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 |
|---|---|---|
| 6Q10 | 2019 | 0 |
| 6Q1Y | 2019 | 0 |
| 6TYJ | 2020 | 0 |
| 6DM6 | 2019 | 0 |
| 5DWM | 2015 | 0 |
| 6DLY | 2019 | 0 |
| 6UCZ | 2019 | 0 |
| 6UDE | 2019 | 0 |
| 6UDG | 2019 | 0 |
| 6UH2 | 2019 | 0 |
| # | PDB | Additional SSGCID structures cited | Link | Title | Year | Citation | Highlighted abstract |
|---|---|---|---|---|---|---|---|
| 1 | 6q09 | - | https://pubs.acs.org/doi/abs/10.1021/acsomega.0c03338 | Correlation of Conservation of Sequence and Structures of Mycobacterial Hemerythrin-like Proteins with Evolutionary Relationship and Host Pathogenicity | 2020 | Z Ma, ML Caldas Nogueira, DP Marchi-Salvador- ACS, 2020 - ACS Publications | Journal Logo. Correlation of Conservation of Sequence and Structures of Mycobacterial Hemerythrin-like Proteins with Evolutionary Relationship and Host Pathogenicity. Zhongxin Ma Zhongxin Ma. Burnett School of Biomedical |
| 2 | 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 |
| 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 | 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 |
| 5 | 6q05 | - | https://www.sciencedirect.com/science/article/pii/S0022283620302874 | Phylogenetic analysis and structural modeling of SARS-CoV-2 spike protein reveals an evolutionary distinct and proteolytically sensitive activation loop | 2020 | JA Jaimes, NM Andr, JS Chappie, JK Millet- Journal of molecular, 2020 - Elsevier | Volume 432, Issue 10, 1 May 2020, Pages 3309-3325. Journal home page for Journal of Molecular Biology. Phylogenetic Analysis and Structural Modeling of SARS-CoV-2 Spike Protein Reveals an Evolutionary Distinct and Proteolytically Sensitive Activation Loop |
| 6 | 6q04 | - | https://www.nature.com/articles/s41594-020-0479-4 | Controlling the SARS-CoV-2 spike glycoprotein conformation | 2020 | R Henderson, RJ Edwards, K Mansouri- Nature structural &, 2020 - nature.com | d, The SARS-2 (left, PDB 6VXX) and MERS (right, PDB 6Q04 ) structures , each with a single protomer depicted in cartoon of the gj angles and dihedrals overlaid on an alignment between a SARS-2 down (cartoon structure with black centroids and lines; PDB 6VXX) and |
| 7 | 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 |
| 8 | 6nae | - | https://www.preprints.org/manuscript/202003.0183 | Two Achilles' Heels of the Ebolavirus Glycoprotein? | 2020 | W Li - 2020 - preprints.org | in complex with a broadly neutralizing human antibody, adi-15946 31 6NAE Crystal Structure Structure of ZEBOV GP in complex with 3T0265 antibody 36 6S8J Structure of ZEBOV 1. Experimentally determined Ebolavirus GP structures inside Protein Data Bank ( PDB [128]) as |
| 9 | 6nb3 | 6nb7, 6nb4, 6nb6, 6vyb, 6vxx | https://link.springer.com/article/10.1007/s00018-020-03580-1 | Protein structure analysis of the interactions between SARS-CoV-2 spike protein and the human ACE2 receptor: from conformational changes to novel | 2020 | I Mercurio, V Tragni, F Busto, A De Grassi- Cellular and Molecular, 2020 - Springer | Download PDF. Download PDF. Original Article; Published: 04 July 2020. Protein structure analysis of the interactions between SARS-CoV-2 spike protein and the human ACE2 receptor: from conformational changes to novel neutralizing antibodies |
| 10 | 6mb1 | - | https://elifesciences.org/articles/57861 | Profiling of myristoylation in Toxoplasma gondii reveals an N-myristoylated protein important for host cell penetration | 2020 | M Broncel, C Dominicus, L Vigetti, SD Nofal, EJ Bartlett- Elife, 2020 - elifesciences.org | structure with bound IMP-1002 ( PDB : 6MB1 , [Schlott et al., 2019]) revealed high sequence identity (57%) and showed that all residues directly involved in compound binding are conserved within the TgNMT active site and therefore predicted to adopt an identical structural |