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 5i1f - https://www.sciencedirect.com/science/article/pii/S1570963917302959 Crystal structure of d-glycero--d-manno-heptose-1-phosphate guanylyltransferase from Yersinia pseudotuberculosis 2017 H Kim, J Park, S Kim, DH Shin- et Biophysica Acta (BBA)-Proteins and, 2017 - Elsevier A PSI-BLAST search targeting PDB showed that the sequences of eight crystal structures (4Y7U, 5I1F , 4ECM, 4AAW, 1WVC, 5L6S, 5B04, 2CU2) have strong The homologue structures are detected with the Dali server using a YpHddC structure as a template
2 4p8r 4lsm https://www.sciencedirect.com/science/article/pii/S1570963918300220 Structural studies of glyceraldehyde-3-phosphate dehydrogenase from Naegleria gruberi, the first one from phylum Percolozoa 2018 ATP Machado, M Silva, J Iulek- et Biophysica Acta (BBA)-Proteins and, 2018 - Elsevier cruzi (glicosomal) ( PDB : 4LSM) [12], Trypanosoma brucei (glicosomal) ( PDB : 4P8R ) [13], Leishmania 3PYM), Homarus americanus ( PDB : 1GPD) [46] and Escherichia coli ( PDB : 1GAD) [47 general, they are similar, with some differences in secondary structure elements; RMSD
3 4ed9 - https://www.sciencedirect.com/science/article/pii/S1570963918301808 Rv3272 encodes a novel Family III CoA transferase that alters the cell wall lipid profile and protects mycobacteria from acidic and oxidative stress 2018 KS Shrimant, S Pandey, A Ansari, S Das- et Biophysica Acta (BBA, 2018 - Elsevier The structure was found similar to the homologues available including MCR ( PDB ID: 1X74), CaiB ( PDB ID: 1XA3), FRC ( PDB ID: 2VJQ), FRC ( PDB ID: 3UBM), ACOCT ( PDB ID: 4ED9 ), YfdE ( PDB ID: 4HL6 3.5. Solution structure using Small Angle X-ray Scattering (SAXS).
4 3ido 3jvi https://www.sciencedirect.com/science/article/pii/S1570963918302012 Vibrio cholerae LMWPTP-2 display unique surface charge and grooves around the active site: Indicative of distinctive substrate specificity and scope to design specific 2019 S Chatterjee, S Nath, B Ghosh, U Sen- Biochimica et Biophysica Acta (BBA, 2019 - Elsevier The surface properties of VcLMWTP-1, although have some distinct features, resembles closely to that of E. histolytica LMWPTP ( PDB : 3IDO ) This closure at the P-loop is also evident from the structural alignment with an 'open structure ' of apo-MPtpA ( PDB : 2LUO) [41] to the
5 5b8i - https://www.sciencedirect.com/science/article/pii/S1570963919300445 Fungal Lanosterol 14-demethylase: A target for next-generation antifungal design 2020 BC Monk, AA Sagatova, P Hosseini, YN Ruma- et Biophysica Acta (BBA, 2020 - Elsevier cerevisiae LDM as a template ( PDB 4LXJ), suggested that crystal structure of the catalytic domain of human CYP51 ( PDB calcineurinB in complex with FK506 ( 5B8I ); S. cerevisiae Elf2
6 3k9w - https://www.sciencedirect.com/science/article/pii/S1570963919300469 Structural and binding studies of phosphopantetheine adenylyl transferase from Acinetobacter baumannii 2019 A Gupta, PK Singh, N Iqbal, P Sharma- et Biophysica Acta (BBA, 2019 - Elsevier PDB ID: 3ND5; 12), HpPPAT ( PDB ID: 3NV7; 13), BpPPAT ( PDB ID: 3K9W ; 14), CbPPAT ( PDB ID: 4F3R; unpublished), PaPPAT ( PDB ID: 3X1J; 15) and MaPPAT ( PDB ID: 5O06 As indicated by the structure of AbPPAT with CoA ( PDB ID: 5YH7), the ligand binding cleft
7 4whx 3u0g https://www.sciencedirect.com/science/article/pii/S1570963919300494 Functional characterization of PLP fold type IV transaminase with a mixed type of activity from Haliangium ochraceum 2019 YS Zeifman, KM Boyko, AY Nikolaeva- et Biophysica Acta (BBA, 2019 - Elsevier These results complement our knowledge of the catalytic diversity of transaminases and indicate the need for further research to understand the structural basis of substrate specificity in these enzymes. Abbreviations PDB entry code, 6H65. 2.8. Structure solution and refinement
8 3dmp 3qbp, 3e5b, 3hm0 https://www.sciencedirect.com/science/article/pii/S1570963920301515 Tetramer protein complex interface residue pairs prediction with LSTM combined with graph representations 2020 D Sun, X Gong- Biochimica et Biophysica Acta (BBA)-Proteins and, 2020 - Elsevier The structure diagram of LSTM neural network is shown in Fig. 3. (See Fig. 1, Fig Table 1. Dataset. DataSet, PDB ID 2H8N, 2JBR, 2NQO, 2Y32, 3DFQ, 3ESI, 3G7K, 3HM0, 3OHP, 3RD4, 3 V15, 1IZ1, 1JL2. 1KAM, 1NSW, 2GJD, 2R90, 2ZYZ, 3CDK, 3CO2, 3DMP , 3F6Z, 1BV4, 1YIF
9 5ts2 3pxu https://www.sciencedirect.com/science/article/pii/S1570963920302132 Phosphopantetheine Adenylyltransferase: A promising drug target to combat antibiotic resistance 2020 A Gupta, P Sharma, TP Singh, S Sharma- Biochimica et Biophysica Acta, 2020 - Elsevier Although, the DPCK domain of the human fusion protein shows high sequence and structural homology to bacterial DPCK The PDB IDs of the structure , percentage sequence identities and rms deviations for the C atoms are also indicated ... The structures of complexes of PPAT with dPCoA from several bacterial species have been determined so far and include EcPPAT (PDB ID: 1B6T), MtPPAT (PDB ID: 3RBA), BpPPAT (PDB ID: 3PXU), MaPPAT (PDB ID: 5O08), PaPPAT (PDB ID: 5TS2) and AbPPAT (PDB ID: 5ZZC
10 3cxk - https://www.sciencedirect.com/science/article/pii/S1570963920302223 Functional characterization of methionine sulfoxide reductases from Leptospira interrogans 2020 N Sasoni, MD Hartman, SA Guerrero- et Biophysica Acta (BBA, 2020 - Elsevier The Met oxidation could change the structure and function of many proteins, not only of those redox-related but also of others involved in different metabolic pathways. Until now, there is no information about the presence or function of Msrs enzymes in Leptospira interrogans