A short history of SHELX

Coot : model-building tools for molecular graphics

Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571

Crystal structure refinement with SHELXL

Sheldrick, G. M. (2015) · Acta Crystallographica Section C Structural Chemistry · doi:10.1107/s2053229614024218 · Cited by 43,982

OLEX2 : a complete structure solution, refinement and analysis program

Dolomanov, O. V., Bourhis, L. J., Gildea, R. J., Howard, J. A. K., & Puschmann, H. (2009) · Journal of Applied Crystallography · doi:10.1107/s0021889808042726 · Cited by 32,811

SHELXT – Integrated space-group and crystal-structure determination

Sheldrick, G. M. (2015) · Acta Crystallographica Section A Foundations and Advances · doi:10.1107/s2053273314026370 · Cited by 29,831

PHENIX : a comprehensive Python-based system for macromolecular structure solution

Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716

Overview of the CCP 4 suite and current developments

Winn, M. D., Ballard, C. C., Cowtan, K. D., Dodson, E. J., Emsley, P., Evans, P. R., Keegan, R. M., Krissinel, E. B., Leslie, A. G. W., McCoy, A., et al. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910045749 · Cited by 12,353

Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix

Liebschner, D., Afonine, P. V., Baker, M. L., Bunkóczi, G., Chen, V. B., Croll, T. I., Hintze, B., Hung, L.-W., Jain, S., McCoy, A. J., et al. (2019) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798319011471 · Cited by 7,953

Towards automated crystallographic structure refinement with phenix.refine

Afonine, P. V., Grosse-Kunstleve, R. W., Echols, N., Headd, J. J., Moriarty, N. W., Mustyakimov, M., Terwilliger, T. C., Urzhumtsev, A., Zwart, P. H., & Adams, P. D. (2012) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444912001308 · Cited by 5,511

MolProbity: More and better reference data for improved all‐atom structure validation

Williams, C. J., Headd, J. J., Moriarty, N. W., Prisant, M. G., Videau, L. L., Deis, L. N., Verma, V., Keedy, D. A., Hintze, B. J., Chen, V. B., et al. (2018) · Protein Science · doi:10.1002/pro.3330 · Cited by 4,599

Comparison of silver and molybdenum microfocus X-ray sources for single-crystal structure determination

Krause, L., Herbst-Irmer, R., Sheldrick, G. M., & Stalke, D. (2015) · Journal of Applied Crystallography · doi:10.1107/s1600576714022985 · Cited by 4,983

Crystal structure of Cas9 in complex with guide RNA and target DNA

Nishimasu, H., Ran, F. A., Hsu, P. D., Konermann, S., Shehata, S. I., Dohmae, N., Ishitani, R., Zhang, F., & Nureki, O. (2014) · Cell · doi:10.1016/j.cell.2014.02.001 · Cited by 2,306

Cell-free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers within Hydrogels

Kato, M., Han, T. W., Xie, S., Shi, K., Du, X., Wu, L. C., Mirzaei, H., Goldsmith, E. J., Longgood, J., Pei, J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.017 · Cited by 2,012

Dirac cone protected by non-symmorphic symmetry and three-dimensional Dirac line node in ZrSiS

Schoop, L. M., Ali, M. N., Straßer, C., Topp, A., Varykhalov, A., Marchenko, D., Duppel, V., Parkin, S. S. P., Lotsch, B. V., & Ast, C. R. (2016) · Nature Communications · doi:10.1038/ncomms11696 · Cited by 782

Chitin-Induced Dimerization Activates a Plant Immune Receptor

Liu, T., Liu, Z., Song, C., Hu, Y., Han, Z., She, J., Fan, F., Wang, J., Jin, C., Chang, J., et al. (2012) · Science · doi:10.1126/science.1218867 · Cited by 680

New Stories of Zeolite Structures: Their Descriptions, Determinations, Predictions, and Evaluations

Li, Y., & Yu, J. (2014) · Chemical Reviews · doi:10.1021/cr500010r · Cited by 603

Structure and control of the actin regulatory WAVE complex

Chen, Z., Borek, D., Padrick, S. B., Gomez, T. S., Metlagel, Z., Ismail, A. M., Umetani, J., Billadeau, D. D., Otwinowski, Z., & Rosen, M. K. (2010) · Nature · doi:10.1038/nature09623 · Cited by 500

Structural Basis of UV DNA-Damage Recognition by the DDB1–DDB2 Complex

Scrima, A., Koníčková, R., Czyzewski, B. K., Kawasaki, Y., Jeffrey, P. D., Groisman, R., Nakatani, Y., Iwai, S., Pavletich, N. P., & Thomä, N. H. (2008) · Cell · doi:10.1016/j.cell.2008.10.045 · Cited by 441

Barely porous organic cages for hydrogen isotope separation

Liu, M., Zhang, L., Little, M. A., Kapil, V., Ceriotti, M., Yang, S., Ding, L., Holden, D. L., Balderas-Xicohténcatl, R., He, D., et al. (2019) · Science · doi:10.1126/science.aax7427 · Cited by 399

Architecture of human mTOR complex 1

Aylett, C. H. S., Sauer, E., Imseng, S., Boehringer, D., Hall, M. N., Ban, N., & Maier, T. (2016) · Science · doi:10.1126/science.aaa3870 · Cited by 344

MFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusion

Cao, Y.-L., Meng, S., Chen, Y., Feng, J.-X., Gu, D.-D., Yu, B., Li, Y.-J., Yang, J.-Y., Liao, S., Chan, D. C., et al. (2017) · Nature · doi:10.1038/nature21077 · Cited by 326

Functional Mesoporous Metal−Organic Frameworks for the Capture of Heavy Metal Ions and Size-Selective Catalysis

Fang, Q.-R., Yuan, D.-Q., Sculley, J., Li, J.-R., Han, Z.-B., & Zhou, H.-C. (2010) · Inorganic Chemistry · doi:10.1021/ic101935f · Cited by 309

Structural basis for a [4Fe–3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase

Shomura, Y., Yoon, K.-S., Nishihara, H., & Higuchi, Y. (2011) · Nature · doi:10.1038/nature10504 · Cited by 290

Structural Biology of Human H3K9 Methyltransferases

Wu, H., Min, J., Lunin, V. V., Antoshenko, T., Dombrovski, L., Zeng, H., Allali-Hassani, A., Campagna-Slater, V., Vedadi, M., Arrowsmith, C. H., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008570 · Cited by 268

A Basis Set of de Novo Coiled-Coil Peptide Oligomers for Rational Protein Design and Synthetic Biology

Fletcher, J. M., Boyle, A. L., Bruning, M., Bartlett, G. J., Vincent, T. L., Zaccai, N. R., Armstrong, C. T., Bromley, E. H. C., Booth, P. J., Brady, R. L., et al. (2012) · ACS Synthetic Biology · doi:10.1021/sb300028q · Cited by 262

A High-Yielding, Strictly Regioselective Prebiotic Purine Nucleoside Formation Pathway

Becker, S., Thoma, I., Deutsch, A., Gehrke, T., Mayer, P., Zipse, H., & Carell, T. (2016) · Science · doi:10.1126/science.aad2808 · Cited by 238

Structure of the Cpf1 endonuclease R-loop complex after target DNA cleavage

Stella, S., Alcón, P., & Montoya, G. (2017) · Nature · doi:10.1038/nature22398 · Cited by 244

Exploring Electronic versus Steric Effects in Stereoselective Ring-Opening Polymerization of Lactide and β-Butyrolactone with Amino-alkoxy-bis(phenolate)–Yttrium Complexes

Bouyahyi, M., Ajellal, N., Kirillov, E., Thomas, C. M., & Carpentier, J. (2011) · Chemistry – A European Journal · doi:10.1002/chem.201002779 · Cited by 217

The prospects of quantum computing in computational molecular biology

Outeiral, C., Strahm, M., Shi, J., Morris, G. M., Benjamin, S. C., & Deane, C. M. (2021) · WIREs Computational Molecular Science · doi:10.1002/wcms.1481 · Cited by 232

Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide

Sharma, A. K., Pavlova, S. T., Kim, J., Finkelstein, D., Hawco, N. J., Rath, N. P., Kim, J., & Mirica, L. M. (2012) · Journal of the American Chemical Society · doi:10.1021/ja210588m · Cited by 202

The methanogenic CO 2 reducing-and-fixing enzyme is bifunctional and contains 46 [4Fe-4S] clusters

Wagner, T., Ermler, U., & Shima, S. (2016) · Science · doi:10.1126/science.aaf9284 · Cited by 184

Structural Basis for a Safety-Belt Mechanism That Anchors Condensin to Chromosomes

Kschonsak, M., Merkel, F., Bisht, S., Metz, J., Rybin, V., Hassler, M., & Haering, C. H. (2017) · Cell · doi:10.1016/j.cell.2017.09.008 · Cited by 152

Molecular basis for SH3 domain regulation of F-BAR–mediated membrane deformation

Rao, Y., Ma, Q., Vahedi-Faridi, A., Sundborger, A., Pechstein, A., Puchkov, D., Luo, L., Shupliakov, O., Saenger, W., & Haucke, V. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003478107 · Cited by 149

The Mu transpososome structure sheds light on DDE recombinase evolution

Montaño, S. P., Pigli, Y. Z., & Rice, P. A. (2012) · Nature · doi:10.1038/nature11602 · Cited by 137

Functional and structural characterization of the integrase from the prototype foamy virus

Valkov, E., Gupta, S. S., Hare, S., Helander, A., Roversi, P., McClure, M., & Cherepanov, P. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkn938 · Cited by 130

Novel Multitarget-Directed Ligands (MTDLs) with Acetylcholinesterase (AChE) Inhibitory and Serotonergic Subtype 4 Receptor (5-HT4R) Agonist Activities As Potential Agents against Alzheimer’s Disease: The Design of Donecopride

Rochais, C., Lecoutey, C., Gaven, F., Giannoni, P., Hamidouche, K., Hedou, D., Dubost, E., Genest, D., Yahiaoui, S., Freret, T., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00115 · Cited by 129

Structural basis for recognition of H3K56-acetylated histone H3–H4 by the chaperone Rtt106

Su, D., Hu, Q., Li, Q., Thompson, J. R., Cui, G., Fazly, A., Davies, B. A., Botuyan, M. V., Zhang, Z., & Mer, G. (2012) · Nature · doi:10.1038/nature10861 · Cited by 128

Outward- and inward-facing structures of a putative bacterial transition-metal transporter with homology to ferroportin

Taniguchi, R., Kato, H. E., Font, J., Deshpande, C. N., Wada, M., Ito, K., Ishitani, R., Jormakka, M., & Nureki, O. (2015) · Nature Communications · doi:10.1038/ncomms9545 · Cited by 120

Stability of iron-bearing carbonates in the deep Earth’s interior

Cerantola, V., Bykova, E., Kupenko, I., Merlini, M., Ismailova, L., McCammon, C., Bykov, M., Chumakov, A. I., Petitgirard, S., Kantor, I., et al. (2017) · Nature Communications · doi:10.1038/ncomms15960 · Cited by 120

Crystal structures of a double-barrelled fluoride ion channel

Stockbridge, R. B., Kolmakova-Partensky, L., Shane, T., Koide, A., Koide, S., Miller, C., & Newstead, S. (2015) · Nature · doi:10.1038/nature14981 · Cited by 119

Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate

Wu, X., Bradley, M. J., Cai, Y., Kümmel, D., De La Cruz, E. M., Barr, F. A., & Reinisch, K. M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1110415108 · Cited by 115

Reversal of synapse loss in Alzheimer mouse models by targeting mGluR5 to prevent synaptic tagging by C1Q

Spurrier, J., Nicholson, L., Fang, X. T., Stoner, A. J., Toyonaga, T., Holden, D., Siegert, T. R., Laird, W., Allnutt, M. A., Chiasseu, M., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abi8593 · Cited by 114

A Simple Approach for Predicting the Spin State of Homoleptic Fe(II) Tris-diimine Complexes

Phan, H., Hrudka, J. J., Igimbayeva, D., Lawson Daku, L. M., & Shatruk, M. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b02098 · Cited by 111

Unusual diheme conformation of the heme-degrading protein from Mycobacterium tuberculosis

Chim, N., Iniguez, A., Nguyen, T. Q., & Goulding, C. W. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.11.025 · Cited by 102

Structure and function of cohesin's Scc3/SA regulatory subunit

Roig, M. B., Löwe, J., Chan, K.-L., Beckouët, F., Metson, J., & Nasmyth, K. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.08.015 · Cited by 91

Implications of AlphaFold 2 for crystallographic phasing by molecular replacement

McCoy, A. J., Sammito, M. D., & Read, R. J. (2022) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798321012122 · Cited by 104

The accessibility of nitrogen sites makes a difference in selective CO 2 adsorption of a family of isostructural metal–organic frameworks

Song, C., Hu, J., Ling, Y., Feng, Y., Krishna, R., Chen, D.-L., & He, Y. (2015) · Journal of Materials Chemistry A · doi:10.1039/c5ta05481h · Cited by 91

A Structural Model for Binding of the Serine-Rich Repeat Adhesin GspB to Host Carbohydrate Receptors

Pyburn, T. M., Bensing, B. A., Xiong, Y. Q., Melancon, B. J., Tomasiak, T. M., Ward, N. J., Yankovskaya, V., Oliver, K. M., Cecchini, G., Sulikowski, G. A., et al. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002112 · Cited by 84

Structural basis of BRCC36 function in DNA repair and immune regulation

Rabl, J., Bunker, R. D., Schenk, A. D., Cavadini, S., Gill, M. E., Abdulrahman, W., Andrés-Pons, A., Luijsterburg, M. S., Ibrahim, A. F. M., Branigan, E., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.06.002 · Cited by 84

Thalidomide mimics uridine binding to an aromatic cage in cereblon

Hartmann, M. D., Boichenko, I., Coles, M., Zanini, F., Lupas, A. N., & Hernandez Alvarez, B. (2014) · Journal of Structural Biology · doi:10.1016/j.jsb.2014.10.010 · Cited by 83

Structural Basis for the Acyltransferase Activity of Lecithin:Retinol Acyltransferase-like Proteins

Golczak, M., Kiser, P. D., Sears, A. E., Lodowski, D. T., Blaner, W. S., & Palczewski, K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.361550 · Cited by 77

Determining crystal structures through crowdsourcing and coursework

Horowitz, S., Koepnick, B., Martin, R., Tymieniecki, A., Winburn, A. A., Cooper, S., Flatten, J., Rogawski, D. S., Koropatkin, N. M., Hailu, T. T., et al. (2016) · Nature Communications · doi:10.1038/ncomms12549 · Cited by 75

Single-crystal X-ray diffraction at megabar pressures and temperatures of thousands of degrees

Dubrovinsky, L., Boffa-Ballaran, T., Glazyrin, K., Kurnosov, A., Frost, D., Merlini, M., Hanfland, M., Prakapenka, V. B., Schouwink, P., Pippinger, T., et al. (2010) · High Pressure Research · doi:10.1080/08957959.2010.534092 · Cited by 68

Facile Synthesis of Well-Defined Titanium Alkoxides Based on Benzotriazole Phenoxide Ligands: Efficient Catalysts for Ring-Opening Polymerization of Cyclic Esters

Li, C.-Y., Yu, C.-J., & Ko, B.-T. (2013) · Organometallics · doi:10.1021/om300962k · Cited by 67

Bis(pyrrolidene) Schiff Base Aluminum Complexes as Isoselective-Biased Initiators for the Controlled Ring-Opening Polymerization of rac-Lactide: Experimental and Theoretical Studies

Tabthong, S., Nanok, T., Sumrit, P., Kongsaeree, P., Prabpai, S., Chuawong, P., & Hormnirun, P. (2015) · Macromolecules · doi:10.1021/acs.macromol.5b01381 · Cited by 64

Crystal Structure of Iron(II) Acetate

Weber, B., Betz, R., Bauer, W., & Schlamp, S. (2011) · Zeitschrift für anorganische und allgemeine Chemie · doi:10.1002/zaac.201000274 · Cited by 64

Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90

Bracher, A., Kozany, C., Thost, A.-K., & Hausch, F. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444911013862 · Cited by 62

Structural Conservation of Components in the Amino Acid Sensing Branch of the TOR Pathway in Yeast and Mammals

Kogan, K., Spear, E. D., Kaiser, C. A., & Fass, D. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.07.034 · Cited by 56

Structure and function of a spectrin-like regulator of bacterial cytokinesis

Cleverley, R. M., Barrett, J. R., Baslé, A., Bui, N. K., Hewitt, L., Solovyova, A., Xu, Z.-Q., Daniel, R. A., Dixon, N. E., Harry, E. J., et al. (2014) · Nature Communications · doi:10.1038/ncomms6421 · Cited by 50

Vanadium-based imido-alkoxide pro-catalysts bearing bisphenolate ligands for ethylene and ε-caprolactone polymerisation

Arbaoui, A., Redshaw, C., Homden, D. M., Wright, J. A., & Elsegood, M. R. J. (2009) · Dalton Transactions · doi:10.1039/b902402f · Cited by 52

Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity

Sharma, A. K., Kim, J., Prior, J. T., Hawco, N. J., Rath, N. P., Kim, J., & Mirica, L. M. (2014) · Inorganic Chemistry · doi:10.1021/ic500926c · Cited by 48

A Possible Prebiotic Origin on Volcanic Islands of Oligopyrrole-Type Photopigments and Electron Transfer Cofactors

Fox, S., & Strasdeit, H. (2013) · Astrobiology · doi:10.1089/ast.2012.0934 · Cited by 48

p-Terphenyl Derivatives from the Endolichenic Fungus Floricola striata

Li, W., Gao, W., Zhang, M., Li, Y.-L., Li, L., Li, X.-B., Chang, W.-Q., Zhao, Z.-T., & Lou, H.-X. (2016) · Journal of Natural Products · doi:10.1021/acs.jnatprod.6b00197 · Cited by 48

Raman study of MgCO3–FeCO3 carbonate solid solution at high pressures up to 55 GPa

Spivak, A., Solopova, N., Cerantola, V., Bykova, E., Zakharchenko, E., Dubrovinsky, L., & Litvin, Y. (2014) · Physics and Chemistry of Minerals · doi:10.1007/s00269-014-0676-y · Cited by 48

Synthesis, characterization and reactivity of single-site aluminium amides bearing benzotriazole phenoxide ligands: catalysis for ring-opening polymerization of lactide and carbon dioxide/propylene oxide coupling

Li, C.-Y., Liu, D.-C., & Ko, B.-T. (2013) · Dalton Transactions · doi:10.1039/c3dt51003d · Cited by 47

Should highly cited items be excluded in impact factor calculation? The effect of review articles on journal impact factor

Lei, L., & Sun, Y. (2020) · Scientometrics · doi:10.1007/s11192-019-03338-y · Cited by 43

The Aspergillus fumigatus Sialidase Is a 3-Deoxy-d-glycero-d-galacto-2-nonulosonic Acid Hydrolase (KDNase)

Telford, J. C., Yeung, J. H. F., Xu, G., Kiefel, M. J., Watts, A. G., Hader, S., Chan, J., Bennet, A. J., Moore, M. M., & Taylor, G. L. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.207043 · Cited by 43

Lactide as the Playmaker of the ROP Game: Theoretical and Experimental Investigation of Ring-Opening Polymerization of Lactide Initiated by Aminonaphtholate Zinc Complexes

Jędrzkiewicz, D., Adamus, G., Kwiecień, M., John, Ł., & Ejfler, J. (2017) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.6b02439 · Cited by 42

Vanadium( iii ) phenoxyimine complexes for ethylene or ε-caprolactone polymerization: mononuclear versus binuclear pre-catalysts

Clowes, L., Walton, M., Redshaw, C., Chao, Y., Walton, A., Elo, P., Sumerin, V., & Hughes, D. L. (2013) · Catal. Sci. Technol. · doi:10.1039/c2cy20571h · Cited by 40

Bimetallic aluminum complexes supported by bis(salicylaldimine) ligand: Synthesis, characterization and ring-opening polymerization of lactide

Shi, T., Zheng, Q.-D., Zuo, W.-W., Liu, S.-F., & Li, Z.-B. (2018) · Chinese Journal of Polymer Science · doi:10.1007/s10118-018-2039-5 · Cited by 39

Controlled random copolymerization of rac‐lactide and ɛ‐caprolactone by well‐designed phenoxyimine Al complexes

Shi, T., Luo, W., Liu, S., & Li, Z. (2018) · Journal of Polymer Science Part A: Polymer Chemistry · doi:10.1002/pola.28932 · Cited by 39

Facilely synthesized benzotriazole phenolate zirconium complexes as versatile catalysts for copolymerization of carbon dioxide with cyclohexene oxide and lactide polymerization

Chuang, H.-J., & Ko, B.-T. (2015) · Dalton Transactions · doi:10.1039/c4dt02774d · Cited by 38

Crystallographic Determination of Three Ni-α-Hydroxyoxime-Carboxylic Acid Synergist Complexes

Barnard, K. R., Nealon, G. L., Ogden, M. I., & Skelton, B. W. (2010) · Solvent Extraction and Ion Exchange · doi:10.1080/07366299.2010.515169 · Cited by 35

Structural and functional analysis of EntV reveals a 12 amino acid fragment protective against fungal infections

Cruz, M. R., Cristy, S., Guha, S., De Cesare, G. B., Evdokimova, E., Sanchez, H., Borek, D., Miramón, P., Yano, J., Fidel, P. L., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33613-1 · Cited by 30

Accurate structure determination of a borosilicate zeolite EMM-26 with two-dimensional 10 × 10 ring channels using rotation electron diffraction

Guo, P., Strohmaier, K., Vroman, H., Afeworki, M., Ravikovitch, P. I., Paur, C. S., Sun, J., Burton, A., & Zou, X. (2016) · Inorganic Chemistry Frontiers · doi:10.1039/c6qi00262e · Cited by 29

Structure and Mechanism of LcpA, a Phosphotransferase That Mediates Glycosylation of a Gram-Positive Bacterial Cell Wall-Anchored Protein

Siegel, S. D., Amer, B. R., Wu, C., Sawaya, M. R., Gosschalk, J. E., Clubb, R. T., & Ton-That, H. (2019) · mBio · doi:10.1128/mbio.01580-18 · Cited by 29

Long-lived charge-separated states produced in supramolecular complexes between anionic and cationic porphyrins

Bill, N. L., Ishida, M., Kawashima, Y., Ohkubo, K., Sung, Y. M., Lynch, V. M., Lim, J. M., Kim, D., Sessler, J. L., & Fukuzumi, S. (2014) · Chem. Sci. · doi:10.1039/c4sc00803k · Cited by 28

Organoaluminium complexes of ortho-, meta-, para-anisidines: synthesis, structural studies and ROP of ε-caprolactone (and rac-lactide)

Li, Y., Zhao, K.-Q., Elsegood, M. R. J., Prior, T. J., Sun, X., Mo, S., & Redshaw, C. (2014) · Catal. Sci. Technol. · doi:10.1039/c4cy00624k · Cited by 25

Elucidation of the Structures of Asymmetric Autocatalyst Based on X-ray Crystallography

Matsumoto, A., Fujiwara, S., Abe, T., Hara, A., Tobita, T., Sasagawa, T., Kawasaki, T., & Soai, K. (2016) · Bulletin of the Chemical Society of Japan · doi:10.1246/bcsj.20160160 · Cited by 24

Structural studies of Schiff-base [2 + 2] macrocycles derived from 2,2'-oxydianiline and the ROP capability of their organoaluminium complexes

Yang, W., Zhao, K.-Q., Prior, T. J., Hughes, D. L., Arbaoui, A., Elsegood, M. R. J., & Redshaw, C. (2016) · Dalton Transactions · doi:10.1039/c6dt01997h · Cited by 23

Vanadium( v ) phenolate complexes for ring opening homo- and co-polymerisation of ε-caprolactone, l -lactide and rac-lactide

Ge, F., Dan, Y., Al-Khafaji, Y., Prior, T. J., Jiang, L., Elsegood, M. R. J., & Redshaw, C. (2016) · RSC Advances · doi:10.1039/c5ra24816g · Cited by 22

Anilido-aldimine aluminum complexes: Synthesis, characterization and lactide polymerization

Allan, L. E. N., Bélanger, J. A., Callaghan, L. M., Cameron, D. J. A., Decken, A., & Shaver, M. P. (2012) · Journal of Organometallic Chemistry · doi:10.1016/j.jorganchem.2012.02.003 · Cited by 22

DNA-binding mechanism and evolution of replication protein A

(2023) · doi:10.1038/s41467-023-38048-w · Cited by 22

Solid‐State Emission from Mono‐ and Bichromophoric Boron Dipyrromethene (BODIPY) Derivatives and Comparison with Fluid Solution

Bozdemir, Ö. A., Al‐Sharif, H. H. T., McFarlane, W., Waddell, P. G., Benniston, A. C., & Harriman, A. (2019) · Chemistry – A European Journal · doi:10.1002/chem.201903902 · Cited by 20

The pentatricopeptide repeat protein Rmd9 recognizes the dodecameric element in the 3′-UTRs of yeast mitochondrial mRNAs

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