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 7k43 7k4n https://pubs.acs.org/doi/abs/10.1021/acs.jpcb.1c00395 Integrated Biophysical Modeling of the SARS-CoV-2 Spike Protein Binding and Allosteric Interactions with Antibodies 2021 GM Verkhivker, L Di Paola- The Journal of Physical Chemistry B, 2021 - ACS Publications Structural and biochemical studies of the severe acute respiratory syndrome (SARS)-CoV-2 spike glycoproteins and complexes with highly potent antibodies have revealed multiple conformation-dependen...
2 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
3 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
4 3pk0 5if3 https://pubs.acs.org/doi/abs/10.1021/acscatal.9b00621 Two enantiocomplementary Ephedrine Dehydrogenases from Arthrobacter sp. TS-15 with broad substrate specificity 2019 T Shanati, C Lockie, L Beloti, G Grogan- ACS, 2019 - ACS Publications provide a detailed insight into both the functional and structural characteristics of PseDH and EDH.. A comparison with 30 structures of SDRs from bacterial species in the PDB suggests that S143 is most commonly a small hydrophobic residue, such as G, A, or V, whereas W152 is most commonly an H, M, or L, although in SDRs from Burkholderia vietnamiensis (5IF3) and Mycobacterium smegmatis (3PK0) the residue is W
5 4lgv - https://pubs.acs.org/doi/abs/10.1021/acscatal.9b02413 Artificial Multienzyme Scaffolds: Pursuing in Vitro Substrate Channeling with an Overview of Current Progress 2019 GA Ellis, WP Klein, G Lasarte-Aragones, M Thakur- ACS, 2019 - ACS Publications Within each material class of scaffolds, attention is given to their inherent chemical diversity, how they are engineered, how they allow for enzymatic attachment, their ease of use, their benefits (eg, inherent three-dimensional architecture ) ... Illustration of the proposed channeling complex using a poly(lysine) bridge as an electrostatic surface between hexokinase (HK) (PDB entry 3VF6) and glucose-6-phosphate dehydrogenase (G6PDH) (PDB entry 4LGV).
6 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
7 7jv2 7jx3 https://pubs.acs.org/doi/abs/10.1021/acscentsci.1c00216 Molecular Aspects Concerning the Use of the SARS-CoV-2 Receptor Binding Domain as a Target for Preventive Vaccines 2021 Y Valdes-Balbin, D Santana-Mederos- ACS Central, 2021 - ACS Publications The development of recombinant COVID-19 vaccines has resulted from scientific progress made at an unprecedented speed during 2020. The recombinant spike glycoprotein monomer, its trimer, and its re... Structural analyses were performed from PDB: 6M0J for the complex ACE2–RBD, (9) PDB: 7BZ5 for B38, (85) PDB: 7BYR for BD23, (86) PDB: 6XEY for Fab2-4, (87) PDB: 7BWJ for P2B-2F6, (88) PDB: 7JV2 for S2H13
8 4mow - https://pubs.acs.org/doi/abs/10.1021/acscentsci.1c00519 Discovery of SARS-CoV-2 Papain-like Protease Inhibitors through a Combination of High-Throughput Screening and a FlipGFP-Based Reporter Assay 2021 C Ma, MD Sacco, Z Xia, G Lambrinidis- ACS Central, 2021 - ACS Publications Using the structure with PDB ID 7JRN as a template, we docked the potent analogues Jun9-53-2, Jun9-72-2, and Jun9-75-4 in the SARS-CoV-2 PL pro drug-binding site. The stability of
9 4iwh - https://pubs.acs.org/doi/abs/10.1021/acscentsci.8b00912 Predicting Protein Complex Structure from Surface-Induced Dissociation Mass Spectrometry Data 2019 JT Seffernick, SR Harvey, VH Wysocki- ACS Central, 2019 - ACS Publications from which data have been favorably compared to known crystal structures on many along with other bioanalytical MS and dissociation techniques, yields useful structural information, the sparse, not allowing for an unambiguous determination of the protein complex structure... Additionally, the Pnear also improved for 56/57 ideal cases (except 4IWH) when SID data were used, as shown in Figure S3A.
10 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