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 |
|---|---|---|
| 9MF3 | 2024 | 0 |
| 9MF6 | 2024 | 0 |
| 9MFC | 2024 | 0 |
| 9MG7 | 2024 | 0 |
| 9MG9 | 2024 | 0 |
| 9MGJ | 2024 | 0 |
| 9MGV | 2024 | 0 |
| 9MGX | 2024 | 0 |
| 9MH2 | 2024 | 0 |
| 9MH4 | 2024 | 0 |
| # | PDB | Additional SSGCID structures cited | Link | Title | Year | Citation | Highlighted abstract |
|---|---|---|---|---|---|---|---|
| 1 | 6q04 | - | https://www.sciencedirect.com/science/article/pii/S1047847721000186 | Spike protein fusion loop controls SARS-CoV-2 fusogenicity and infectivity | 2021 | D Pal- Journal of Structural Biology, 2021 - Elsevier | The structural and dynamics analyses of the Spike show that its fusion loop spatially organizes three fusion peptides contiguous to each other to synergistically I propose a Contact Initiation Model based on the architecture of the Spike quaternary structure that explains the |
| 2 | 6q04 | - | https://www.sciencedirect.com/science/article/pii/S0024320521007608 | Evolutionary selectivity of amino acid is inspired from the enhanced structural stability and flexibility of the folded protein | 2021 | SJA Rao, NP Shetty- Life Sciences, 2021 - Elsevier | Evolutionary selectivity of amino acid is inspired from the enhanced structural stability and flexibility of the folded protein certain positions is governed by a well-orchestrated feedback mechanism, which follows increased stability and flexibility in the folded structure compared to |
| 3 | 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 |
| 4 | 6q04 | - | https://www.biorxiv.org/content/10.1101/2021.02.09.430519v1.abstract | Transformations, Comparisons, and Analysis of Down to Up Protomer States of Variants of the SARS-CoV-2 Prefusion Spike Protein Including the UK Variant B. 1.1. 7 | 2021 | O Basidas, D Kokron, CE Henze- bioRxiv, 2021 - biorxiv.org | Clustal Omega uses a structure guided hidden Markov model (HMM) for multiple sequence alignment. Sequences were obtained directly from the PDB files across four different corona viruses SARS-CoV (6ACD) [14], SARS-CoV-2 (6VSB) [10], MERS-CoV ( 6Q04 ) [20], and |
| 5 | 6q04 | - | https://science.sciencemag.org/content/370/6520/1089.abstract | Structural analysis of full-length SARS-CoV-2 spike protein from an advanced vaccine candidate | 2020 | S Bangaru, G Ozorowski, HL Turner- , 2020 - science.sciencemag.org | Report. Structural analysis of full-length SARS-CoV-2 spike protein from an advanced vaccine candidate 1Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA |
| 6 | 6q04 | - | https://www.tandfonline.com/doi/abs/10.1080/14760584.2020.1813574 | An overview of Middle East respiratory syndrome coronavirus vaccines in preclinical studies | 2020 | N Zhang, J Shang, C Li, K Zhou, L Du- Expert Review of Vaccines, 2020 - Taylor & Francis | Structures of MERS-CoV S1-NTD and MERS-CoV S1-NTD-Neu5Ac complex are presented by ribbon model ( PDB code 6Q04 ) (A) Structure of MERS Both MERS-CoV macro domain and ADP-ribose are presented by ribbon model in green and red, separately ( PDB code 5DUS |
| 7 | 6q04 | 6VXX | https://www.researchsquare.com/article/rs-37300/latest.pdf | N-terminal domain (NTD) of SARS-CoV-2 spike-protein structurally resembles MERS-CoV NTD sialoside-binding pocket | 2020 | M Awasthi, S Gulati, DP Sarkar, S Tiwari, S Kateriya - 2020 - researchsquare.com | W program [14]. Structure preparation The cryo-EM structures of SARS-CoV-2 ( PDB ID: 6VXX) [8] and MERS-CoV ( PDB ID: 6Q04 ) [10] spike spike glycoprotein (YP_009724390. 1) was strongly biased on the crystal structure of SARS-CoV-2, while |
| 8 | 6q05 | - | https://arxiv.org/abs/2002.06196 | Structural modeling of 2019-novel coronavirus (nCoV) spike protein reveals a proteolytically-sensitive activation loop as a distinguishing feature compared to SARS | 2020 | JA Jaimes, NM Andre, JK Millet- arXiv preprint arXiv, 2020 - arxiv.org | Protein Data Base: HCoV-HKU1 ( PDB # 5I08), MHV ( PDB # 3JCL), MERS-CoV ( PDB # 6Q05 ), SARS-CoV ( PDB # 5X58), FCoV-UU4 ( PDB # 6JX7), IBV-M41 ( PDB # 6CV0) and HCoV-NL63 ( PDB # 5SZS). Pairwise S structure . Additional |
| 9 | 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 |
| 10 | 6q05 | - | https://www.journal.atmph-specialissues.org/uploads/179/8422_pdf.pdf | A Review of Current Literature on sudden Upsurge of COVID-19 | 2020 | R Sharma- Annals of Tropical Medicine and Public, 2020 - journal.atmph-specialissues.org | 6Q05 MERSCoV S structure in complex with SialylLewis Available from: http://www.rcsb.org/ pdb /results/results.do?tabtoshow=Unreleased and qrid=7E90BED0 coronavirus papain-like novel protease inhibitors: Design, synthesis, protein-ligand X-ray structure and biological |