SSGCID
Seattle Structural Genomics Center for Infectious Disease

Cited Structures: list of articles citing SSGCID structures

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.

Cited structures

Manually reviewed citations

# PDB Additional SSGCID structures cited Link Title Year Citation Highlighted abstract
1 7jv2 7jvc, 7jw0, 7ra8, 7ral https://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1010260 Structural and antigenic variations in the spike protein of emerging SARS-CoV-2 variants 2022 A Mittal, A Khattri, V Verma- PLoS Pathogens, 2022 - journals.plos.org Recent structural and functional studies have mapped the -CoV-2 variants; (2) the structural basis for antibody-mediated fitness, and in conjunction with the structures of the spike-nAb ... the neutralization mechanism involves direct competition with the ACE2 receptor. These antibodies include C002 (PDB: 7K8S) [70], C104 (PDB: 7K8U) [70], S2H13 (PDB: 7JV2) [77], C119 (PDB: 7K8U) [70], C121 (PDB: 7K8X) [70], LY-CoV555 (PDB: 7KMG), DH1041 (7LAA), COVA2-15 (EMD-22061) [82], 2–43 (EMD-22275) [94],
2 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
3 3dah - https://journals.asm.org/doi/abs/10.1128/MMBR.00040-16 Phosphoribosyl diphosphate (PRPP): biosynthesis, enzymology, utilization, and metabolic significance 2017 B Hove-Jensen, KR Andersen, M Kilstrup- Microbiology and, 2017 - Am Soc Microbiol been crystallized, and high-resolution structures have been determined (4952). A three-dimensional structure has been determined also for the PRPP synthase from the Gram-negative bacterium Burkholderia (Pseudomonas) pseudomallei strain 1710b ( PDB code 3dah ) (53
4 7jzl - https://www.sciencedirect.com/science/article/pii/S0022283621003892 A brief history of de novo protein design: minimal, rational, and computational 2021 DN Woolfson- Journal of Molecular Biology, 2021 - Elsevier For comparison, the whole PDB is doubling in size approximately every 67 years. There are now over 100 structures of de novo peptides and proteins, which is a good resource ... Figure 2. A gallery of high-resolution de novo designed peptide and protein structures .. additional protein chains are shown in grey these are for protein fusions to the designs (6FES99) or with targeted protein-protein interactions (4OYD,5VID,6IWB,6XXV,7JZL,6YWC)
5 4ixo - https://pubs.acs.org/doi/abs/10.1021/acs.chemrev.2c00106 Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere 2022 C Van Stappen, Y Deng, Y Liu, H Heidari- Chemical, 2022 - ACS Publications structure of the active site of cytochrome c peroxidase ( PDB structure of the active site of the F43H/H64L Mb mutant ( PDB bound Ni 2+ ( PDB ID: 4IXO ) and (f) Co 2+ ( PDB ID: 4IWW).
6 7r7n - https://www.nature.com/articles/s41467-022-28882-9 Cryo-EM structure of a SARS-CoV-2 omicron spike protein ectodomain 2022 G Ye, B Liu, F Li- Nature communications, 2022 - nature.com The atomic models generated in this study have been deposited into the PDB with accession number 7TGW (omicron open spike), 7TGX (prototypic open spike), and 7TGY (prototypic ... Forty-nine PDBs of neutralizing antibody/RBD complexes were analyzed using PDBePISA ... 7r7n, 7sn2. Fab: antigen-binding fragment.
7 6ws6 - https://www.science.org/doi/abs/10.1126/scitranslmed.abj7125 A broadly cross-reactive antibody neutralizes and protects against sarbecovirus challenge in mice 2021 DR Martinez, A Schfer, S Gobeil, D Li- Science translational, 2021 - science.org Binding and structural analysis showed high affinity binding of DH1047 to an epitope that is ACE2 (yellow surface representation, PDB 6VW1) binding to RBD is sterically hindered by
8 6wps 7jw0, 7k45, 7jx3, 7jv6, 7jva, 7jvc https://pubs.rsc.org/en/content/articlehtml/2021/sc/d1sc01203g Prediction and mitigation of mutation threats to COVID-19 vaccines and antibody therapies 2021 J Chen, K Gao, R Wang, GW Wei- Chemical science, 2021 - pubs.rsc.org Our predictions are built from the X-ray crystal structure of SARS-CoV-2 S protein and ACE2 ( PDB 6M0J), 57 and various antibodies (PDBs 6WPS , 66 6XC2, 58 6XC3, 58 6XC4, 58 6XC7, 58 6XE1, 64 6XEY, 83 6XKP, 72 6XKQ, 72.
9 5uxx - https://www.nature.com/articles/s41579-020-00450-2 Diverse and unified mechanisms of transcription initiation in bacteria 2020 J Chen, H Boyaci, EA Campbell- Nature Reviews Microbiology, 2020 - nature.com Transcription of DNA is a fundamental process in all cellular organisms. The enzyme responsible for transcription, RNA polymerase, is conserved in general architecture and catalytic function across the three domains of life. ... Fig 5 Mycobacterium tuberculosis σK–RskA (PDB ID 4NQW; panel Ae) 85, Bartonella quintana σE–NepR (PDB ID 5UXX: panel Af),
10 4hr2 - https://www.nature.com/articles/s41594-020-00530-0 Structures of radial spokes and associated complexes important for ciliary motility 2021 M Gui, M Ma, E Sze-Tu, X Wang, F Koh- Nature Structural &, 2021 - nature.com In motile cilia, a mechanoregulatory network is responsible for converting the action of thousands of dynein motors bound to doublet microtubules into a single propulsive waveform. Here, we use two complementary cryo-EM strategies to determine structures of the major