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 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
2 4f47 - https://pubs.acs.org/doi/abs/10.1021/acsinfecdis.0c00329 Post-translational Succinylation of Mycobacterium tuberculosis Enoyl-CoA Hydratase EchA19 Slows Catalytic Hydration of Cholesterol Catabolite 3-Oxo-chol-4,22 2020 AC Bonds, T Yuan, JM Werman, J Jang- ACS Infectious, 2020 - ACS Publications Cholesterol is a major carbon source for Mycobacterium tuberculosis (Mtb) during infection, and cholesterol utilization plays a significant role in persistence and virulence within host macrophages...
3 5vir 4fry, 4ymi https://pubs.acs.org/doi/abs/10.1021/acsinfecdis.0c00735 Structural and Molecular Dynamics of Mycobacterium tuberculosis Malic Enzyme, a Potential Anti-TB Drug Target 2020 KH Burley, BJ Cuthbert, P Basu- ACS Infectious, 2020 - ACS Publications \ Interestingly, the three top-scoring NADP+ molecules are found in structures of Mtb nicotinamide-mononucleotide adenylyltransferase (NadD) (PDB ID: 4S1O) and Mycobacterium abscessus NadD (PDB ID: 4YMI and 5VIR). These results
4 4kzp - https://pubs.acs.org/doi/abs/10.1021/acsinfecdis.1c00069 Enzymatic -Oxidation of the Cholesterol Side Chain in Mycobacterium tuberculosis Bifurcates Stereospecifically at Hydration of 3-Oxo-cholest-4,22-dien-24-oyl-CoA 2021 T Yuan, JM Werman, X Yin, M Yang- ACS Infectious, 2021 - ACS Publications The unique ability of Mycobacterium tuberculosis (Mtb) to utilize host lipids such as cholesterol for survival, persistence, and virulence has made the metabolic pathway of cholesterol an area of great interest for therapeutics development. Herein, we identify and characterize two genes from the Cho-region (... A search model for the apo-protein was created from 4KZP and the holo-protein model was created from the ChsB1 apo-protein model.
5 6uld - https://pubs.acs.org/doi/abs/10.1021/acsinfecdis.5c00996 The Pyridoxal-5-Phosphate-Dependent Enzymes of Mycobacterium tuberculosis 2026 A Peracchi, B Baker- ACS Infectious Diseases, 2026 - ACS Publications from the PDB database (sequences derived from structural studies). Initially this search yielded 87 hits, many of which, however, were not pertinent (such as enzymes involved in the
6 4wkw - https://pubs.acs.org/doi/abs/10.1021/acsinfecdis.7b00111 Identification of a Mycothiol-Dependent Nitroreductase from Mycobacterium tuberculosis 2018 A Negri, P Javidnia, R Mu, X Zhang- ACS infectious, 2018 - ACS Publications Compared with published crystal structures of Rv2466c (PDB ID: 4NXI, 4ZIL) and the M. leprae homologue (PDB ID: 4WKW), there were significant conformational changes in one subunit of our structure
7 4k73 - https://pubs.acs.org/doi/abs/10.1021/acsinfecdis.8b00244 Structural Basis for the Interaction and Processing of -Lactam Antibiotics by l,d-Transpeptidase 3 (LdtMt3) from Mycobacterium tuberculosis 2019 GA Libreros-Ziga, C dos Santos Silva- ACS Infectious, 2019 - ACS Publications Structural Basis for the Interaction and Processing of -Lactam Antibiotics by l,d-Transpeptidase 3 These structures revealed a fold and catalytic diad similar to those of other Ldts Mt The Ldt Mt3 faropenem structure indicated that faropenem is degraded after Cys-246 acylation The phases were obtained by molecular replacement with Phaser53 from CCP4 suite,54 adopting the PDB entries 4K73 and 5DU727 as models for LdtMt3 and LdtMt5 structures, respectively
8 6vxx - https://pubs.acs.org/doi/abs/10.1021/acsmedchemlett.0c00410 Structural impact of mutation D614G in SARS-CoV-2 spike protein: enhanced infectivity and therapeutic opportunity 2020 A Fernndez- ACS medicinal chemistry letters, 2020 - ACS Publications Figure 1. Structural and epistructural interactions at the S1/S2 interface in the spike protein of SARS-CoV-2. (a) Positioning of D614 in the S1 chain (magenta) relative to T859 in the S2 chain (blue) at the S1/S2 interface for the spike protein structure reported in PDB6VXX
9 4jv3 4f32 https://pubs.acs.org/doi/abs/10.1021/acsmedchemlett.0c00653 Semisynthesis and Biological Evaluation of Platencin Thioether Derivatives: Dual FabF and FabH Inhibitors against MRSA 2021 Y Li, X Weng, Y Deng, J Pan, S Zhu- ACS medicinal, 2021 - ACS Publications The discovery and clinical use of multitarget monotherapeutic antibiotics is regarded as a promising approach to reduce the development of antibiotic resistance. Platencin (PTN), a potent natural a... On the basis of the X-ray structures of PTN with ecFabF(C163Q), Burkholderia vietnamiensis FabF, and Brucella melitensis FabB (PDB IDs 3HO2, 4F32, and 4JV3, respectively) as well as that of platencin A1 with ecFabF-(C163Q) (PDB ID 3HO9), it is likely that these PTN derivatives may also interact with FabF or
10 6nb3 - https://pubs.acs.org/doi/abs/10.1021/acsmedchemlett.1c00263 Discovery of Small Molecule Entry Inhibitors Targeting the Fusion Peptide of SARS-CoV-2 Spike Protein 2021 X Hu, CZ Chen, M Xu, Z Hu, H Guo, Z Itkin- ACS Medicinal, 2021 - ACS Publications SARS-CoV-2 entry into host cells relies on the spike (S) protein binding to the human ACE2 receptor. In this study, we investigated the structural dynamics of the viral S protein at the fusion pept... Comparison of the FP binding pocket of the spike protein of SARS-CoV-2 (PDB 6XR8), SARS-CoV-1 (PDB 5WRG), and MERS (PDB 6NB3). The spike protein is rendered in ribbons with the FP colored in magenta and the HR1 domain in blue.