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 |
|---|---|---|
| 7TY0 | 2022 | 0 |
| 7TXZ | 2022 | 0 |
| # | PDB | Additional SSGCID structures cited | Link | Title | Year | Citation | Highlighted abstract |
|---|---|---|---|---|---|---|---|
| 1 | 4ed9 | - | http://broncoscholar.library.cpp.edu/handle/10211.3/215321 | Overexpression and Purification of the Protein BaiK for Structural Characterization by X-Ray Crystallography | 2020 | S Khuu - 2020 - broncoscholar.library.cpp.edu | Initially , BaiK was overexpressed to produce large quantity of protein for use in structural and structure being very similar to histidine while also being added at a high concentration. 11 formation of more ordered crystal structures . The effective concentration of the protein |
| 2 | 3vab | - | https://www.biorxiv.org/content/10.1101/2020.10.01.322594v1.full-text | The Phaeodactylum tricornutum Diaminopimelate Decarboxylase was Acquired via Horizontal Gene Transfer from Bacteria and Displays Substrate | 2020 | VA Bielinski, JK Brunson, A Ghosh, MA Moosburner- bioRxiv, 2020 - biorxiv.org | in the active site. The structure underscores features unique to the PtLYSA clan of DAPDC and provides structural insight into the determinants responsible for the substrate-promiscuity observed in PtLYSA. ... Akin to protomer 2 of PtLYSA, this segment is not included in the structures of DAPDC from Aquifex aeolicus (PDB 2P3E) and Brucella melitensis (PDB 3VAB). |
| 3 | 3gwc | - | https://pubs.acs.org/doi/abs/10.1021/acsomega.0c01224 | dUMP/F-dUMP Binding to Thymidylate Synthase: Human Versus Mycobacterium tuberculosis | 2020 | K Gaurav, T Adhikary, P Satpati- ACS omega, 2020 - ACS Publications | Thymidylate synthase is an enzyme that catalyzes deoxythymidine monophosphate (dTMP) synthesis from substrate deoxyuridine monophosphate (dUMP). Thymidylate synthase of Mycobacterium tuberculosis (... (a) X-ray structure of MtbThyX (homotetramer; monomeric units are in yellow, cyan, green and purple, PDB 3GWC(16)). Each ligand-binding site (out of four) is at the intersection of three monomeric units. |
| 4 | 3gbz | - | https://pubs.rsc.org/en/content/articlehtml/2020/me/c9me00097f | How evolution designs functional free energy landscapes of proteins? A case study on emergence of regulation in CDK family kinases. | 2020 | Z Shamsi, D Shukla- Molecular Systems Design & Engineering, 2020 - pubs.rsc.org | structures of CDK2 ( PDB ID: 5OSM, 6Q3F, 6Q4A, 6Q4B, 6Q4C, 6Q4D, 6Q4K), G/CDK ( PDB ID: 3GBZ ), and pfpk5 structures are native-like based on GA341 score and have comparable DOPE score with CDK2 native structure as shown in PDB ID for CMGI for native CDK2 score |
| 5 | 6wpt | - | https://www.sciencedirect.com/science/article/pii/S0165614720301668 | Fruitful neutralizing antibody pipeline brings hope to defeat SARS-Cov-2 | 2020 | A Renn, Y Fu, X Hu, MD Hall, A Simeonov- Trends in pharmacological, 2020 - Elsevier | and a receptor-binding subdomain also referred to as receptor binding motif (RBM, residues 438505) which loops out of the core domain structure to directly The structures used for superimposition of S309 and CR3022 are with RBD of SARS-CoV-2 ( PDB 6WPT [41] and |
| 6 | 5dvw | - | https://core.ac.uk/download/pdf/323470394.pdf | Napovedni modeli za identifikacijo potencialnih inhibitorjev razlinih proteinov virusa ebole | 2020 | V Hudi - 2020 - core.ac.uk | Monte Carlo MLR Multivariatna linearna regresija mRNA Informacijska ribonukleinska kislina NP Nukleoprotein PCA Metoda glavnih komponent PDB Podatkovna knjinica Knowledge of the viral structure gives us insight into the functioning of the virus and allows us to predict |
| 7 | 6nb7 | 6nb8, 6wps, 6wpt, 6ws6 | https://www.sciencedirect.com/science/article/pii/S1471490620302118 | Structural basis of SARS-CoV-2 and SARS-CoVantibody interactions | 2020 | E Gavor, YK Choong, SY Er, H Sivaraman- Trends in, 2020 - Elsevier | While the binding of COV21 to the S-glycoprotein resembles the binding of the SARS-CoV S230( PDB : 6NB7 )[73], the binding interface SARS-CoV-2-S-S309-Fab[12] complex ( PDB : 6WPS/6WPT/6WS6) and the crystal structure of SARS |
| 8 | 6x79 | - | https://pubs.acs.org/doi/abs/10.1021/acsomega.0c03512 | Characterization of the SARS-CoV-2 S protein: biophysical, biochemical, structural, and antigenic analysis | 2020 | NG Herrera, NC Morano, A Celikgil, GI Georgiev- ACS, 2020 - ACS Publications | need to produce large quantities of high-quality SARS-CoV-2 Spike (S) protein for use in both clinical and basic science settings. To address this need, we have evaluated the expression and purification of two previously reported S protein constructs in Expi293F and ExpiCHO-S cells... In nine structures that align well in this region (conformation 1: 6VXX, 6X29, 6X2C, 6X79, 6ZOX, 6ZOY, 6ZP0, 6ZP1, 6ZWV), the amino acid segment 621–640 was not modeled, presumably due to disorder |
| 9 | 3lr0 | - | https://arxiv.org/abs/2009.07466 | The role of hydrophobic interactions in folding of -sheets | 2020 | J Li, X Ma, H Zhang, C Hou, L Shi, S Guo- arXiv preprint arXiv, 2020 - arxiv.org | Nature Structural Biology 10, 980, doi:10.1038/nsb1203-980 (2003). 19 Berman, H., Henrick, K., Nakamura, H. & Markley, JL The worldwide Protein Data Bank (wwPDB): ensuring a single, uniform archive of PDB data Structure relaxation via long trajectories made stable |
| 10 | 3u0g | - | https://link.springer.com/article/10.1007/s00253-020-10369-6 | Structural insight into the substrate specificity of PLP fold type IV transaminases | 2020 | EY Bezsudnova, VO Popov, KM Boyko- Applied Microbiology and, 2020 - Springer | Due to the rigid structure of the -sheet, the residues constituting it form a peculiar mold for substrate binding. The interdomain loop (light blue) and -turn (black) of the large domain of the first subunit confine the P-pocket from the other sides PDB ID:*. X-strand 3U0G |