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 |
|---|---|---|
| 3PZY | 2011 | 0 |
| 7SSQ | 2023 | 0 |
| 3P2Y | 2010 | 0 |
| 7SL5 | 2022 | 0 |
| 3OA3 | 2010 | 0 |
| 3O0K | 2010 | 0 |
| 5SCN | 2022 | 0 |
| 2MZY | 2015 | 0 |
| 3N7T | 2010 | 0 |
| 3LUZ | 2010 | 0 |
| # | PDB | Additional SSGCID structures cited | Link | Title | Year | Citation | Highlighted abstract |
|---|---|---|---|---|---|---|---|
| 1 | 5dd7 | - | https://repository.up.ac.za/handle/2263/77810 | Structural and inhibition studies of thiamine monosphosphate kinase from Mycobacterium tuberculosis | 2020 | LS Dlamini - 2020 - repository.up.ac.za | OT Oxythiamine PDB Protein data bank 38 Figure 3.5: Crystal structure of MtbThiL homodimer ..... 40 bind to both free enzyme and the ES complex. Detailed structural information particularly high resolution crystal structures of substrate |
| 2 | 3mx6 | - | https://www.mdpi.com/2218-273X/10/4/659 | P1 Residue-Oriented Virtual Screening for Potent and Selective Phosphinic (Dehydro) Dipeptide Inhibitors of Metallo-Aminopeptidases | 2020 | M Talma, A Mucha- Biomolecules, 2020 - mdpi.com | 20 to keep the size similar to the grid from the first step (36 for PDB : 2EK8 In general, the structure proposed here surpasses known inhibitors As the overall architecture of the S1 binding sites of porcine, bacterial, and protozoal APNs is rather conserved, the advantageous ... Table 1. Cont. Rickettsia prowazekii 3MX6 [41] |
| 3 | 6vxx | - | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7505244/ | Comparative molecular docking analysis of the SARS CoV-2 Spike glycoprotein with the human ACE-2 receptors and thrombin | 2020 | P Bhanu, NH Kumar, SH Kumar, M Relekar- , 2020 - ncbi.nlm.nih.gov | PDB ID, Ligand, Binding Pose, Binding Energy (Kcal/mol), RMSD, Receptor, Bond Length ( Figure 1a: Structural representation of 6VXX and thrombin, Figure 1b: Molecular interaction of with the 7th pose, Key - the sticks represents thrombin, the secondary structure represents the |
| 4 | 3f0d | - | https://pubs.acs.org/doi/abs/10.1021/acsomega.0c01337 | Upgraded AMBER Force Field for Zinc-Binding Residues and Ligands for Predicting Structural Properties and Binding Affinities in Zinc-Proteins | 2020 | M Macchiagodena, M Pagliai, C Andreini, A Rosato- ACS, 2020 - ACS Publications | Journal Logo. Upgraded AMBER Force Field for Zinc-Binding Residues and Ligands for Predicting Structural Properties and Binding Affinities in Zinc-Proteins. Marina Macchiagodena Marina Macchiagodena. Dipartimento di |
| 5 | 3rr6 | 3qdf, 4pfz, 4maq | https://sfamjournals.onlinelibrary.wiley.com/doi/abs/10.1111/1462-2920.14844 | Sequence, structure and functionbased classification of the broadly conserved FAH superfamily reveals two distinct fumarylpyruvate hydrolase subfamilies | 2020 | H Hong, H Seo, W Park, KJ Kim- Environmental microbiology, 2020 - Wiley Online Library | This article is protected by copyright. All rights reserved. Page 24. uncharacterized protein from M. abscessus DSM 44196 ( PDB code 3RR6 , 36 % sequence identity) as a search model. The structure model was built using the WinCoot program (Emsley |
| 6 | 6bfu | - | https://journals.asm.org/doi/abs/10.1128/jvi.01301-20 | Cryo-electron microscopy structure of the swine acute diarrhea syndrome coronavirus spike glycoprotein provides insights into evolution of unique coronavirus spike | 2020 | H Guan, Y Wang, V Perulija, AFUH Saeed- Journal of, 2020 - Am Soc Microbiol | HCoV-NL63 ( PDB accession number 5SZS); (C) S trimer of the deltacoronavirus PdCoV ( PDB accession number 6BFU ); (D) S bronchitis virus (IBV) ( PDB accession number 6CV0); (E) S trimer of the betacoronavirus SARS-CoV ( PDB accession number 5X58 (F) Structure of the |
| 7 | 6bfu | - | https://www.nature.com/articles/s41594-020-0478-5 | A thermostable, closed SARS-CoV-2 spike protein trimer | 2020 | X Xiong, K Qu, KA Ciazynska, M Hosmillo- Nature Structural &, 2020 - nature.com | Structures of the disulfide-stabilized and non-disulfide-stabilized proteins reveal distinct closed and locked conformations of the S trimer with the target cell, and is a dominant target of the immune system 4 . S protein is trimeric and has two distinct structural statesprefusion ... porcine deltacoronavirus (PDCoV, a deltacoronavirus, PDBID: 6BFU). S proteins are structurally aligned based on S2. S protein trimers from all 4 genera of |
| 8 | 5cy4 | - | https://munin.uit.no/handle/10037/17279 | A functional and structural study of three bacterial nucleic acid-interacting proteins. The story of a Ferric Uptake Regulator, an Oligoribonuclease and an ATP | 2020 | K Berg - 2020 - munin.uit.no | Acinetobacter baumannii (PDB 5CY4) and E. coli (PDB code 1YTA )[148]. All Orn homologs are structurally similar and topologically arranged |
| 9 | 6q04 | - | https://www.sciencedirect.com/science/article/pii/S0079610720301103 | Human coronavirus spike protein-host receptor recognition | 2020 | L Guruprasad- Progress in biophysics and molecular biology, 2020 - Elsevier | cause infection. In this review, we discuss structural features of HCoV spike proteins and recognition of host proteins and carbohydrate receptors. Keywords. Human coronavirus. SARS-CoV. SARS-CoV-2. MERS-CoV. HCoV-HKU1. |
| 10 | 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 |