV ( PDB ID: 6Q04 ) [11] spike glycoproteins were used as the starting point for |
| 2 | 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 |
| 3 | 6q06 | - | https://www.sciencedirect.com/science/article/pii/S0924857920301102 | Structural and molecular modelling studies reveal a new mechanism of action of chloroquine and hydroxychloroquine against SARS-CoV-2 infection | 2020 | J Fantini, C Di Scala, H Chahinian, N Yahi- International journal of, 2020 - Elsevier | N-acetylneuraminic acid (Neu5Ac) was generated with the Hyperchem database. 9-O-acetyl-N-acetylneuraminic acid (9-O-SIA) was retrieved from pdb file 6Q06 [18] Its three-dimensioanl structure was retrieved from pdb file # 4V2O [19] |
| 4 | 6q06 | - | https://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1008943 | Convergent structural features of respiratory syncytial virus neutralizing antibodies and plasticity of the site V epitope on prefusion F | 2020 | W Harshbarger, S Tian, N Wahome, A Balsaraf- PLoS, 2020 - journals.plos.org | ]To fully elucidate the RSB1 paratope and the targeted PreF epitope architecture and better understand the competition with multiple antigenic sites, we determined the crystal structure of the ... Surface potential around PreF residue Asn200 from the structure of RSV B PreF PDB 6Q06 (left), with the RSB1 interacting residue Arg53(LCDR2) is shown again for comparison |
| 5 | 6q06 | 3sia | https://www.mdpi.com/2076-393X/8/4/587 | Host Receptors of Influenza Viruses and CoronavirusesMolecular Mechanisms of Recognition | 2020 | N Sriwilaijaroen, Y Suzuki- Vaccines, 2020 - mdpi.com | A CoV structure with S and HE spikes and positions of S1-NTD and S1-CTD on the S IAVs from avians, either wild birds or domestic birds, typically prefer the 2, 3Sia terminal This representative viral HA is from pdb ID of 3ube, which showed a 2009 pandemic HA in complex... Side view of a surface diagram of a trimeric CoV S protein (pdb: 6q06 [148]) |
| 6 | 6tys | - | https://www.mdpi.com/1999-4915/12/3/342 | Structural insight into paramyxovirus and pneumovirus entry inhibition | 2020 | M Aggarwal, RK Plemper- Viruses, 2020 - mdpi.com | 19,20,21] have furthermore created a novel opportunity for structure -informed mechanistic Structural information is very limited compared to that available for the paramyxovirus attachment Consequently, crystal structures of prefusion PIV5 and NiV F ectodomains could only be |
| 7 | 6uk3 | 5v96, 6aph, 3d64, 3n58, 3glq | https://www.mdpi.com/2218-273X/10/12/1682 | S-adenosyl-l-homocysteine Hydrolase: A Structural Perspective on the Enzyme with Two Rossmann-Fold Domains | 2020 | K Brzezinski- Biomolecules, 2020 - mdpi.com | major [3G1U, unpublished], Cryptosporidium parvum [5HM8 unpublished], Acanthamoeba castellanii [ 6UK3 , unpublished], Naegleria Crystal structures of SAHases were acquired from PDB cofactor-binding domains was performed based on secondary structure assignments in |
| 8 | 3sw5 | 3fq3 | https://link.springer.com/article/10.1134/S0006297920030086 | Effect of Structure Variations in the Inter-subunit Contact Zone on the Activity and Allosteric Regulation of Inorganic Pyrophosphatase from Mycobacterium tuberculosis | 2020 | RS Romanov, SA Kurilova, AA Baykov- Biochemistry (Moscow, 2020 - Springer | of Ec PPase [15, 16], and bound L malate was found in the crystal struc ture of PPase from Bartonella henselae ( PDB ID 3SW5 ) Furthermore, modification of the subunit contact zones does not change the oligomeric structure of Mt PPase, but makes it less compact, as shown |
| 9 | 3cez | 3cxk | https://www.liebertpub.com/doi/abs/10.1089/ars.2020.8037 | Structure and Electron-transfer Pathway of the Human Methionine Sulfoxide Reductase MsrB3 | 2020 | G Javitt, Z Cao, E Resnick, R Gabizon- and Redox Signaling, 2020 - liebertpub.com | MsrB3 molecules per asymmetric unit. The structure was solved by molecular replacement using a bacterial MsrB protein ( PDB code 3CEZ ) with high sequence identity to human MsrB3 (74 of 119 residues, or 62%) (6). Though the amino-terminal segment containing |
| 10 | 4g50 | 3uqb | https://pubs.acs.org/doi/abs/10.1021/acs.jmedchem.0c00911 | Targeting Protein Folding: A Novel Approach for the Treatment of Pathogenic Bacteria | 2020 | NJ Scheuplein, NM Bzdyl, EA Kibble- Journal of Medicinal, 2020 - ACS Publications | Infectious diseases are a major cause of morbidity and mortality worldwide, exacerbated by increasing antibiotic resistance in many bacterial species. The development of drugs with new modes of act... |