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

Structure	Year released	#citations
6WWD	2020	0
6WQM	2020	0
6WOM	2020	0
6WHJ	2020	0
6WFM	2020	0
6WBD	2020	0
9YN9	2025	0
6W80	2020	0
6W6A	2020	0
9YRU	2025	0

Manually reviewed citations

#	PDB	Additional SSGCID structures cited	Link	Title	Year	Citation	Highlighted abstract
1	2mu0	2kok	https://pubs.acs.org/doi/abs/10.1021/acs.biochem.0c00651	Isofunctional Clustering and Conformational Analysis of the Arsenate Reductase Superfamily Reveals Nine Distinct Clusters	2020	MR Rosen, JB Leuthaeuser, CA Parish, JS Fetrow- Biochemistry, 2020 - ACS Publications	Arsenate reductase (ArsC) is a superfamily of enzymes that reduce arsenate. Due to active site similarities, some ArsC can function as low-molecular weight protein tyrosine phosphatases (LMW-PTPs).... We performed MD simulations to better understand the conformational behavior of each of the nine classes of proteins identified by autoMISST. Starting structures for these simulations were obtained from the following data available in the RCSB PDB:34 group 3AAA, 2KOK (chain A); group 4AA, 2MU0 (chain A); gro
2	7kqa	-	https://pubs.acs.org/doi/abs/10.1021/acs.biochem.5c00284	SH N Contacts between Side Chains of Cys and Backbone Nitrogen Atoms in Proteins Are Weak Interactions and Not Hydrogen Bonds	2025	P Singh, R Sankararamakrishnan- Biochemistry, 2025 - ACS Publications	We retained the same internal parameters found in PDB structures for all non-self-contacting Cys involved in potential SHN hydrogen bonds. When B3LYP was used, only 13 to 23
3	4o5o	-	https://pubs.acs.org/doi/abs/10.1021/acs.biochem.7b01186	Engineering Erg10 Thiolase from Saccharomyces cerevisiae as a Synthetic Toolkit for the Production of Branched-Chain Alcohols	2018	P Torres-Salas, V Bernal, F Lopez-Gallego- Biochemistry, 2018 - ACS Publications	Using a combined computational/experimental approach, and guided by structural information, we have studied the potential of thiolases to with novel properties, the naturally occurring metabolism of microorganisms is not always sufficient to obtain any desired structure
4	3rih	3pk0	https://pubs.acs.org/doi/abs/10.1021/acs.biochem.8b00464	Structure and Kinetics of the S-(+)-1-Amino-2-propanol Dehydrogenase from the RMM Microcompartment of Mycobacterium smegmatis	2018	E Mallette, MS Kimber- Biochemistry, 2018 - ACS Publications	We determined the structure of APDH in both apo form (at 1.7 ) and as a ternary enzyme complex with NADP + and aminoacetone... This work has shown that 3PK0 (APDHMSM0779) is an orthologue, and analysis (see below) suggests that 3RIH is also likely a Mycobacterial APDH orthologue
5	3k5p	-	https://pubs.acs.org/doi/abs/10.1021/acs.biochem.8b00990	3-Phosphoglycerate Transhydrogenation Instead of Dehydrogenation Alleviates the Redox State Dependency of Yeast de Novo l-Serine Synthesis	2019	N Paczia, J Becker-Kettern, JF Conrotte- Biochemistry, 2019 - ACS Publications	Structural Biology Unit, CIC bioGUNE Technological Park of Bizkaia, 48160 Derio , Vizcaya , Spain. IKERBASQUE, Basque Foundation for Here, we provide a detailed biochemical and sequence structure relationship characterization of the yeast PHGDH homologues
6	4hvt	-	https://pubs.acs.org/doi/abs/10.1021/acs.biochem.9b00031	Crystal Structure and Conformational Dynamics of Pyrococcus furiosus Prolyl Oligopeptidase	2019	K Ellis-Guardiola, H Rui, RL Beckner, P Srivastava- Biochemistry, 2019 - ACS Publications	Crystal Structure and Conformational Dynamics of Pyrococcus furiosus Prolyl Oligopeptidase While extensive structural characterization of bacterial and mammalian POPs has been performed, no structures for archaeal POPs have been reported
7	5udf	-	https://pubs.acs.org/doi/abs/10.1021/acs.chemrev.1c00055	Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria	2021	I Alav, J Kobylka, MS Kuth, KM Pos, M Picard- Chemical, 2021 - ACS Publications	Journal Logo. Structure , Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria. Ilyas Alav Ilyas Alav. Institute of Microbiology and Infection, College of Medical and Dental Sciences
8	4ixo	-	https://pubs.acs.org/doi/abs/10.1021/acs.chemrev.2c00106	Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere	2022	C Van Stappen, Y Deng, Y Liu, H Heidari- Chemical, 2022 - ACS Publications	structure of the active site of cytochrome c peroxidase ( PDB structure of the active site of the F43H/H64L Mb mutant ( PDB bound Ni 2+ ( PDB ID: 4IXO ) and (f) Co 2+ ( PDB ID: 4IWW).
9	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...
10	3iew	3k2x	https://pubs.acs.org/doi/abs/10.1021/acs.jcim.0c00877	Benchmark Sets for Binding Hot Spot Identification in Fragment-Based Ligand Discovery	2020	AE Wakefield, C Yueh, D Beglov- Journal of Chemical, 2020 - ACS Publications	Binding hot spots are regions of proteins that, due to their potentially high contribution to the binding free energy, have high propensity to bind small molecules. We present benchmark sets for te...