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 |
---|---|---|
5VN4 | 2017 | 5 |
4JNQ | 2013 | 5 |
4J07 | 2013 | 5 |
3IEW | 2009 | 5 |
4W65 | 2014 | 5 |
3PGZ | 2010 | 5 |
3PFD | 2010 | 5 |
3GBZ | 2009 | 5 |
3ENN | 2008 | 5 |
3HWI | 2009 | 5 |
# | PDB | Additional SSGCID structures cited | Link | Title | Year | Citation | Highlighted abstract |
---|---|---|---|---|---|---|---|
1 | 4g7f | - | https://www.sciencedirect.com/science/article/pii/S1093326319305844 | In silico repositioning of etidronate as a potential inhibitor of the Trypanosoma cruzi enolase | 2020 | EA Valera-Vera, M Say, C Reigada- Journal of Molecular, 2020 - Elsevier | Preparation of the PDBQT files (Protein Data Bank, partial charge (Q), and atom type (T)) was performed using AutoDock Tools v1.5.6 [29]. A search in the Protein Data Bank ( PDB ) [30] was carried to find the crystal structure of TcENO ( PDB ID: 4G7F , Resolution: 2.4 , R |
2 | 4qfh | 4g7f, 4gie | https://www.mdpi.com/2218-273X/9/9/484 | Insights into Ergosterol Peroxide's Trypanocidal Activity | 2019 | T Meza-Menchaca, A Ramos-Ligonio- Biomolecules, 2019 - mdpi.com | \To identify potential Tc proteins that might directly interact with ergosterol peroxide, an inverse-docking screening was performed on a subset of Tc protein crystallography structures.. Table 1. The best matches between T. cruzi proteins and ergosterol peroxide in descending order of ∆G predictive value ... Dihydroorotate dehydrogenase 4QFH 3W1R −9.1 −11.17 6.407 |
3 | 3rrp | - | https://www.sciencedirect.com/science/article/pii/S0141022918302370 | Enhancing the thermostability of fumarase C from Corynebacterium glutamicum via molecular modification | 2018 | L Lin, Y Wang, M Wu, L Zhu, L Yang, J Lin- Enzyme and microbial, 2018 - Elsevier | The modeled structure of cgFumC was completed through homology modeling with the Swiss-Model server by using the crystal structure of the fumarate hydratase Fum ( PDB ID: 3RRP ) from Mycobacterium abscessus as a template, which shares a 75.76% sequence |
4 | 6brl | - | https://onlinelibrary.wiley.com/doi/abs/10.1002/jimd.12387 | Metabolic impact of pathogenic variants in the mitochondrial glutamyltRNA synthetase EARS2 | 2021 | M Ni, LF Black, C Pan, H Vu, J Pei, B Ko- Journal of Inherited, 2021 - Wiley Online Library | 3A and B). Structural modeling of human EARS2 was obtained from the SWISS-MODEL Page 10. repository (Bienert et al 2017) based on the crystal structure of the glutamyl-tRNA synthetase from Elizabethkingia meningosepticum ( PDB : 6brl ), and superimposed on the crystal |
5 | 5deo | - | https://pubs.acs.org/doi/abs/10.1021/acschembio.9b00124 | Novel antimycobacterial compounds suppress NAD biogenesis by targeting a unique pocket of NaMN adenylyltransferase | 2019 | AL Osterman, I Rodionova, X Li, E Sergienko- ACS chemical, 2019 - ACS Publications | ADVERTISEMENT. Log In Register. Cart. ACS; ACS Publications; C&EN; CAS. ACS Publications: ACS Journals; ACS eBooks; C&EN Global Enterprise. A; Accounts of Chemical Research; ACS Applied Bio Materials; ACS Applied Electronic |
6 | 3m4s | - | https://www.nature.com/articles/srep30494 | Crystal structures of RidA, an important enzyme for the prevention of toxic side products | 2016 | X Liu, J Zeng, X Chen, W Xie- Scientific reports, 2016 - nature.com | 2DYY, dirty violet), and Entamoeba histolytica l-PSP ( PDB code 3M4S , gray) respectively unpublished), and a putative endoribonuclease l-PSP from Entamoeba histolytica ( PDB code3M4S, unpublished AtRidA is highly similar to other RidA family members in structure , and their |
7 | 3eiy | - | https://arxiv.org/abs/2012.05716 | Utilising Graph Machine Learning within Drug Discovery and Development | 2020 | T Gaudelet, B Day, AR Jamasb, J Soman- arXiv preprint arXiv, 2020 - arxiv.org | and evolve along a temporal dimension resulting in changes to composition, structure and attributes One such approach is to use a graph's structural information to regularise embeddings authors suggest the atten- tion mechanism is decoupled from the architecture and should |
8 | 5thw | 4wjb, 5i4m | https://www.nature.com/articles/s41598-018-31259-y | A fundamental catalytic difference between zinc and manganese dependent enzymes revealed in a bacterial isatin hydrolase | 2018 | T Sommer, K Bjerregaard-Andersen, L Uribe- Scientific reports, 2018 - nature.com | with a central scaffold resembling the swivelling // fold 18 , while the majority of AHS members contains a monomeric (/) 8 -TIM like-barrel structural fold 19 The finalised model and structure factors were deposited to Protein Data Bank ( PDB ) and given the PDB |
9 | 5cy4 | - | https://www.nature.com/articles/s41598-019-39641-0 | Structural basis of small RNA hydrolysis by oligoribonuclease (Cps ORN) from Colwellia psychrerythraea strain 34H | 2019 | CW Lee, SH Park, CS Jeong, SS Cha, H Park- Scientific reports, 2019 - nature.com | Structure alignment search using DALI server showed that CpsORN exhibited high structural similarity with ORN HinORN; PDB code 1J9A), and Acinetobacter baumannii (AbaORN; PDB code 5CY4 ), and XC847 from Xanthomonas campestris (XcaORN; PDB code 2GBZ |
10 | 5k85 | - | https://www.sciencedirect.com/science/article/pii/S0022283619303092 | Structures of 2-Hydroxyisobutyric Acid-CoA Ligase Reveal Determinants of Substrate Specificity and Describe a Multi-Conformational Catalytic Cycle | 2019 | M Zahn, N Kurteva-Yaneva, J Schuster, U Krug- Journal of molecular, 2019 - Elsevier | The substrate specificity of HCL corresponds well to the adenylate-forming active-site architecture ... This is in contrast to other ANL ligase structures, where the CoA or acyl-CoA molecules adopt more stretched conformations, for example, in the thioester-forming conformations of bacterial [38] and fungal acetyl-CoA synthetase (PDB ID: 5K85), |