MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

The Protein Data Bank

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Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?

Brogden, K. A. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1098 · Cited by 5,829

The Pfam protein families database

Bateman, A. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh121 · Cited by 3,127

HADDOCK: A Protein−Protein Docking Approach Based on Biochemical or Biophysical Information

Dominguez, C., Boelens, R., & Bonvin, A. M. J. J. (2003) · Journal of the American Chemical Society · doi:10.1021/ja026939x · Cited by 3,187

Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain

Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.948 · Cited by 2,206

Anatomy of hot spots in protein interfaces

Bogan, A. A., & Thorn, K. S. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1843 · Cited by 1,988

X-ray Crystal Structure of the Fe-Only Hydrogenase (CpI) from Clostridium pasteurianum to 1.8 Angstrom Resolution

Peters, J. W. (1998) · Science · doi:10.1126/science.282.5395.1853 · Cited by 1,891

The Guanine Nucleotide-Binding Switch in Three Dimensions

Vetter, I. R., & Wittinghofer, A. (2001) · Science · doi:10.1126/science.1062023 · Cited by 1,875

Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors

Finnin, M. S., Donigian, J. R., Cohen, A., Richon, V. M., Rifkind, R. A., Marks, P. A., Breslow, R., & Pavletich, N. P. (1999) · Nature · doi:10.1038/43710 · Cited by 1,714

The 26S Proteasome: A Molecular Machine Designed for Controlled Proteolysis

Voges, D., Zwickl, P., & Baumeister, W. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.1015 · Cited by 1,608

Epidermal growth factor receptor: Mechanisms of activation and signalling

Jorissen, R. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(02)00098-8 · Cited by 1,565

Structure of influenza haemagglutinin at the pH of membrane fusion

Bullough, P. A., Hughson, F. M., Skehel, J. J., & Wiley, D. C. (1994) · Nature · doi:10.1038/371037a0 · Cited by 1,564

The Ras-RasGAP Complex: Structural Basis for GTPase Activation and Its Loss in Oncogenic Ras Mutants

Scheffzek, K., Ahmadian, M. R., Kabsch, W., Wiesmüller, L., Lautwein, A., Schmitz, F., & Wittinghofer, A. (1997) · Science · doi:10.1126/science.277.5324.333 · Cited by 1,543

Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex

Zheng, N., Schulman, B. A., Song, L., Miller, J. J., Jeffrey, P. D., Wang, P., Chu, C., Koepp, D. M., Elledge, S. J., Pagano, M., et al. (2002) · Nature · doi:10.1038/416703a · Cited by 1,507

Structural Basis of Transcription: RNA Polymerase II at 2.8 Ångstrom Resolution

Cramer, P., Bushnell, D. A., & Kornberg, R. D. (2001) · Science · doi:10.1126/science.1059493 · Cited by 1,247

Complete Structure of the 11-Subunit Bovine Mitochondrial Cytochrome bc 1 Complex

Iwata, S., Lee, J. W., Okada, K., Lee, J. K., Iwata, M., Rasmussen, B., Link, T. A., Ramaswamy, S., & Jap, B. K. (1998) · Science · doi:10.1126/science.281.5373.64 · Cited by 1,253

Crystal Structure of a Ternary FGF-FGFR-Heparin Complex Reveals a Dual Role for Heparin in FGFR Binding and Dimerization

Schlessinger, J., Plotnikov, A. N., Ibrahimi, O. A., Eliseenkova, A. V., Yeh, B. K., Yayon, A., Linhardt, R. J., & Mohammadi, M. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00073-3 · Cited by 1,199

Structural basis of water-specific transport through the AQP1 water channel

Sui, H., Han, B.-G., Lee, J. K., Walian, P., & Jap, B. K. (2001) · Nature · doi:10.1038/414872a · Cited by 1,166

The Retinal Conformation and its Environment in Rhodopsin in Light of a New 2.2 Å Crystal Structure

Okada, T., Sugihara, M., Bondar, A.-N., Elstner, M., Entel, P., & Buss, V. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.07.044 · Cited by 1,049

Reducing the Environmental Sensitivity of Yellow Fluorescent Protein

Griesbeck, O., Baird, G. S., Campbell, R. E., Zacharias, D. A., & Tsien, R. Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102815200 · Cited by 1,023

Structure and mechanism of carbonic anhydrase

Lindskog, S. (1997) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(96)00198-2 · Cited by 1,022

Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin.

Roe, S. M., Prodromou, C., O'Brien, R., Ladbury, J. E., Piper, P. W., & Pearl, L. H. (1999) · Journal of Medicinal Chemistry · doi:10.1021/jm980403y · Cited by 1,004

Investigating Mitochondrial Redox Potential with Redox-sensitive Green Fluorescent Protein Indicators

Hanson, G. T., Aggeler, R., Oglesbee, D., Cannon, M., Capaldi, R. A., Tsien, R. Y., & Remington, S. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312846200 · Cited by 988

Crystal Structure of a Laccase from the FungusTrametes versicolor at 1.90-Å Resolution Containing a Full Complement of Coppers

Piontek, K., Antorini, M., & Choinowski, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204571200 · Cited by 909

Subtilases: the superfamily of subtilisin-like serine proteases.

Siezen, R. J., & Leunissen, J. A. M. (1997) · Protein Science · doi:10.1002/pro.5560060301 · Cited by 896

Shiga-like toxins are neutralized by tailored multivalent carbohydrate ligands

Kitov, P. I., Sadowska, J. M., Mulvey, G., Armstrong, G. D., Ling, H., Pannu, N. S., Read, R. J., & Bundle, D. R. (2000) · Nature · doi:10.1038/35001095 · Cited by 869

Structural and biochemical basis of apoptotic activation by Smac/DIABLO

Chai, J., Du, C., Wu, J.-W., Kyin, S., Wang, X., & Shi, Y. (2000) · Nature · doi:10.1038/35022514 · Cited by 864

Structure of a c-Cbl–UbcH7 Complex

Zheng, N., Wang, P., Jeffrey, P. D., & Pavletich, N. P. (2000) · Cell · doi:10.1016/s0092-8674(00)00057-x · Cited by 839

Mineralization in ferritin: an efficient means of iron storage

Chasteen, N. D., & Harrison, P. M. (1999) · Journal of Structural Biology · doi:10.1006/jsbi.1999.4118 · Cited by 815

The physiological structure of human C-reactive protein and its complex with phosphocholine

Thompson, D., Pepys, M. B., & Wood, S. P. (1999) · Structure · doi:10.1016/s0969-2126(99)80023-9 · Cited by 818

Crystal Structure of the Catalytic Domain of HIV-1 Integrase: Similarity to Other Polynucleotidyl Transferases

Dyda, F., Hickman, A. B., Jenkins, T. M., Engelman, A., Craigie, R., & Davies, D. R. (1994) · Science · doi:10.1126/science.7801124 · Cited by 810

Siderophore-Mediated Iron Transport: Crystal Structure of FhuA with Bound Lipopolysaccharide

Ferguson, A. D., Hofmann, E., Coulton, J. W., Diederichs, K., & Welte, W. (1998) · Science · doi:10.1126/science.282.5397.2215 · Cited by 787

Structure of an HIF-1α-pVHL Complex: Hydroxyproline Recognition in Signaling

Min, J.-H., Yang, H., Ivan, M., Gertler, F., Kaelin, W. G., & Pavletich, N. P. (2002) · Science · doi:10.1126/science.1073440 · Cited by 765

ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer

Smith, P. C., Karpowich, N., Millen, L., Moody, J. E., Rosen, J., Thomas, P. J., & Hunt, J. F. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00576-2 · Cited by 773

Energetic optimization of ion conduction rate by the K+ selectivity filter

Morais-Cabral, J. H., Zhou, Y., & MacKinnon, R. (2001) · Nature · doi:10.1038/35102000 · Cited by 761

Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes

Wang, M., Roberts, D. L., Paschke, R., Shea, T. M., Masters, B. S. S., & Kim, J.-J. P. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.16.8411 · Cited by 744

Solution structure and basis for functional activity of stromal cell‐derived factor‐1; dissociation of CXCR4 activation from binding and inhibition of HIV‐1

Crump, M. P., Gong, J., Loetscher, P., Rajarathnam, K., Amara, A., Arenzana‐Seisdedos, F., Virelizier, J., Baggiolini, M., Sykes, B. D., & Clark‐Lewis, I. (1997) · The EMBO Journal · doi:10.1093/emboj/16.23.6996 · Cited by 731

Activation mechanism of the MAP kinase ERK2 by dual phosphorylation

Canagarajah, B. J., Khokhlatchev, A., Cobb, M. H., & Goldsmith, E. J. (1997) · Cell · doi:10.1016/s0092-8674(00)80351-7 · Cited by 729

A leucine-rich nuclear export signal in the p53 tetramerization domain: regulation of subcellular localization and p53 activity by NES masking

Stommel, J. M., Marchenko, N. D., Jimenez, G. S., Moll, U. M., Hope, T. J., & Wahl, G. M. (1999) · The EMBO Journal · doi:10.1093/emboj/18.6.1660 · Cited by 738

INHIBITORS OF HIV-1 PROTEASE: A Major Success of Structure-Assisted Drug Design

Wlodawer, A., & Vondrasek, J. (1998) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.27.1.249 · Cited by 734

ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo

Panaretou, B., Prodromou, C., Roe, S. M., O'Brien, R., Ladbury, J. E., Piper, P. W., & Pearl, L. H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.16.4829 · Cited by 735

Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion

Enroth, C., Eger, B. T., Okamoto, K., Nishino, T., Nishino, T., & Pai, E. F. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.20.10723 · Cited by 733

Crystal Structure of Human Cyclophilin A Bound to the Amino-Terminal Domain of HIV-1 Capsid

Gamble, T. R., Vajdos, F. F., Yoo, S., Worthylake, D. K., Houseweart, M., Sundquist, W. I., & Hill, C. P. (1996) · Cell · doi:10.1016/s0092-8674(00)81823-1 · Cited by 706

Structural Snapshots of Human HDAC8 Provide Insights into the Class I Histone Deacetylases

Somoza, J. R., Skene, R. J., Katz, B. A., Mol, C., Ho, J. D., Jennings, A. J., Luong, C., Arvai, A., Buggy, J. J., Chi, E., et al. (2004) · Structure · doi:10.1016/j.str.2004.04.012 · Cited by 710

Insights into DNA recombination from the structure of a RAD51–BRCA2 complex

Pellegrini, L., Yu, D. S., Lo, T., Anand, S., Lee, M., Blundell, T. L., & Venkitaraman, A. R. (2002) · Nature · doi:10.1038/nature01230 · Cited by 704

Structural basis of calcium-induced E-cadherin rigidification and dimerization

Nagar, B., Overduin, M., Ikura, M., & Rini, J. M. (1996) · Nature · doi:10.1038/380360a0 · Cited by 684

Selection of tRNA by the Ribosome Requires a Transition from an Open to a Closed Form

Ogle, J. M., Murphy, F. V., Tarry, M. J., & Ramakrishnan, V. (2002) · Cell · doi:10.1016/s0092-8674(02)01086-3 · Cited by 663

Structure of the HIV-1 Nucleocapsid Protein Bound to the SL3 Ψ-RNA Recognition Element

De Guzman, R. N., Wu, Z. R., Stalling, C. C., Pappalardo, L., Borer, P. N., & Summers, M. F. (1998) · Science · doi:10.1126/science.279.5349.384 · Cited by 659

Structure of a β-TrCP1-Skp1-β-Catenin Complex

Wu, G., Xu, G., Schulman, B. A., Jeffrey, P. D., Harper, J. W., & Pavletich, N. P. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00234-x · Cited by 612

Structural Evidence for Ligand Specificity in the Binding Domain of the Human Androgen Receptor

Matias, P. M., Donner, P., Coelho, R., Thomaz, M., Peixoto, C., Macedo, S., Otto, N., Joschko, S., Scholz, P., Wegg, A., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004571200 · Cited by 608

The fibronectin type III domain as a scaffold for novel binding proteins

Koide, A., Bailey, C. W., Huang, X., & Koide, S. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2238 · Cited by 585

The Design of Coiled-Coil Structures and Assemblies

Woolfson, D. N. (2005) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(05)70004-8 · Cited by 585

Phosphorylation of Ser-20 mediates stabilization of human p53 in response to DNA damage.

Chehab, N. H., Malikzay, A., Stavridi, E. S., & Halazonetis, T. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.13777 · Cited by 583

Absolute Binding Free Energies: A Quantitative Approach for Their Calculation

Boresch, S., Tettinger, F., Leitgeb, M., & Karplus, M. (2003) · The Journal of Physical Chemistry B · doi:10.1021/jp0217839 · Cited by 569

IL-17s adopt a cystine knot fold: structure and activity of a novel cytokine, IL-17F, and implications for receptor binding

Hymowitz, S. G., Filvaroff, E. H., Yin, J., Lee, J., Cai, L., Risser, P., Maruoka, M., Mao, W., Foster, J., Kelley, R. F., et al. (2001) · The EMBO Journal · doi:10.1093/emboj/20.19.5332 · Cited by 548

X-Ray Structures of Myc-Max and Mad-Max Recognizing DNA

Nair, S. K., & Burley, S. K. (2003) · Cell · doi:10.1016/s0092-8674(02)01284-9 · Cited by 551

Transmembrane Signaling across the Ligand-Gated FhuA Receptor

Locher, K. P., Rees, B., Koebnik, R., Mitschler, A., Moulinier, L., Rosenbusch, J. P., & Moras, D. (1998) · Cell · doi:10.1016/s0092-8674(00)81700-6 · Cited by 540

Structural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4a

Russo, A. A., Tong, L., Lee, J.-O., Jeffrey, P. D., & Pavletich, N. P. (1998) · Nature · doi:10.1038/26155 · Cited by 524

Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA

Chen, L., Glover, J. N. M., Hogan, P. G., Rao, A., & Harrison, S. C. (1998) · Nature · doi:10.1038/32100 · Cited by 521

Latrunculin alters the actin-monomer subunit interface to prevent polymerization

Morton, W. M., Ayscough, K. R., & McLaughlin, P. J. (2000) · Nature Cell Biology · doi:10.1038/35014075 · Cited by 523

Structure of the LDL Receptor Extracellular Domain at Endosomal pH

Rudenko, G., Henry, L., Henderson, K., Ichtchenko, K., Brown, M. S., Goldstein, J. L., & Deisenhofer, J. (2002) · Science · doi:10.1126/science.1078124 · Cited by 482

Crystal structure of an isoleucine-zipper trimer

Harbury, P. B., Kim, P. S., & Alber, T. (1994) · Nature · doi:10.1038/371080a0 · Cited by 472

Structure of the Protein Phosphatase 2A Holoenzyme

Xu, Y., Xing, Y., Chen, Y., Chao, Y., Lin, Z., Fan, E., Yu, J. W., Strack, S., Jeffrey, P. D., & Shi, Y. (2006) · Cell · doi:10.1016/j.cell.2006.11.033 · Cited by 450

Structure of the Amino-Terminal Core Domain of the HIV-1 Capsid Protein

Gitti, R. K., Lee, B. M., Walker, J., Summers, M. F., Yoo, S., & Sundquist, W. I. (1996) · Science · doi:10.1126/science.273.5272.231 · Cited by 459

Structure of a unique binuclear manganese cluster in arginase

Kanyo, Z. F., Scolnick, L. R., Ash, D. E., & Christianson, D. W. (1996) · Nature · doi:10.1038/383554a0 · Cited by 441

Signal peptidases.

Paetzel, M., Karla, A., Strynadka, N. C. J., & Dalbey, R. E. (2002) · Chemical Reviews · doi:10.1021/cr010166y · Cited by 440

Structure of Human Methionine Aminopeptidase-2 Complexed with Fumagillin

Liu, S., Widom, J., Kemp, C. W., Crews, C. M., & Clardy, J. (1998) · Science · doi:10.1126/science.282.5392.1324 · Cited by 440

An Extremely Potent Inhibitor of Xanthine Oxidoreductase

Okamoto, K., Eger, B. T., Nishino, T., Kondo, S., Pai, E. F., & Nishino, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208307200 · Cited by 434

The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD) 1 1Edited by P. E. Wight

Bateman, A., & Bycroft, M. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3778 · Cited by 432

Dali/FSSP classification of three-dimensional protein folds

Holm, L., & Sander, C. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.1.231 · Cited by 421

DNA Polymerase γ, The Mitochondrial Replicase

Kaguni, L. S. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161455 · Cited by 414

GTPase-activating proteins: Helping hands to complement an active site

Scheffzek, K., Ahmadian, M. R., & Wittinghofer, A. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01224-9 · Cited by 410

Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance

Hinrichs, W., Kisker, C., Düvel, M., Müller, A., Tovar, K., Hillen, W., & Saenger, W. (1994) · Science · doi:10.1126/science.8153629 · Cited by 408

Crystal structure of the HIV-1 integrase catalytic core and C-terminal domains: a model for viral DNA binding

Chen, J. C.-H., Krucinski, J., Miercke, L. J. W., Finer-Moore, J. S., Tang, A. H., Leavitt, A. D., & Stroud, R. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.150220297 · Cited by 404

Structure of Factor-inhibiting Hypoxia-inducible Factor (HIF) Reveals Mechanism of Oxidative Modification of HIF-1α

Elkins, J. M., Hewitson, K. S., McNeill, L. A., Seibel, J. F., Schlemminger, I., Pugh, C. W., Ratcliffe, P. J., & Schofield, C. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200644200 · Cited by 391

Crystal Structure at 2.8 Å of an FcRn/Heterodimeric Fc Complex

Martin, W. L., West, A. P., Gan, L., & Bjorkman, P. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00230-1 · Cited by 391

Microtubule interaction site of the kinesin motor

Woehlke, G., Ruby, A. K., Hart, C. L., Ly, B., Hom-Booher, N., & Vale, R. D. (1997) · Cell · doi:10.1016/s0092-8674(00)80329-3 · Cited by 386

Identification of amino acid residues in the capsid proteins of adeno-associated virus type 2 that contribute to heparan sulfate proteoglycan binding

Opie, S. R., Warrington, Agbandje-McKenna, M., Zolotukhin, S., & Muzyczka, N. (2003) · Journal of Virology · doi:10.1128/jvi.77.12.6995-7006.2003 · Cited by 364

Evolutionary history, structural features and biochemical diversity of the NlpC/P60 superfamily of enzymes

Anantharaman, V., & Aravind, L. (2003) · Genome Biology · doi:10.1186/gb-2003-4-2-r11 · Cited by 365

SOCKET: a program for identifying and analysing coiled-coil motifs within protein structures11Edited by J. Thornton

Walshaw, J., & Woolfson, D. N. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4545 · Cited by 357

Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1

Worthylake, D. K., Rossman, K. L., & Sondek, J. (2000) · Nature · doi:10.1038/35047014 · Cited by 355

Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms

Nagashima, S., Nakasako, M., Dohmae, N., Tsujimura, M., Takio, K., Odaka, M., Yohda, M., Kamiya, N., & Endo, I. (1998) · Nature Structural Biology · doi:10.1038/nsb0598-347 · Cited by 353

Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins

Xing, Y., Xu, Y., Chen, Y., Jeffrey, P. D., Chao, Y., Lin, Z., Li, Z., Strack, S., Stock, J. B., & Shi, Y. (2006) · Cell · doi:10.1016/j.cell.2006.09.025 · Cited by 334

Understanding how proteins fold: the lysozyme story so far

Dobson, C. M., Evans, P. A., & Radford, S. E. (1994) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(94)90171-6 · Cited by 340

Revealing mechanisms for SH2 domain mediated regulation of the protein tyrosine phosphatase SHP-2

Barford, D., & Neel, B. G. (1998) · Structure · doi:10.1016/s0969-2126(98)00027-6 · Cited by 321

Architecture of a protein central to iron homeostasis: crystal structure and spectroscopic analysis of the ferric uptake regulator

Pohl, E., Haller, J. C., Mijovilovich, A., Meyer‐Klaucke, W., Garman, E., & Vasil, M. L. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03337.x · Cited by 326

Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase a receptor.

Fernandez‐Catalan, C., Bode, W., Huber, R., Turk, D., Calvete, J. J., Lichte, A., Tschesche, H., & Maskos, K. (1998) · The EMBO Journal · doi:10.1093/emboj/17.17.5238 · Cited by 321

Rhodopsin: Structural Basis of Molecular Physiology

Menon, S. T., Han, M., & Sakmar, T. P. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.4.1659 · Cited by 304

Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling

Daumke, O., Lundmark, R., Vallis, Y., Martens, S., Butler, P. J. G., & McMahon, H. T. (2007) · Nature · doi:10.1038/nature06173 · Cited by 304

Structure–function studies on nitric oxide synthases

LI, H., & POULOS, T. (2005) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2004.10.016 · Cited by 302

Structure of Internalin, a Major Invasion Protein of Listeria monocytogenes, in Complex with Its Human Receptor E-Cadherin

Schubert, W.-D., Urbanke, C., Ziehm, T., Beier, V., Machner, M. P., Domann, E., Wehland, J., Chakraborty, T., & Heinz, D. W. (2002) · Cell · doi:10.1016/s0092-8674(02)01136-4 · Cited by 302

The Mad2 spindle checkpoint protein has two distinct natively folded states

Luo, X., Tang, Z., Xia, G., Wassmann, K., Matsumoto, T., Rizo, J., & Yu, H. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb748 · Cited by 297

Crystal structure of protoporphyrinogen IX oxidase: a key enzyme in haem and chlorophyll biosynthesis

Koch, M., Breithaupt, C., Kiefersauer, R., Freigang, J., Huber, R., & Messerschmidt, A. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600189 · Cited by 299

The crystal structure of xanthine oxidoreductase during catalysis: Implications for reaction mechanism and enzyme inhibition

Okamoto, K., Matsumoto, K., Hille, R., Eger, B. T., Pai, E. F., & Nishino, T. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400973101 · Cited by 286

Crystal Structure of Invasin: A Bacterial Integrin-Binding Protein

Hamburger, Z. A., Brown, M. S., Isberg, R. R., & Bjorkman, P. J. (1999) · Science · doi:10.1126/science.286.5438.291 · Cited by 287

Structure of a voltage-dependent K+ channel β subunit

Gulbis, J. M., Mann, S., & MacKinnon, R. (1999) · Cell · doi:10.1016/s0092-8674(00)80805-3 · Cited by 283

Crystal structure of the first dissimilatory nitrate reductase at 1.9 Å solved by MAD methods

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Crystallographic studies of quinol oxidation site inhibitors: a modified classification of inhibitors for the cytochrome bc(1) complex

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