Announcing the worldwide Protein Data Bank

The Protein Data Bank

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The protein data bank: A computer-based archival file for macromolecular structures

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[30] Macromolecular crystallographic information file

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Biocooperative Regenerative Materials by Harnessing Blood‐Clotting and Peptide Self‐Assembly

Padilla‐Lopategui, S., Ligorio, C., Bu, W., Yin, C., Laurenza, D., Redondo, C., Owen, R., Sun, H., Rose, F. R. A. J., Iskratsch, T., et al. (2024) · Advanced Materials · doi:10.1002/adma.202407156 · Cited by 26

Bioinformatic approaches to augment study of epithelial-to-mesenchymal transition in lung cancer

Beck, T. N., Chikwem, A. J., Solanki-Patel, N., & Golemis, E. A. (2014) · Physiological Genomics · doi:10.1152/physiolgenomics.00062.2014 · Cited by 26

A less‐biased analysis of metalloproteins reveals novel zinc coordination geometries

Yao, S., Flight, R. M., Rouchka, E. C., & Moseley, H. (2015) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24834 · Cited by 26

Nanoinformatics: developing new computing applications for nanomedicine

Maojo, V., Fritts, M. J., Martin-Sanchez, F. J., de la Iglesia, D., Cachau, R. E., García-Remesal, M., Crespo, J., Mitchell, J. A., Anguita, A., Baker, N., et al. (2012) · Computing · doi:10.1007/s00607-012-0191-2 · Cited by 26

BDB: Databank of PDB files with consistent B-factors

Touw, W. G., & Vriend, G. (2014) · Protein Engineering Design and Selection · doi:10.1093/protein/gzu044 · Cited by 26

A unique structural domain in Methanococcoides burtonii ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) acts as a small subunit mimic

Gunn, L. H., Valegard, K., & Andersson, I. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.767145 · Cited by 25

Ligand fitting with CCP 4

Nicholls, R. A. (2017) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798316020143 · Cited by 26

Novel Semisynthetic Derivatives of Bile Acids as Effective Tyrosyl-DNA Phosphodiesterase 1 Inhibitors

Salomatina, O. V., Popadyuk, I. I., Zakharenko, A. L., Zakharova, O. D., Fadeev, D. S., Комарова, Н. И., Reynisson, J., Arabshahi, H. J., Raina, C., Volcho, K. P., et al. (2018) · Molecules · doi:10.3390/molecules23030679 · Cited by 26

ProtDCal‐Suite: A web server for the numerical codification and functional analysis of proteins

Romero‐Molina, S., Ruiz‐Blanco, Y. B., Green, J. R., & Sánchez‐García, E. (2019) · Protein Science · doi:10.1002/pro.3673 · Cited by 26

Unusual interplay of contrasting selective pressures on β-defensin genes implicated in male fertility of the Buffalo (Bubalus bubalis)

Batra, V., Maheshwarappa, A., Dagar, K., Kumar, S., Soni, A., Kumaresan, A., Kumar, R., & Datta, T. K. (2019) · BMC Evolutionary Biology · doi:10.1186/s12862-019-1535-8 · Cited by 26

The CC′ loop of IgV domains of the immune checkpoint receptors, plays a key role in receptor:ligand affinity modulation

Kundapura, S. V., & Ramagopal, U. A. (2019) · Scientific Reports · doi:10.1038/s41598-019-54623-y · Cited by 25

RGD-hirudin-based low molecular weight peptide prevents blood coagulation via subcutaneous injection

Li, Y., Huang, Y., Zhao, B., Wu, M., Li, T.-Y., Zhang, Y., Chen, D., Yu, M., & Mo, W. (2020) · Acta Pharmacologica Sinica · doi:10.1038/s41401-019-0347-0 · Cited by 26

Inhibiting HTLV-1 Protease: A Viable Antiviral Target

Lockbaum, G. J., Henes, M., Talledge, N., Rusere, L. N., Kosovrasti, K., Nalivaika, E. A., Somasundaran, M., Ali, A., Mansky, L. M., Yılmaz, N. K., et al. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.0c00975 · Cited by 26

Novel Tdp1 Inhibitors Based on Adamantane Connected with Monoterpene Moieties via Heterocyclic Fragments

Munkuev, A. A., Mozhaitsev, E. S., Chepanova, A. A., Суслов, Е. В., Викторовна, К. Д., Zakharova, O. D., Ilina, E. S., Dyrkheeva, N. S., Zakharenko, A. L., Reynisson, J., et al. (2021) · Molecules · doi:10.3390/molecules26113128 · Cited by 26

Structure of human cytomegalovirus virion reveals host tRNA binding to capsid-associated tegument protein pp150

Liu, Y.-T., Strugatsky, D., Liu, W., & Zhou, Z. H. (2021) · Nature Communications · doi:10.1038/s41467-021-25791-1 · Cited by 28

Proteome based mapping and reverse vaccinology techniques to contrive multi-epitope based subunit vaccine (MEBSV) against Streptococcus pyogenes.

Aslam, S., Ashfaq, U., Zia, T., Aslam, N., Alrumaihi, F. A., Shahid, F., Noor, F., & Qasim, M. (2022) · Infection, Genetics and Evolution · doi:10.1016/j.meegid.2022.105259 · Cited by 22

The impact of AlphaFold2 on experimental structure solution

Edich, M., Briggs, D. C., Kippes, O., Gao, Y., & Thorn, A. (2022) · Faraday Discussions · doi:10.1039/d2fd00072e · Cited by 29

Biallelic TLR4 deficiency in humans

Capitani, M., Al‐Shaibi, A., Pandey, S., Gartner, L., Taylor, H., Hubrack, S., Agrebi, N., Almohannadi, M., Kaabi, S. A., Vogl, T., et al. (2022) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2022.08.030 · Cited by 26

Multivalency of nucleosome recognition by LEDGF

Koutná, E., Lux, V., Kouba, T., Škerlová, J., Nováček, J., Srb, P., Hexnerova, R., Šváchová, H., Kukačka, Z., Novák, P., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad674 · Cited by 25

Chapter 12 Molecular Modeling and Simulation Studies of Ion Channel Structures, Dynamics and Mechanisms

Tai, K., Fowler, P. W., Mokrab, Y., Stansfeld, P. J., & Sansom, M. S. P. (2008) · Methods in cell biology · doi:10.1016/s0091-679x(08)00812-1 · Cited by 26

Distinct Conformation of ATP Molecule in Solution and on Protein

Kobayashi, E., Yura, K., & Nagai, Y. (2013) · BIOPHYSICS · doi:10.2142/biophysics.9.1 · Cited by 26

Static and dynamic interactions between GALK enzyme and known inhibitors: Guidelines to design new drugs for galactosemic patients

Chiappori, F., Ivan Merelli, A., Milanesi, L., & Marabotti, A. (2013) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2013.02.021 · Cited by 26

Distributed structure determination at the JCSG

Bedem, H. V. D., Wolf, G., Xu, Q., & Deacon, A. M. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910039934 · Cited by 26

Proteins analysed as virtual knots

Alexander, K., Taylor, A. J., & Dennis, M. R. (2017) · Scientific Reports · doi:10.1038/srep42300 · Cited by 26

CaMELS:In silicoprediction of calmodulin binding proteins and their binding sites

Abbasi, W. A., Asif, A., Andleeb, S., & Minhas, F. (2017) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25330 · Cited by 28

Synthesis, Biological Evaluation and Docking Studies of Benzoxazoles Derived from Thymoquinone

Glamočlija, U., Padhyé, S., Špirtović‐Halilović, S., Osmanović, A., Veljović, E., Roca, S., Novaković, I., Mandić, B., Turel, I., Kljun, J., et al. (2018) · Molecules · doi:10.3390/molecules23123297 · Cited by 26

Alzheimer’s Disease: the Potential of Epigenetic Treatments and Current Clinical Candidates

Coneys, R., & Wood, I. C. (2020) · Neurodegenerative Disease Management · doi:10.2217/nmt-2019-0034 · Cited by 26

Using the Tools and Resources of the RCSB Protein Data Bank

Dutta, S., Berman, H. M., & Bluhm, W. F. (2007) · Current Protocols in Bioinformatics · doi:10.1002/0471250953.bi0109s20 · Cited by 26

Influence of the Nucleophile on the Candida antarctica Lipase B‐Catalysed Resolution of a Chiral Acyl Donor

García‐Urdiales, E., Ríos‐Lombardía, N., Mangas‐Sánchez, J., Gotor‐Fernández, V., & Gotor, V. (2009) · ChemBioChem · doi:10.1002/cbic.200900204 · Cited by 26

Conserved Water Mediated H-bonding Dynamics of Inhibitor, Cofactor, Asp 364 and Asn 303 in Human IMPDH II

Bairagya, H. R., Mukhopadhyay, B. P., & Sekar, K. (2009) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2009.10507265 · Cited by 26

ModelCIF: An Extension of PDBx/mmCIF Data Representation for Computed Structure Models

Vallat, B., Tauriello, G., Bienert, S., Haas, J., Webb, B. M., Žídek, A., Zheng, W., Peisach, E., Piehl, D. W., Anischanka, I., et al. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168021 · Cited by 26

A Review of Cross-Disciplinary Approaches for the Identification of Novel Industrially Relevant Plastic-Degrading Enzymes

Herbert, J., Beckett, A. H., & Robson, S. C. (2022) · Sustainability · doi:10.3390/su142315898 · Cited by 27

Identification of potential DNA gyrase inhibitors: virtual screening, extra-precision docking and molecular dynamics simulation study

Kumar, A., Prasun, C., Rathi, E., Nair, M. S., & Kini, S. G. (2023) · Chemical Papers · doi:10.1007/s11696-023-02971-5 · Cited by 25

Current Status of the Application of Antimicrobial Peptides and Their Conjugated Derivatives

del Olmo, M., & Andreu, C. (2025) · Molecules · doi:10.3390/molecules30153070 · Cited by 27

Structure-guided expansion of kinase fragment libraries driven by support vector machine models

Erickson, J. A., Mader, M. M., Watson, I. A., Webster, Y., Higgs, R. E., Bell, M. A., & Vieth, M. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.12.002 · Cited by 25

Visualization methods for molecular studies on the web platform

Callieri, M., Andrei, R. M., Benedetto, M. D., Zoppè, M., & Scopigno, R. (2010) · international conference on 3D web technology · doi:10.1145/1836049.1836067 · Cited by 25

Three-Dimensional Structures of Galectins

Kamitori, S. (2018) · Trends in Glycoscience and Glycotechnology · doi:10.4052/tigg.1731.1se · Cited by 25

High resolution crystal structure of substrate-free human neprilysin

Moss, S., Subramanian, V., & Acharya, K. R. (2018) · Journal of Structural Biology · doi:10.1016/j.jsb.2018.06.004 · Cited by 25

Modelling lipid systems in fluid with Lattice Boltzmann Molecular Dynamics simulations and hydrodynamics

Brandner, A. F., Timr, Š., Melchionna, S., Derreumaux, P., Baaden, M., & Sterpone, F. (2019) · Scientific Reports · doi:10.1038/s41598-019-52760-y · Cited by 29

Identifying intermolecular atom⋯atom interactions that are not just bonding but also competitive

Taylor, R. (2020) · CrystEngComm · doi:10.1039/d0ce00270d · Cited by 25

Knowledge‐based structural models of SARS‐CoV‐2 proteins and their complexes with potential drugs

Hijikata, A., Shionyu‐Mitsuyama, C., Nakae, S., Shionyu, M., Ota, M., Kanaya, S., & Shirai, T. (2020) · FEBS Letters · doi:10.1002/1873-3468.13806 · Cited by 25

"In Vitro: Natural Compounds (Thymol, Carvacrol, Hesperidine, and Thymoquinone) against Sars-Cov2 Strain Isolated from Egypt"

SEADAWY, A. R., Gad, A. F., Elhoseny, M. F., ELharty, B. E., Shamel, M. D., Elfiky, A. A., Ahmed, A., & Zekri, A. R. N. (2021) · Biomedical Journal of Scientific & Technical Research · doi:10.26717/bjstr.2021.34.005552 · Cited by 25

Pink-beam serial femtosecond crystallography for accurate structure-factor determination at an X-ray free-electron laser

Nass, K., Bacellar, C., Cirelli, C., Dworkowski, F., Gevorkov, Y., James, D., Johnson, P. J. M., Kekilli, D., Knopp, G., Martiel, I., et al. (2021) · IUCrJ · doi:10.1107/s2052252521008046 · Cited by 25

Protein binding sites for drug design

Konc, J., & Janežič, D. (2022) · Biophysical Reviews · doi:10.1007/s12551-022-01028-3 · Cited by 25

Cyclocondensation of 3,4-diaminobenzophenone with glyoxal: Synthesis, X-ray structure, density functional theory calculation and molecular docking studies

Kaya, Y., Kaya, S., Бериша, А., & Erçağ, A. (2023) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2023.135973 · Cited by 25

Structure-based prediction of protein-nucleic acid binding using graph neural networks

Sagendorf, J. M., Mitra, R., Huang, J., Chen, X. S., & Rohs, R. (2024) · Biophysical Reviews · doi:10.1007/s12551-024-01201-w · Cited by 26

Albumin-directed stereoselective reduction of 1,3-diketones and β-hydroxyketones to anti diols

Berti, F., Bincoletto, S., Donati, I., Fontanive, G., Fregonese, M., & Benedetti, F. M. (2010) · Organic & Biomolecular Chemistry · doi:10.1039/c0ob00648c · Cited by 25

The histone-fold complex MHF is remodeled by FANCM to recognize branched DNA and protect genome stability

Fox, D., Yan, Z., Ling, C., Zhao, Y., Lee, D., Fukagawa, T., Yang, W., & Wang, W. (2014) · Cell Research · doi:10.1038/cr.2014.42 · Cited by 25

RESOPS: A Database for Analyzing the Correspondence of RNA Editing Sites to Protein Three-Dimensional Structures

Yura, K., Sulaiman, S., Hatta, Y., Shionyu, M., & Gō, M. (2009) · Plant and Cell Physiology · doi:10.1093/pcp/pcp132 · Cited by 25

Improvements in GROMACS plugin for PyMOL including implicit solvent simulations and displaying results of PCA analysis

Makarewicz, T., & Kaźmierkiewicz, R. (2016) · Journal of Molecular Modeling · doi:10.1007/s00894-016-2982-4 · Cited by 25

High-throughput quantum-mechanics/molecular-mechanics (ONIOM) macromolecular crystallographic refinement withPHENIX/DivCon: the impact of mixed Hamiltonian methods on ligand and protein structure

Borbulevych, O. Y., Martin, R. I., & Westerhoff, L. M. (2018) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798318012913 · Cited by 25

Identification, Functional Characterization, and Regulon Prediction of the Zinc Uptake Regulator (zur) of Bacillus anthracis – An Insight Into the Zinc Homeostasis of the Pathogen

Kandari, D., Gopalani, M., Gupta, M. K., Joshi, H., Bhatnagar, S., & Bhatnagar, R. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.03314 · Cited by 25

Archiving and disseminating integrative structure models

Vallat, B. K., Webb, B., Westbrook, J., Šali, A., & Berman, H. M. (2019) · Journal of Biomolecular NMR · doi:10.1007/s10858-019-00264-2 · Cited by 25

Similarity search for local protein structures at atomic resolution by exploiting a database management system

Kinjo, A. R., & Nakamura, H. (2007) · BIOPHYSICS · doi:10.2142/biophysics.3.75 · Cited by 25

Stereoselective Chemoenzymatic Preparation of β‐Amino Esters: Molecular Modelling Considerations in Lipase‐Mediated Processes and Application to the Synthesis of (S)‐Dapoxetine

Rodríguez‐Mata, M., García‐Urdiales, E., Gotor‐Fernández, V., & Gotor, V. (2010) · Advanced Synthesis & Catalysis · doi:10.1002/adsc.200900676 · Cited by 25

Anti-influenza activity of diazaadamantanes combined with monoterpene moieties

Суслов, Е. В., Zarubaev, V. V., Slita, A. V., Ponomarev, K. Y., Викторовна, К. Д., Ayine‐Tora, D. M., Reynisson, J., Volcho, K. P., & Salakhutdinov, N. F. (2017) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2017.08.062 · Cited by 25

D ‐Trehalose/ D ‐maltose‐binding protein from the hyperthermophilic archaeon Thermococcus litoralis: The binding of trehalose and maltose results in different protein conformational states

Heřman, P., Staiano, M., Marabotti, A., Varriale, A., Scirè, A., Tanfani, F., Večeř, J., Rossi, M., & D’Auria, S. (2006) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20952 · Cited by 25

Applications of Bio-molecular Databases in Bioinformatics

Kumari, A., Kanchan, S., Sinha, R. P., & Kesheri, M. (2016) · Studies in computational intelligence · doi:10.1007/978-3-319-33793-7_15 · Cited by 24

Challenge for Deep Learning: Protein Structure Prediction of Ligand-Induced Conformational Changes at Allosteric and Orthosteric Sites

Olanders, G., Testa, G., Tibo, A., Nittinger, E., & Tyrchan, C. (2024) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.4c01475 · Cited by 27

Myosin cleft closure determines the energetics of the actomyosin interaction

Takács, B., O'Neall-Hennessey, E., Hetényi, C., Kardos, J., Szent‐Györgyi, A. G., & Kovács, M. (2010) · The FASEB Journal · doi:10.1096/fj.10-164871 · Cited by 24

Structure-Guided Protein Transition Modeling with a Probabilistic Roadmap Algorithm

Maximova, T., Plaku, E., & Shehu, A. (2016) · IEEE Transactions on Computational Biology and Bioinformatics · doi:10.1109/tcbb.2016.2586044 · Cited by 25

A Survey of Computational Treatments of Biomolecules by Robotics-Inspired Methods Modeling Equilibrium Structure and Dynamic

Shehu, A., & Plaku, E. (2016) · Journal of Artificial Intelligence Research · doi:10.1613/jair.5040 · Cited by 25

Design, synthesis and biological evaluation of 2,3-dihydro-[1,4]dioxino[2,3-f]quinazoline derivatives as EGFR inhibitors

Qin, X., Yang, L., Liu, P., Yang, L., Chen, L., Hu, L., & Jiang, M. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.104743 · Cited by 24

Adaptive Cartesian and torsional restraints for interactive model rebuilding

Croll, T. I., & Read, R. J. (2021) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798321001145 · Cited by 23

The Moringin/α-CD Pretreatment Induces Neuroprotection in an In Vitro Model of Alzheimer’s Disease: A Transcriptomic Study

Silvestro, S., Chiricosta, L., Gugliandolo, A., Iori, R., Rollin, P., Perenzoni, D., Mattivi, F., Bramanti, P., & Mazzon, E. (2021) · Current Issues in Molecular Biology · doi:10.3390/cimb43010017 · Cited by 28

Accommodation of ring C expanded deoxyvasicinone in the HDAC inhibitory pharmacophore culminates into a tractable anti-lung cancer agent and pH-responsive nanocarrier

Sharma, R., Chatterjee, E., Mathew, J., Sharma, S., Rao, N. V., Pan, C., Lee, S., Dhingra, A. K., Grewal, A. S., Liou, J., et al. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114602 · Cited by 24

Novel NO2 semicarbazone ligand and its metal complexes as VEGFR‐2 inhibitors: Synthesis, spectral characterization, density functional theory calculations, molecular docking, and antimicrobial and antitumor evaluation

Salah, N., Emara, A. A. A., Adly, O. M. I., Taha, A., Nabeel, A. I., Abdelaziz, M., & Ibrahim, M. A. (2022) · Applied Organometallic Chemistry · doi:10.1002/aoc.6845 · Cited by 24

Multiple and Variable Binding of Pharmacologically Active Bis(maltolato)oxidovanadium(IV) to Lysozyme

Ferraro, G., Paolillo, M., Sciortino, G., Garribba, E., & Merlino, A. (2022) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.2c02690 · Cited by 24

The Effect of Treatment-Associated Mutations on HIV Replication and Transmission Cycles

Johnson, M. M., Jones, C. E., & Clark, D. N. (2022) · Viruses · doi:10.3390/v15010107 · Cited by 29

Molecular interactions, binding stability, and synergistic inhibition on Acetylcholinesterase activity of Safranin O in combination with Quercetin and Gallic acid: In vitro and in silico study

Kadi, I., Eltayb, W. A., Boufissiou, A., Benaceur, F., Bouchareb, A., Soltan, W. B., Baladehi, M. H., Kheniche, A., & Abdalla, M. (2023) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2023.135562 · Cited by 24

Synthesis, X-ray crystallography, antimicrobial, molecular docking, and DFT study of bis-triazoles linked ampyrone

Lal, B., Tittal, R. K., Mathpati, R. S., Ghule Vikas, D., Nehra, N., & Lal, K. (2023) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2023.136455 · Cited by 25

A population-based evolutionary search approach to the multiple minima problem in de novo protein structure prediction

Saleh, S. N., Olson, B., & Shehu, A. (2013) · BMC Structural Biology · doi:10.1186/1472-6807-13-s1-s4 · Cited by 24

Validation of Arsenic Resistance in Bacillus cereus Strain AG27 by Comparative Protein Modeling of arsC Gene Product

Jain, S., Saluja, B., Gupta, A., Marla, S. S., & Goel, R. (2011) · The Protein Journal · doi:10.1007/s10930-011-9305-5 · Cited by 24

Symmetry versus Asymmetry in the Molecules of Life: Homomeric Protein Assemblies

Kojić‐Prodić, B., & Štefanić, Z. (2010) · Symmetry · doi:10.3390/sym2020884 · Cited by 23

Understanding the role of base stacking in nucleic acids. MD and QM analysis of tandem GA base pairs in RNA duplexes

Morgado, C. A., Svozil, D., Turner, D. H., & Šponer, J. (2012) · Physical Chemistry Chemical Physics · doi:10.1039/c2cp40556c · Cited by 24

Investigation of vital pathogenic target orotate phosphoribosyltransferases (OPRTase) from Thermus thermophilus HB8: Phylogenetic and molecular modeling approach

Kanagarajan, S., Prabhu, D., Mariadasse, R., Nachiappan, M., Biswal, J., & Jeyakanthan, J. (2016) · Gene · doi:10.1016/j.gene.2016.02.006 · Cited by 24

Conformations of the HIV-1 protease: A crystal structure data set analysis

Palese, L. L. (2017) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2017.08.009 · Cited by 24

Biophysical characterization and structure of the Fab fragment from the NIST reference antibody, RM 8671

Karageorgos, I. L., Gallagher, E. S., Galvin, C. V., Gallagher, D. T., & Hudgens, J. W. (2017) · Biologicals · doi:10.1016/j.biologicals.2017.09.005 · Cited by 24

Conformational Aspects in the Design of Inhibitors for Serine Hydroxymethyltransferase (SHMT): Biphenyl, Aryl Sulfonamide, and Aryl Sulfone Motifs.

Schwertz, G., Frei, M. S., Witschel, M., Rottmann, M., Leartsakulpanich, U., Chitnumsub, P., Jaruwat, A., Ittarat, W., Schäfer, A., Aponte, R. A., et al. (2017) · Chemistry · doi:10.1002/chem.201703244 · Cited by 24

Evaluation of Cyclosaplin Efficacy Using a Silk Based 3D Tumor Model

Mishra, A., Mukhopadhyay, S. K., & Dey, S. (2019) · Biomolecules · doi:10.3390/biom9040123 · Cited by 24

Water Loss in Aging Erythrocytes Provides a Clue to a General Mechanism of Cellular Senescence

Minton, A. P. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2020.10.004 · Cited by 23

Feasibility of one-shot-per-crystal structure determination using Laue diffraction

Cornaby, S. W., Szebenyi, D. M. E., Smilgies, D., Schuller, D. J., Gillilan, R. E., Hao, Q., & Bilderback, D. H. (2009) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909037731 · Cited by 24

Discovery of aminoquinolines as a new class of potent inhibitors of heat shock protein 90 (Hsp90): Synthesis, biology, and molecular modeling

Ganesh, T., Min, J., Thepchatri, P., Du, Y., Li, L., Lewis, I., Wilson, L. J., Fu, H., Chiosis, G., Dingledine, R. J., et al. (2008) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2008.05.047 · Cited by 24

The Research Collaboratory for Structural Bioinformatics Protein Data Bank

Bourne, P. E., Bluhm, W. F., Deshpande, N., Zhang, Q., Berman, H. M., & Flippen-Anderson, J. L. (2007) · Elsevier eBooks · doi:10.1016/b0-08-045044-x/00090-0 · Cited by 24

Structural basis for the unique molecular properties of broad-range phospholipase C from Listeria monocytogenes

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