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 3krs - https://www.mdpi.com/2076-2607/8/1/40 Gene Cloning, Recombinant Expression, Characterization, and Molecular Modeling of the Glycolytic Enzyme Triosephosphate Isomerase from Fusarium oxysporum 2020 B Hernndez-Ochoa, S Gmez-Manzo- Microorganisms, 2020 - mdpi.com Triosephosphate isomerase (TPI) is a glycolysis enzyme, which catalyzes the reversible isomerization between dihydroxyactetone-3-phosphate (DHAP) and glyceraldehyde-3-phosphate (GAP). In pathogenic organisms, TPI is essential to obtain the energy used to survive and infect ... Figure 2. Bioinformatic analysis of FoxTPI with other triosephosphate isomerases (TPIs)... , 3KRS (Cryptosporidium Parvum), 5UPR (Toxoplasma gondii),
2 5i7w - https://onlinelibrary.wiley.com/doi/abs/10.1111/jeu.12834 Characterization of Cystathionine Synthase TtCbs1 and Cysteine Synthase TtCsa1 Involved in Cysteine Biosynthesis in Tetrahymena thermophila 2020 H Lv, J Xu, T Bo, W Wang- Journal of Eukaryotic Microbiology, 2020 - Wiley Online Library TtCsa1 has more than 30% sequence identities with B. abortus CS ( PDB ID: 5JIS) (Dharavath et al. 2017), B. suis CS ( PDB ID: 5I7W ), and L. major CS ( PDB ID: 4AIR) (Fyfe et al. 2012), and we modeled the overall structure of TtCsa1 with these crystal structures
3 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
4 3t7c 3s55 https://www.biorxiv.org/content/10.1101/2020.10.15.341941v1.abstract Structural studies on M. tuberculosis decaprenyl phosphoryl--D-ribose epimerase-2 enzyme involved in cell wall biogenesis 2020 SP Gangwar, A Bandyopadhyay, AK Saxena- bioRxiv, 2020 - biorxiv.org The MtbDprE2 structure was aligned with structures of PDB database using TM- structural alignment program of I-TASSER server, which yielded ten closest structural homologs (as coverage=97.2% [54] (vi) PDB - 3t7c , identity=13.3%, coverage=97.2% [55] (vii) PDB -1ipe
5 5umh - https://pubs.acs.org/doi/abs/10.1021/acs.jcim.0c00802 Estimating Change in Foldability Due to Multipoint Deletions in Protein Structures 2020 A Banerjee, A Kumar, KK Ghosh- Journal of Chemical, 2020 - ACS Publications Figure S6: Root mean-square fluctuation of each residue of the protein in its original conformation (in magenta) and of the protein subject to MPD in residue stretches in the nonloop region (in sea green) for PDB IDs: 4XGQ chain A, 5UMH chain A, 4A5M chain A, 3GUD chain A, and...
6 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]
7 6bfu 6nb6, 6nb7, 6nb3, 6tys, 6q04 https://papers.ssrn.com/sol3/papers.cfm?abstract_id=3541361 Candidate targets for immune responses to 2019-Novel Coronavirus (nCoV): sequence homology-and bioinformatic-based predictions 2020 A Grifoni, J Sidney, Y Zhang- -HOST-MICROBE-D, 2020 - papers.ssrn.com with data about immune epitopes, protein structures , and host responses to virus infections (Pickett et al., 2012) glycoprotein structure ( PDB : 6ACD). The calculated surface of the top 10 amino acid residues Non- structural protein 3b 2 0 Protein 7a 2 0 Protein 9b 2 0
8 3oc6 - https://www.mdpi.com/1422-0067/21/14/4831 Characterizing the Fused TvG6PD:: 6PGL Protein from the Protozoan Trichomonas vaginalis, and Effects of the NADP+ Molecule on Enzyme Stability 2020 L Morales-Luna, B Hernndez-Ochoa- International journal of, 2020 - mdpi.com This report describes a functional and structural analysis of fused glucose-6-phosphate dehydrogenase dehydrogenase-phosphogluconolactonase protein from the protozoan Trichomonas vaginalis (T. vaginalis). The glucose-6-phosphate dehydrogenase (g6pd) gene ... Structural superposition of the 6PGL crystal structure from Mycolicibacterium smegmatis MC2 155 (PDB entry 3OC6, steel blue) with the C-terminal 6PGL region of the TvG6PD::6PGL model (spring green).
9 3p0x - https://www.sciencedirect.com/science/article/pii/S0166685120300992 Characterisation and structural analysis of glyoxylate cycle enzymes of Teladorsagia circumcincta 2020 S Umair, C Bouchet, N Palevich, HV Simpson- Molecular and Biochemical, 2020 - Elsevier to compare the TciICL and TciMS protein sequences with deposited structures in the Protein Data Bank ( PDB ) Locations are shown of the C- and N-terminus in the predicted tertiary structure of TciICL C) and TciMS in salmon (F) within 4 of the superimposed 3P0X and 3S9Z
10 3p96 - https://www.sciencedirect.com/science/article/pii/S0006291X20314042 Biochemical characterization of phosphoserine phosphatase SerB2 from Mycobacterium marinum 2020 E Pierson, J Wouters- Biochemical and Biophysical Research, 2020 - Elsevier MmaSerB2 and MtbSerB2 are similar in their catalytic behaviour and architecture . Fig. 2. A) Structure of MmaSerB2 modeled by homology on the basis of M. avium SerB structure ( PDB 3P96 ). The individual domains are labelled. Active site residues are shown in red