Structure of a 14-3-3 Coordinated Hexamer of the Plant Plasma Membrane H+-ATPase by Combining X-Ray Crystallography and Electron Cryomicroscopy

UCSF Chimera—A visualization system for exploratory research and analysis

Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 45,260 · see citing works

PROCHECK: a program to check the stereochemical quality of protein structures

Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581 · see citing works

The PyMOL Molecular Graphics System

DeLano, W. L. (2002) · Medical Entomology and Zoology · Cited by 18,147 · see citing works

The CCP4 suite: programs for protein crystallography

Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,299 · see citing works

Comparative Protein Modelling by Satisfaction of Spatial Restraints

Šali, A., & Blundell, T. L. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1626 · Cited by 12,977 · see citing works

Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants

Kabsch, W. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889893005588 · Cited by 3,562 · see citing works

Validation of the general purpose tripos 5.2 force field

Clark, M., CRAMER, R. D. I., & Opdenbosch, N. V. (1989) · Journal of Computational Chemistry · doi:10.1002/jcc.540100804 · Cited by 2,803 · see citing works

XtalView/Xfit—A Versatile Program for Manipulating Atomic Coordinates and Electron Density

McRee, D. E. (1999) · Journal of Structural Biology · doi:10.1006/jsbi.1999.4094 · Cited by 2,096 · see citing works

SPIDER and WEB: Processing and Visualization of Images in 3D Electron Microscopy and Related Fields

Frank, J., Radermacher, M., Penczek, P. A., Zhu, J., Li, Y., Ladjadj, M., & Leith, A. G. (1996) · Journal of Structural Biology · doi:10.1006/jsbi.1996.0030 · Cited by 2,026 · see citing works

Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution

Toyoshima, C., Nakasako, M., NOMURA, H., & Ogawa, H. (2000) · Nature · doi:10.1038/35015017 · Cited by 1,798 · see citing works

The Structural Basis for 14-3-3:Phosphopeptide Binding Specificity

Yaffe, M. B., Rittinger, K., Volinia, S., Caron, P. R., Aitken, A., Leffers, H. C. B., Gamblin, S. J., Smerdon, S. J., & Cantley, L. C. (1997) · Cell · doi:10.1016/s0092-8674(00)80487-0 · Cited by 1,604 · see citing works

Efficient anisotropic refinement of macromolecular structures using FFT

Murshudov, G. N., Vagin, A. A., Lebedev, A., Wilson, K. S., & Dodson, E. J. (1999) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s090744499801405x · Cited by 937 · see citing works

Fusicoccin: A Tool in Plant Physiology

Marrè, E. (1979) · Annual Review of Plant Physiology · doi:10.1146/annurev.pp.30.060179.001421 · Cited by 806 · see citing works

Comparative protein modeling by satisfaction of spatial restraints

⩽ali, A. (1995) · Molecular Medicine Today · doi:10.1016/s1357-4310(95)91170-7 · Cited by 785 · see citing works

Implementation of molecular replacement in AMoRe

Navaza, J. (2001) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444901012422 · Cited by 615 · see citing works

Exact filters for general geometry three dimensional reconstruction

Harauz, G., & van Heel, M. (1986) · Optik · Cited by 534 · see citing works

Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes

MacKintosh, C. (2004) · Biochemical Journal · doi:10.1042/bj20031332 · Cited by 527 · see citing works

Improved prediction of protein secondary structure by use of sequence profiles and neural networks.

Rost, B., & Sander, C. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.16.7558 · Cited by 516 · see citing works

Crystal Structure of the 14-3-3ζ:Serotonin N-Acetyltransferase Complex

Obšil, T., Ghirlando, R., Klein, D. C., Ganguly, S., & Dyda, F. (2001) · Cell · doi:10.1016/s0092-8674(01)00316-6 · Cited by 389 · see citing works

Structural view of a fungal toxin acting on a 14‐3‐3 regulatory complex

Würtele, M., Jelich-Ottmann, C., Wittinghofer, A., & Oecking, C. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg104 · Cited by 349 · see citing works

Binding of 14-3-3 Protein to the Plasma Membrane H+-ATPase AHA2 Involves the Three C-terminal Residues Tyr946-Thr-Val and Requires Phosphorylation of Thr947

Fuglsang, A. T., Visconti, S., Drumm, K., Jahn, T. P., Stensballe, A., Mattei, B., Jensen, O. N., Aducci, P., & Palmgren, M. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.51.36774 · Cited by 343 · see citing works

Phosphorylation‐dependent interactions between enzymes of plant metabolism and 14‐3‐3 proteins

Moorhead, G. B. G., Douglas, P., Cotelle, V., Harthill, J. E., MORRICE, N. A., Meek, S. E. M., Deiting, U., Stitt, M., Scarabel, M., Aitken, A., et al. (1999) · The Plant Journal · doi:10.1046/j.1365-313x.1999.00417.x · Cited by 278 · see citing works

Phosphorylation of Thr-948 at the C Terminus of the Plasma Membrane H+-ATPase Creates a Binding Site for the Regulatory 14-3-3 Protein

Svennelid, F., Olsson, A., Piotrowski, M., Rosenquist, M., Ottman, C., Larsson, C. U., Oecking, C., & Sommarin, M. (1999) · The Plant Cell · doi:10.1105/tpc.11.12.2379 · Cited by 248 · see citing works

Melatonin synthesis: 14-3-3-dependent activation and inhibition of arylalkylamine N -acetyltransferase mediated by phosphoserine-205

Ganguly, S., Weller, J. L., Ho, A., Chemineau, P., Malpaux, B., & Klein, D. C. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406871102 · Cited by 220 · see citing works

Structure of keyhole limpet hemocyanin type 1 (KLH1) at 15 Å resolution by electron cryomicroscopy and angular reconstitution † 1 †This article is dedicated to the memory of Anneke van Heel. 1Edited by M.F. Moody

Orlova, E. V., Dube, P., Harris, J. R., Beckman, E., Zemlin, F., Markl, J., & van Heel, M. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1182 · Cited by 203 · see citing works

Xmipp: An Image Processing Package for Electron Microscopy

Marabini, R., Masegosa, I. M., Martı́n, C. S., et al. (1996) · Journal of Structural Biology · doi:10.1006/jsbi.1996.0036 · Cited by 196 · see citing works

A Plant Plasma Membrane H+-ATPase Expressed in Yeast Is Activated by Phosphorylation at Its Penultimate Residue and Binding of 14-3-3 Regulatory Proteins in the Absence of Fusicoccin

Maudoux, O., Batoko, H., Oecking, C., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m909690199 · Cited by 147 · see citing works

Topology and target interaction of the fusicoccin‐binding 14‐3‐3 homologs of Commelina communis

Oecking, C., Piotrowski, M., Hagemeier, J., et al. (1997) · The Plant Journal · doi:10.1046/j.1365-313x.1997.12020441.x · Cited by 133 · see citing works

Single Point Mutations Distributed in 10 Soluble and Membrane Regions of the Nicotiana plumbaginifolia Plasma Membrane PMA2 H+-ATPase Activate the Enzyme and Modify the Structure of the C-terminal Region

Morsomme, P., Dambly, S., Maudoux, O., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.52.34837 · Cited by 129 · see citing works

Activation of the plant plasma membrane H + -ATPase by phosphorylation and binding of 14-3-3 proteins converts a dimer into a hexamer

Kanczewska, J., Marco, S., Vandermeeren, C., Maudoux, O., Rigaud, J., & Boutry, M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504498102 · Cited by 127 · see citing works

Phosphorylation of Thr-948 at the C Terminus of the Plasma Membrane H + -ATPase Creates a Binding Site for the Regulatory 14-3-3 Protein

Svennelid, F., Olsson, A., Piotrowski, M., et al. (1999) · The Plant Cell · doi:10.2307/3870962 · Cited by 127 · see citing works

The Binding Site for Regulatory 14-3-3 Protein in Plant Plasma Membrane H+-ATPase

Fuglsang, A. T., Borch, J., Bych, K., Jahn, T. P., Roepstorff, P., & Palmgren, M. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306707200 · Cited by 114 · see citing works

A highly sensitive and non-lethal β-galactosidase plate assay for yeast

Duttweiler, H. M. (1996) · Trends in Genetics · doi:10.1016/s0168-9525(96)80008-4 · Cited by 114 · see citing works

Structure, Mechanism, and Regulation of the Neurospora Plasma Membrane H + -ATPase

Kühlbrandt, W., Zeelen, J., & Dietrich, J. (2002) · Science · doi:10.1126/science.1072574 · Cited by 112 · see citing works

Pattern recognition and classification of images of biological macromolecules using artificial neural networks

Marabini, R., & Carazo, J. M. (1994) · Biophysical Journal · doi:10.1016/s0006-3495(94)80974-9 · Cited by 110 · see citing works

Molecular Dissection of the C-Terminal Regulatory Domain of the Plant Plasma Membrane H + -ATPase AHA2: Mapping of Residues that When Altered Give Rise to an Activated Enzyme

Axelsen, K. B., Venema, K., Jahn, T. P., Baunsgaard, L., & Palmgren, M. B. (1999) · Biochemistry · doi:10.1021/bi982482l · Cited by 105 · see citing works

C-terminal Recognition by 14-3-3 Proteins for Surface Expression of Membrane Receptors

Coblitz, B., Shikano, S., Wu, M., Gabelli, S. B., Cockrell, L. M., Spieker, M., Hanyu, Y., Fu, H., Amzel, L. M., & Li, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507559200 · Cited by 101 · see citing works

14-3-3ζ C-terminal Stretch Changes Its Conformation upon Ligand Binding and Phosphorylation at Thr232

Obšilová, V., Heřman, P., Večeř, J., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m306939200 · Cited by 91 · see citing works

Correlation of Internal Torsional Motion with Overall Molecular Motion in Crystals

Schomaker, V., & Trueblood, K. N. (1998) · Acta Crystallographica Section B Structural Science · doi:10.1107/s0108768198003243 · Cited by 89 · see citing works

Role of the 14‐3‐3 C‐terminal loop in ligand interaction

Truong, A. B., Masters, S. C., Yang, H., et al. (2002) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10210 · Cited by 71 · see citing works

A variant to the “random approximation” of the reference-free alignment algorithm

Marco, S., Chagoyen, M., de la Fraga, L. G., et al. (1996) · Ultramicroscopy · doi:10.1016/s0304-3991(96)00083-6 · Cited by 65 · see citing works

Complementation of the Saccharomyces cerevisiaePlasma Membrane H+-ATPase by a Plant H+-ATPase Generates a Highly Abundant Fusicoccin Binding Site

Piotrowski, M., Morsomme, P., Boutry, M., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.45.30018 · Cited by 55 · see citing works

Binding of Regulatory 14-3-3 Proteins to the C Terminus of the Plant Plasma Membrane H+-ATPase Involves Part of Its Autoinhibitory Region

Jelich-Ottmann, C., Weiler, E. W., & Oecking, C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106746200 · Cited by 48 · see citing works

The C‐terminal tail of Arabidopsis 14‐3‐3ω functions as an autoinhibitor and may contain a tenth α‐helix

Shen, W., Clark, A. C., & Huber, S. C. (2003) · The Plant Journal · doi:10.1046/j.1365-313x.2003.01739.x · Cited by 42 · see citing works

Association of 14-3-3 proteins with the C-terminal autoinhibitory domain of the plant plasma-membrane H + -ATPase generates a fusicoccin-binding complex

Oecking, C., & Hagemann, K. (1999) · Planta · doi:10.1007/s004250050507 · Cited by 41 · see citing works

Domain movements of plasma membrane H+‐ATPase: 3D structures of two states by electron cryo‐microscopy

Rhee, K., Scarborough, G. A., & Henderson, R. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf385 · Cited by 28 · see citing works

The Two Major Plant Plasma Membrane H+-ATPases Display Different Regulatory Properties

Dambly, S., & Boutry, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007740200 · Cited by 22 · see citing works

Regulatory 14-3-3 proteins bind the atypical motif within the C terminus of the plant plasma membrane H + -ATPase via their typical amphipathic groove

Jaspert, N., & Oecking, C. (2002) · Planta · doi:10.1007/s00425-002-0915-1 · Cited by 13 · see citing works

Recent advances in the development of protein–protein interactions modulators: mechanisms and clinical trials

Lu, H., Zhou, Q., He, J., Jiang, Z., Peng, C., Tong, R., & Shi, J. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00315-3 · Cited by 891 · see citing works

Modulators of Protein–Protein Interactions

Milroy, L.-G., Grossmann, T. N., Hennig, S., Brunsveld, L., & Ottmann, C. (2014) · Chemical Reviews · doi:10.1021/cr400698c · Cited by 497 · see citing works

Chasing molecular glue degraders: screening approaches

Domostegui, A., Nieto-Barrado, L., Perez-Lopez, C., & Mayor-Ruiz, C. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00197g · Cited by 200 · see citing works

A Semisynthetic Fusicoccane Stabilizes a Protein-Protein Interaction and Enhances the Expression of K+ Channels at the Cell Surface

Anders, C., Higuchi, Y., Koschinsky, K., Bartel, M., Schumacher, B., Thiel, P., Nitta, H., Preisig-Müller, R., Schlichthörl, G., Renigunta, V., et al. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.03.015 · Cited by 106 · see citing works

A Structural Rationale for Selective Stabilization of Anti-tumor Interactions of 14-3-3 proteins by Cotylenin A

Ottmann, C., Weyand, M., Sassa, T., Inoue, T., Kato, N., Wittinghofer, A., & Oecking, C. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.01.005 · Cited by 94 · see citing works

Stabilization and Inhibition of Protein–Protein Interactions: The 14-3-3 Case Study

Milroy, L.-G., Brunsveld, L., & Ottmann, C. (2013) · ACS Chemical Biology · doi:10.1021/cb300599t · Cited by 88 · see citing works

Small molecule modulators of protein-protein interactions: selected case studies

Aeluri, M., Chamakuri, S., Dasari, B., Guduru, S. K. R., Jimmidi, R., Jogula, S., & Arya, P. (2014) · Chemical Reviews · doi:10.1021/cr4004049 · Cited by 79 · see citing works

Mechanism of head-to-head MCM double-hexamer formation revealed by cryo-EM

Miller, T. C. R., Locke, J., Greiwe, J. F., et al. (2019) · Nature · doi:10.1038/s41586-019-1768-0 · Cited by 154 · see citing works

The ?? complexes of ATP synthase: the ?3?3 oligomer and ?1?1 protomer

Kagawa, Y., Ohta, S., Harada, M., et al. (1992) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf00762360 · Cited by 9 · see citing works

Explicit Solvent Molecular Dynamics Simulation Studies of the Dissociation of Human Insulin Hexamer into the Dimeric Units

Yusuff, O. K., Raji, A. T., Raheem, M. A. O. A., et al. (2020) · doi:10.22034/ajca.2020.107265 · Cited by 2 · see citing works

What Gives an Insulin Hexamer Its Unique Shape and Stability? Role of Ten Confined Water Molecules

Mukherjee, S., Mondal, S., Deshmukh, A., et al. (2018) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.8b00453 · Cited by 58 · see citing works

The structure of the S6-symmetric methanol hexamer assembled in a supramolecular hydrophobic cavity

Weyhermüller, T., & Wieghardt, K. E. (1998) · Chemical Communications · doi:10.1039/a708730f · Cited by 6 · see citing works