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 4noz 4mh4 https://pubs.acs.org/doi/abs/10.1021/acscatal.0c01257 Substrate and product-assisted catalysis: molecular aspects behind structural switches along Organic Hydroperoxide Resistance Protein catalytic cycle 2020 R Mateus Domingos, RD Teixeira, A Zeida- ACS, 2020 - ACS Publications The Ohr active site architecture is composed of two cysteines structures (Figure S1). Notably, when analyzing the other Ohr structures available in the PDB , we observed that the position of the Arg-loop in the Bacillus subtilis OhrB (BsOhrB) structure presents an intermediate
2 3p96 - https://www.mdpi.com/1420-3049/25/2/415 Identification and Repurposing of Trisubstituted Harmine Derivatives as Novel Inhibitors of Mycobacterium tuberculosis Phosphoserine Phosphatase 2020 E Pierson, M Haufroid, TP Gosain, P Chopra, R Singh- Molecules, 2020 - mdpi.com SerB2 model generated by homology modeling based on the crystal structure of Mycobacterium avium SerB (Protein Data Bank ( PDB ) entry 3P96 ) is in The docked structure of the best inhibitor, compound 124, is shown in Figure 4. Analysis of those structures shows that
3 4odj - https://onlinelibrary.wiley.com/doi/abs/10.1002/anie.202012623 Engineered SAM synthetases for enzymatic generation of AdoMet analogs with photocaging groups and reversible DNA modification in cascade reactions 2020 F Michailidou, N Klcker- Angewandte Chemie, 2020 - Wiley Online Library Figure 3. A) Superimposed structures of WT-ChMAT ( 4ODJ , shown in yellow) with product bound PC-ChMAT (6LTV, shown in grey) and share a sequence identity of 51% and are highly conserved in the active site (Figure S17), and our structure of PC-ChMAT ( PDB ID: 6LTV
4 4odj - https://pubs.rsc.org/en/content/articlehtml/2019/cc/c9cc07807j Nucleoside-modified AdoMet analogues for differential methyltransferase targeting 2020 NV Cornelissen, F Michailidou, F Muttach- Chemical, 2020 - pubs.rsc.org 39 In addition, we tested the putative wildtype MAT from Cryptosporidium hominis (ChMAT) that had been crystallized by the Seattle Structural Genomics Center for Infectious Disease (SSGCID) but was otherwise ChMAT ( PDB : 4ODJ ) and hMAT2a ( PDB : 5A1G) have 59
5 4ohc - https://pubs.acs.org/doi/abs/10.1021/acscatal.9b05294 Elucidating the Catalytic Reaction Mechanism of Orotate Phosphoribosyltransferase by means of X-ray Crystallography and Computational Simulations 2020 M Roca, S Navas-Yuste, K Zinovjev- ACS, 2020 - ACS Publications Then, the dimeric architecture of OPRTase plays an essential role in the catalysis since The coordinates and structure factors have been deposited in the Protein Data Bank ( PDB ) with accession codes 6TAI (EcOPRT), 6TAJ (EcOPRT/OA) and 6TAK (EcOPRT/OA/SO4 2-). 2.5
6 4ot8 - https://pubs.acs.org/doi/abs/10.1021/acschembio.0c00753 l-Threonine Transaldolase Activity Is Enabled by a Persistent Catalytic Intermediate 2020 P Kumar, A Meza, JM Ellis, GA Carlson- ACS Chemical, 2020 - ACS Publications l-Threonine transaldolases (lTTAs) are a poorly characterized class of pyridoxal-5-phosphate (PLP) dependent enzymes responsible for the biosynthesis of diverse -hydroxy amino acids... The structure was solved by molecular replacement with a distantly related serine hydroxymethyltransferase (PDB ID: 4OT8, 28.2% identity
7 4q04 - https://link.springer.com/article/10.1007/s12551-020-00766-6 Structural and functional diversity of Entamoeba histolytica calcium-binding proteins 2020 S Kumar, S Mishra, S Gourinath- Biophysical Reviews, 2020 - Springer 78% identical). Here, along with the reported structures of amoebic CaBP1, CaBP2, CaBP3, and CaBP5, we have complied the structural information of an unpublished structure of EhCaBP19 ( PDB deposited) as well. In this
8 4q4l - https://pubs.acs.org/doi/abs/10.1021/acs.orglett.0c01922 Design and Synthesis of Near-Infrared Mechanically Interlocked Molecules for Specific Targeting of Mitochondria 2020 RS Das, PC Saha, N Sepay, A Mukherjee- Organic, 2020 - ACS Publications The entrapment of squaraine (SQ) within a molecular container to form rotaxane has been shown to improve the dye stability and the fluorescence proficiency inside the mitochondria. The macrocycle p... The molecular docking of MSQ with Cys exposed mitochondrial protein ATP synthase subunit beta 1 (PDB: 4Q4L), and other SH-exposed proteins showed interactions between the SH moieties and MSQ
9 4qji - https://www.sciencedirect.com/science/article/pii/B9780128179031000097 Natural products encompassing antituberculosis activities 2020 A Monga, A Sharma- Studies in Natural Products Chemistry, 2020 - Elsevier The structure and composition of the cell envelope of M. tuberculosis are distinguished from that of other kinds of prokaryotes S. No. PDB ID, Title, Anti-TB agents 1OY0, Pantothenate kinase, 1e. 4QJI , Phosphopantothenate-cysteine ligase, Phosphopantetheine
10 4twr - https://www.sciencedirect.com/science/article/pii/S1367593120301289 Molecular evolution and functional divergence of UDP-hexose 4-epimerases 2020 S Fushinobu- Current Opinion in Chemical Biology, 2020 - Elsevier Figure 3. Structural basis for the substrate specificity of group 1b and group 2b enzymes The rotated conformation structure was obtained using the S124A/Y149F double mutant ... Substrate-free structures of GalEs from Bacillus anthracis (BAS5114, PDB: 2C20) and Brucella abortus (PDB: 4TWR) are also available in the database