Structural basis for protein antiaggregation activity of the trigger factor chaperone.

NMRPipe: A multidimensional spectral processing system based on UNIX pipes

Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,961

Molecular chaperones in protein folding and proteostasis

Hartl, F. U., Bracher, A., & Hayer-Hartl, M. (2011) · Nature · doi:10.1038/nature10317 · Cited by 3,381

Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein

Hartl, F. U., & Hayer-Hartl, M. K. (2002) · Science · doi:10.1126/science.1068408 · Cited by 3,335

TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts

Shen, Y., Delaglio, F., Cornilescu, G., & Bax, A. (2009) · Journal of Biomolecular NMR · doi:10.1007/s10858-009-9333-z · Cited by 2,538

Molecular Chaperones and Protein Quality Control

Bukau, B., Weissman, J. S., & Horwich, A. L. (2006) · Cell · doi:10.1016/j.cell.2006.04.014 · Cited by 1,580

Automated NMR Structure Calculation With CYANA

Güntert, P. (2004) · Humana Press eBooks · doi:10.1385/1-59259-809-9:353 · Cited by 1,354

Version 1.2 of the Crystallography and NMR system

Brünger, A. T. (2007) · Nature Protocols · doi:10.1038/nprot.2007.406 · Cited by 1,325

Converging concepts of protein folding in vitro and in vivo

Hartl, F. U., & Hayer-Hartl, M. K. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1591 · Cited by 1,235

Chaperone machines for protein folding, unfolding and disaggregation

Saibil, H. R. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3658 · Cited by 1,211

Pathways of chaperone-mediated protein folding in the cytosol

Young, J. C., Agashe, V. R., Siegers, K., & Hartl, F. U. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1492 · Cited by 1,121

In vivo aspects of protein folding and quality control

Balchin, D., Hayer-Hartl, M. K., & Hartl, F. U. (2016) · Science · doi:10.1126/science.aac4354 · Cited by 1,477

Protein export through the bacterial Sec pathway

Tsirigotaki, A., De Geyter, J., Šoštaric´, N., Economou, A., & Karamanou, S. (2017) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2016.161 · Cited by 447

Regulation of α-synuclein by chaperones in mammalian cells

Burmann, B. M., Gerez, J. A., Matečko-Burmann, I., Campioni, S., Kumari, P., Ghosh, D., Mazur, A., Aspholm, E. E., Šulskis, D., Wawrzyniuk, M., et al. (2020) · Nature · doi:10.1038/s41586-019-1808-9 · Cited by 255

NMR spectroscopy captures the essential role of dynamics in regulating biomolecular function

Alderson, T. R., & Kay, L. E. (2021) · Cell · doi:10.1016/j.cell.2020.12.034 · Cited by 233

Single-Molecule Studies of Protein Folding with Optical Tweezers

Bustamante, C., Alexander, L., Maciuba, K., & Kaiser, C. (2020) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-013118-111442 · Cited by 200

Mechanisms of Cotranslational Maturation of Newly Synthesized Proteins

Krämer, G., Shiber, A., & Bukau, B. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-013118-111717 · Cited by 191

Methyl-specific isotopic labeling: a molecular tool box for solution NMR studies of large proteins

Kerfah, R., Plevin, M. J., Sounier, R., Gans, P., & Boisbouvier, J. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.03.009 · Cited by 200

Biological phase separation: cell biology meets biophysics

Yoshizawa, T., Nozawa, R., Jia, T. Z., Saio, T., & Mori, E. (2020) · Biophysical Reviews · doi:10.1007/s12551-020-00680-x · Cited by 194

Profiling Ssb-Nascent Chain Interactions Reveals Principles of Hsp70-Assisted Folding

Döring, K., Ahmed, N., Riemer, T., Suresh, H. G., Vainshtein, Y., Habich, M., Riemer, J., Mayer, M. P., O’Brien, E. P., Krämer, G., et al. (2017) · Cell · doi:10.1016/j.cell.2017.06.038 · Cited by 181

Inorganic polyphosphate, a multifunctional polyanionic protein scaffold

Xie, L., & Jakob, U. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.rev118.002808 · Cited by 172

Protein dynamics and function from solution state NMR spectroscopy

Kovermann, M., Rogne, P., & Wolf‐Watz, M. (2016) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583516000019 · Cited by 177

Structural basis for the antifolding activity of a molecular chaperone

Huang, C., Rossi, P., Saio, T., & Kalodimos, C. G. (2016) · Nature · doi:10.1038/nature18965 · Cited by 168

Methyl TROSY spectroscopy: A versatile NMR approach to study challenging biological systems

Schütz, S., & Sprangers, R. (2019) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/j.pnmrs.2019.09.004 · Cited by 157

Nature and Regulation of Protein Folding on the Ribosome

Waudby, C. A., Dobson, C. M., & Christodoulou, J. (2019) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2019.06.008 · Cited by 147

Structural basis for client recognition and activity of Hsp40 chaperones

Jiang, Y., Rossi, P., & Kalodimos, C. G. (2019) · Science · doi:10.1126/science.aax1280 · Cited by 149

Gcn4-Mediator Specificity Is Mediated by a Large and Dynamic Fuzzy Protein-Protein Complex

Tuttle, L. M., Pacheco, D., Warfield, L., Luo, J., Ranish, J. A., Hahn, S., & Klevit, R. E. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.02.097 · Cited by 142

Recent applications of light scattering measurement in the biological and biopharmaceutical sciences

Minton, A. P. (2016) · Analytical Biochemistry · doi:10.1016/j.ab.2016.02.007 · Cited by 143

Structured States of Disordered Proteins from Genomic Sequences

Tóth-Petróczy, Á., Palmedo, P., Ingraham, J., Hopf, T. A., Berger, B., Sander, C., & Marks, D. S. (2016) · Cell · doi:10.1016/j.cell.2016.09.010 · Cited by 124

Substrate-binding domain conformational dynamics mediate Hsp70 allostery

Zhuravleva, A., & Gierasch, L. M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1506692112 · Cited by 124

Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space

Weinhäupl, K., Lindau, C., Hessel, A., Wang, Y., Schütze, C., Jores, T., Melchionda, L., Schönfisch, B., Kalbacher, H., Bersch, B., et al. (2018) · Cell · doi:10.1016/j.cell.2018.10.039 · Cited by 121

Forces Driving Chaperone Action

Koldewey, P., Stull, F. W., Horowitz, S. A., Martin, R., & Bardwell, J. C. A. (2016) · Cell · doi:10.1016/j.cell.2016.05.054 · Cited by 110

The Protein Disulfide Isomerase Family: from proteostasis to pathogenesis

Matsusaki, M., Kanemura, S., Kinoshita, M., Lee, Y., Inaba, K., & Okumura, M. (2019) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2019.04.003 · Cited by 111

ClpB N-terminal domain plays a regulatory role in protein disaggregation

Rosenzweig, R., Farber, P. J., Vėlyvis, A., Rennella, E., Latham, M. P., & Kay, L. E. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1512783112 · Cited by 109

Mimicking Molecular Chaperones to Regulate Protein Folding

Ma, F., Li, C., Liu, Y., & Shi, L. (2019) · Advanced Materials · doi:10.1002/adma.201805945 · Cited by 109

The Ribosome Cooperates with a Chaperone to Guide Multi-domain Protein Folding

Liu, K., Maciuba, K., & Kaiser, C. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.01.043 · Cited by 104

Chaperone Interactions at the RibosomePreprint

Deuerling, E., Gamerdinger, M., & Kreft, S. G. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033977 · Cited by 104

Local unfolding of the HSP27 monomer regulates chaperone activity

Alderson, T. R., Roche, J., Gastall, H. Y., Dias, D. M. G., Pritišanac, I., Ying, J., Bax, A., Benesch, J. L. P., & Baldwin, A. J. (2019) · Nature Communications · doi:10.1038/s41467-019-08557-8 · Cited by 103

Dynamic assembly of protein disulfide isomerase in catalysis of oxidative folding

Okumura, M., Noi, K., Kanemura, S., Kinoshita, M., Saio, T., Inoue, Y., Hikima, T., Akiyama, S., Ogura, T., & Inaba, K. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0268-8 · Cited by 102

The Dynamic SecYEG Translocon

Oswald, J., Njenga, R., Natriashvili, A., Sarmah, P., & Koch, H.-G. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.664241 · Cited by 88

Structures of Large Protein Complexes Determined by Nuclear Magnetic Resonance Spectroscopy

Huang, C., & Kalodimos, C. G. (2017) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-070816-033701 · Cited by 96

Mapping the conformation of a client protein through the Hsp70 functional cycle

Sekhar, A., Rosenzweig, R., Bouvignies, G., & Kay, L. E. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1508504112 · Cited by 95

Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles

Rosenzweig, R., Sekhar, A., Nagesh, J., & Kay, L. E. (2017) · eLife · doi:10.7554/elife.28030 · Cited by 94

Outer membrane protein folding from an energy landscape perspective

Schiffrin, B., Brockwell, D. J., & Radford, S. E. (2017) · BMC Biology · doi:10.1186/s12915-017-0464-5 · Cited by 89

Multitasking SecB chaperones in bacteria

Sala, A. J., Bordes, P., & Genevaux, P. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00666 · Cited by 89

Methyl groups as NMR probes for biomolecular interactions

Wiesner, S., & Sprangers, R. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.08.010 · Cited by 86

Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system

Xing, Q., Shi, K., Portaliou, A. G., Rossi, P., Economou, A., & Kalodimos, C. G. (2018) · Nature Communications · doi:10.1038/s41467-018-04137-4 · Cited by 85

Prolyl Isomerization and Its Catalysis in Protein Folding and Protein Function

Schmidpeter, P. A. M., & Schmid, F. X. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.01.023 · Cited by 85

Preprotein mature domains contain translocase targeting signals that are essential for secretion.

Chatzi, K. E., Sardis, M. F., Tsirigotaki, A., Koukaki, M., Šoštarić, N., Konijnenberg, A., Sobott, F., Kalodimos, C. G., Karamanou, S., & Economou, A. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201609022 · Cited by 72

NMR Studies of Large Proteins

Jiang, Y., & Kalodimos, C. G. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.07.007 · Cited by 76

Bacterial Signal Peptides- Navigating the Journey of Proteins

Kaushik, S., He, H., & Dalbey, R. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.933153 · Cited by 83

Trigger factor chaperone acts as a mechanical foldase

Haldar, S., Tapia‐Rojo, R., Eckels, E. C., Valle‐Orero, J., & Fernández, J. M. (2017) · Nature Communications · doi:10.1038/s41467-017-00771-6 · Cited by 74

Oligomerization of a molecular chaperone modulates its activity

Saio, T., Kawagoe, S., Ishimori, K., & Kalodimos, C. G. (2018) · eLife · doi:10.7554/elife.35731 · Cited by 73

Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients

Calabrese, A. N., Schiffrin, B., Watson, M. A., Karamanos, T. K., Walko, M., Humes, J. R., Horne, J. E., White, P. C., Wilson, A. J., Kalli, A. C., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15702-1 · Cited by 74

15N and 13C- SOFAST-HMQC editing enhances 3D-NOESY sensitivity in highly deuterated, selectively [1H,13C]-labeled proteins

Rossi, P., Xia, Y., Khanra, N., Veglia, G., & Kalodimos, C. G. (2016) · Journal of Biomolecular NMR · doi:10.1007/s10858-016-0074-5 · Cited by 67

A Review: Molecular Chaperone-mediated Folding, Unfolding and Disaggregation of Expressed Recombinant Proteins

Fatima, K., Naqvi, F., & Younas, H. (2021) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-021-00970-5 · Cited by 66

The Mechanical Power of Titin Folding

Eckels, E. C., Haldar, S., Tapia‐Rojo, R., Rivas‐Pardo, J. A., & Fernández, J. M. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.04.046 · Cited by 66

Atomic view of the energy landscape in the allosteric regulation of Abl kinase

Saleh, T., Rossi, P., & Kalodimos, C. G. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3470 · Cited by 67

Population-based heteropolymer design to mimic protein mixtures

Ruan, Z., Li, S., Grigoropoulos, A., Amiri, H., Hilburg, S. L., Chen, H., Jayapurna, I., Jiang, T., Gu, Z., Alexander-Katz, A., et al. (2023) · Nature · doi:10.1038/s41586-022-05675-0 · Cited by 64

Visualizing chaperone-assisted protein folding

Horowitz, S. A., Salmon, L., Koldewey, P., Ahlstrom, L. S., Martin, R., Quan, S., Afonine, P. V., van den Bedem, H., Wang, L., Xu, Q., et al. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3237 · Cited by 62

Non-chaperone Proteins Can Inhibit Aggregation and Cytotoxicity of Alzheimer Amyloid β Peptide

Luo, J., Wärmländer, S. K. T. S., Gräslund, A., & Abrahams, J. P. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.574947 · Cited by 60

Automatic Assignment of Methyl-NMR Spectra of Supramolecular Machines Using Graph Theory

Pritišanac, I., Degiacomi, M. T., Alderson, T. R., Carneiro, M. G., Eiso, A. B., Siegal, G., & Baldwin, A. J. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.6b11358 · Cited by 61

Protein folding by NMR

Zhuravleva, A., & Korzhnev, D. M. (2016) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/j.pnmrs.2016.10.002 · Cited by 60

Universal protein misfolding intermediates can bypass the proteostasis network and remain soluble and less functional

Nissley, D. A., Jiang, Y., Trovato, F., Sitarik, I. M., Narayan, K. B., To, P., Xia, Y., Fried, S. D., & O’Brien, E. P. (2022) · Nature Communications · doi:10.1038/s41467-022-30548-5 · Cited by 53

The dynamic dimer structure of the chaperone Trigger Factor

Morgado, L., Burmann, B. M., Sharpe, T., Mazur, A., & Hiller, S. (2017) · Nature Communications · doi:10.1038/s41467-017-02196-7 · Cited by 59

Structural characterization of the interaction of α-synuclein nascent chains with the ribosomal surface and trigger factor

Deckert, A., Waudby, C. A., Włodarski, T., Wentink, A. S., Wang, X., Kirkpatrick, J., Paton, J. F. S., Camilloni, C., Kukić, P., Dobson, C. M., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1519124113 · Cited by 58

Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking

Capdevila, D. A., Rondón, J. J., Edmonds, K. A., Rocchio, J. S., Dujovne, M. V., & Giedroc, D. P. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00264 · Cited by 64

Automatic methyl assignment in large proteins by the MAGIC algorithm

Monneau, Y. R., Rossi, P., Bhaumik, A., Huang, C., Jiang, Y., Saleh, T., Xie, T., Xing, Q., & Kalodimos, C. G. (2017) · Journal of Biomolecular NMR · doi:10.1007/s10858-017-0149-y · Cited by 56

Chaperone-Bound Clients: The Importance of Being Dynamic

Hiller, S. (2019) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.12.005 · Cited by 54

The interactions of molecular chaperones with client proteins: why are they so weak?

Arhar, T., Shkedi, A., Nadel, C. M., & Gestwicki, J. E. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101282 · Cited by 55

Synthetic Nanochaperones Facilitate Refolding of Denatured Proteins

Ma, F.-H., An, Y., Wang, J., Song, Y., Liu, Y., & Shi, L. (2017) · ACS Nano · doi:10.1021/acsnano.7b05947 · Cited by 55

The future of integrated structural biology

Schwalbe, H., Audergon, P. N. C. B., Haley, N., Amaro, C. A., Agirre, J., Baldus, M., Banci, L., Baumeister, W. P., Blackledge, M. J., Carazo, J. M., et al. (2024) · Structure · doi:10.1016/j.str.2024.08.014 · Cited by 57

Protein transport across the bacterial plasma membrane by the sec pathway.

Smets, D., Loos, M. S., Karamanou, S., & Economou, A. (2019) · The Protein Journal · doi:10.1007/s10930-019-09841-8 · Cited by 48

Dimeric Structure of the Bacterial Extracellular Foldase PrsA

Jakob, R. P., Koch, J. R., Burmann, B. M., Schmidpeter, P. A. M., Hunkeler, M., Hiller, S., Schmid, F. X., & Maier, T. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.622910 · Cited by 58

ATP-Independent Chaperones

Mitra, R., Wu, K., Lee, C. D., & Bardwell, J. C. A. (2022) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-090121-082906 · Cited by 50

Changes in conformational equilibria regulate the activity of the Dcp2 decapping enzyme

Wurm, J. P., Holdermann, I., Overbeck, J. H., Mayer, P., & Sprangers, R. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1704496114 · Cited by 52

Interactions between nascent proteins and the ribosome surface inhibit co-translational folding

Cassaignau, A. M. E., Włodarski, T., Chan, S. H. S., Woodburn, L. F., Bukvin, I. V., Streit, J. O., Cabrita, L. D., Waudby, C. A., & Christodoulou, J. (2021) · Nature Chemistry · doi:10.1038/s41557-021-00796-x · Cited by 48

Trigger factor both holds and folds its client proteins

Wu, K., Minshull, T. C., Radford, S. E., Calabrese, A. N., & Bardwell, J. C. A. (2022) · Nature Communications · doi:10.1038/s41467-022-31767-6 · Cited by 50

Long-Lived Folding Intermediates Predominate the Targeting-Competent Secretome.

Tsirigotaki, A., Chatzi, K., Koukaki, M., Geyter, J. D., Portaliou, A. G., Orfanoudaki, G., Sardis, M., Trelle, M. B., Jørgensen, T., Karamanou, S., et al. (2018) · Structure · doi:10.1016/j.str.2018.03.006 · Cited by 44

Terminal Regions Confer Plasticity to the Tetrameric Assembly of Human HspB2 and HspB3

Clark, A. R., Egberts, W. V., Kondrat, F. D. L., Hilton, G. R., Ray, N. J., Cole, A. R., Carver, J. A., Benesch, J. L. P., Keep, N. H., Boelens, W. C., et al. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.06.047 · Cited by 44

SurA is a cryptically grooved chaperone that expands unfolded outer membrane proteins

Marx, D. C., Plummer, A. M., Faustino, A. M., Devlin, T., Roskopf, M. A., Leblanc, M. J., Lessen, H. J., Amann, B. T., Fleming, P. J., Krueger, S., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2008175117 · Cited by 43

C9orf72-derived arginine-rich poly-dipeptides impede phase modifiers

Nanaura, H., Kawamukai, H., Fujiwara, A., Uehara, T., Aiba, Y., Nakanishi, M., Shiota, T., Hibino, M., Wiriyasermkul, P., Kikuchi, S., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25560-0 · Cited by 43

Protein Folding Mediated by Trigger Factor and Hsp70: New Insights from Single-Molecule Approaches

Wruck, F., Avellaneda, M. J., Koers, E. J., Minde, D., Mayer, M. P., Krämer, G., Mashaghi, A., & Tans, S. J. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.09.004 · Cited by 41

Structural basis of client specificity in mitochondrial membrane-protein chaperones

Sučec, I., Wang, Y., Dakhlaoui, O., Weinhäupl, K., Jores, T., Costa, D., Hessel, A., Brennich, M., Rapaport, D., Lindorff‐Larsen, K., et al. (2020) · Science Advances · doi:10.1126/sciadv.abd0263 · Cited by 42

Chaperones and chaperone–substrate complexes: Dynamic playgrounds for NMR spectroscopists

Burmann, B. M., & Hiller, S. (2015) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/j.pnmrs.2015.02.004 · Cited by 40

The Activity of Escherichia coli Chaperone SurA Is Regulated by Conformational Changes Involving a Parvulin Domain

Soltes, G. R., Schwalm, J., Ricci, D. P., & Silhavy, T. J. (2016) · Journal of Bacteriology · doi:10.1128/jb.00889-15 · Cited by 42

Recent advances in measuring the kinetics of biomolecules by NMR relaxation dispersion spectroscopy

Ban, D., Smith, C. A., de Groot, B. L., Griesinger, C., & Lee, D. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2017.05.016 · Cited by 42

Dual Role of Ribosome-Binding Domain of NAC as a Potent Suppressor of Protein Aggregation and Aging-Related Proteinopathies

Shen, K., Gamerdinger, M., Chan, R., Gense, K., Martin, E. M., Sachs, N., Knight, P., Schlömer, R., Calabrese, A. N., Stewart, K. L., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.03.012 · Cited by 41

PDI Family Members as Guides for Client Folding and Assembly

Kanemura, S., Matsusaki, M., Inaba, K., & Okumura, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249351 · Cited by 41

Trigger factor is a bona fide secretory pathway chaperone that interacts with SecB and the translocase.

De Geyter, J., Portaliou, A. G., Srinivasu, B., Krishnamurthy, S., Economou, A., & Karamanou, S. (2020) · The EMBO Reports · doi:10.15252/embr.201949054 · Cited by 40

Dynamic Behavior of Trigger Factor on the Ribosome

Deeng, J., Chan, K., van der Sluis, E. O., Berninghausen, O., Han, W., Gumbart, J. C., Schulten, K. J., Beatrix, B., & Beckmann, R. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.06.007 · Cited by 40

Selective promiscuity in the binding of E. coli Hsp70 to an unfolded protein

Clérico, E. M., Pozhidaeva, A., Jansen, R. M., Özden, C., Tilitsky, J. M., & Gierasch, L. M. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2016962118 · Cited by 38

FKBPs in bacterial infections

Ünal, C., & Steinert, M. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.12.018 · Cited by 37

Reciprocal Molecular Interactions between the Aβ Peptide Linked to Alzheimer’s Disease and Insulin Linked to Diabetes Mellitus Type II

Luo, J., Wärmländer, S. K. T. S., Gräslund, A., & Abrahams, J. P. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00325 · Cited by 39

Mechanisms of Cotranslational Protein Maturation in Bacteria

Koubek, J., Schmitt, J. L., Galmozzi, C. V., & Krämer, G. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.689755 · Cited by 35

Ligand-driven conformational changes of MurD visualized by paramagnetic NMR

Saio, T., Ogura, K., Kumeta, H., Kobashigawa, Y., Shimizu, K., Yokochi, M., Kodama, K., Yamaguchi, H. Q., Tsujishita, H., & Inagaki, F. (2015) · Scientific Reports · doi:10.1038/srep16685 · Cited by 38

Resolving chaperone-assisted protein folding on the ribosome at the peptide level

Wales, T. E., Pajak, A., Roeselová, A., Shivakumaraswamy, S., Howell, S. A., Kjær, S., Hartl, F. U., Engen, J. R., & Balchin, D. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01355-x · Cited by 38

Substrate Interaction Networks of the Escherichia coli Chaperones: Trigger Factor, DnaK and GroEL

Bhandari, V., & Houry, W. A. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-23603-2_15 · Cited by 35

Isotope-labeling strategies for solution NMR studies of macromolecular assemblies

Zhang, H., & van Ingen, H. (2016) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.05.008 · Cited by 37

Solution NMR Spectroscopy Provides an Avenue for the Study of Functionally Dynamic Molecular Machines: The Example of Protein Disaggregation

Rosenzweig, R., & Kay, L. E. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b11346 · Cited by 35

Facilitating unambiguous NMR assignments and enabling higher probe density through selective labeling of all methyl containing amino acids

Proudfoot, A., Frank, A. O., Ruggiu, F., Mamo, M., & Lingel, A. (2016) · Journal of Biomolecular NMR · doi:10.1007/s10858-016-0032-2 · Cited by 36

Solution NMR views of dynamical ordering of biomacromolecules

Ikeya, T., Ban, D., Lee, D., Ito, Y., Kato, K., & Griesinger, C. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.08.020 · Cited by 37

Investigation on the conformational changes of bovine serum albumin in a wide pH range from 2 to 12

Chi, Z., Hong, B., Ren, X., Cheng, K., Lu, Y., & Liu, X. (2018) · Spectroscopy Letters · doi:10.1080/00387010.2018.1471092 · Cited by 36

Mechanism of chaperone coordination during cotranslational protein folding in bacteria

Roeselová, A., Maslen, S., Shivakumaraswamy, S., Pellowe, G. A., Howell, S. A., Joshi, D., Redmond, J. M., Kjær, S., Skehel, M. J., & Balchin, D. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.06.002 · Cited by 35

Detection of intermolecular NOE interactions in large protein complexes

Anglister, J., Srivastava, G., & Naider, F. R. (2016) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/j.pnmrs.2016.08.002 · Cited by 35

Recognition and targeting mechanisms by chaperones in flagellum assembly and operation

Khanra, N., Rossi, P., Economou, A., & Kalodimos, C. G. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1607845113 · Cited by 34

Simulation of Complex Biomolecular Systems: The Ribosome Challenge

Bock, L. V., Gabrielli, S., Kolář, M. H., & Grubmüller, H. (2023) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-111622-091147 · Cited by 34

Thermosensitive PBP2a requires extracellular folding factors PrsA and HtrA1 for Staphylococcus aureus MRSA β-lactam resistance

Roch, M., Lelong, E., Panasenko, O. O., Sierra, R., Renzoni, A., & Kelley, W. L. (2019) · Communications Biology · doi:10.1038/s42003-019-0667-0 · Cited by 32

Protein folding in vitro and in the cell: From a solitary journey to a team effort

Mecha, M. F., Hutchinson, R. B., Lee, J. H., & Cavagnero, S. (2022) · Biophysical Chemistry · doi:10.1016/j.bpc.2022.106821 · Cited by 33

The Trigger Factor Chaperone Encapsulates and Stabilizes Partial Folds of Substrate Proteins

Singhal, K., Vreede, J., Mashaghi, A., Tans, S. J., & Bolhuis, P. G. (2015) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1004444 · Cited by 32

Assessing Site-Specific Enhancements Imparted by Hyperpolarized Water in Folded and Unfolded Proteins by 2D HMQC NMR

Szekely, O., Olsen, G. L., Novakovic, M., Rosenzweig, R., & Frydman, L. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c00807 · Cited by 32

RESEARCH ARTICLE The Trigger Factor Chaperone Encapsulates and Stabilizes Partial Folds of Substrate Proteins

Singhal, K., Vreede, J., Mashaghi, A., & Tans, E. J. (2016)

The Trigger Factor Chaperone Encapsulates and Stabilizes Partial Folds of Substrate Proteins

Singhal, K., Vreede, J., Mashaghi, A., Tans, S. J., & Bolhuis, P. G. (2015) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1004444 · Cited by 32

A Molecular Dynamics Study of the Flexibility and Protein-Binding of the Trigger Factor Chaperone in Solution

Singhal, K., Vreede, J., Mashaghi, A., Tans, S. J., & Bolhuis, P. G. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2012.11.3172

Oligomerization of a molecular chaperone modulates its activity

Saio, T., Kawagoe, S., Ishimori, K., & Kalodimos, C. G. (2018) · eLife · doi:10.7554/elife.35731 · Cited by 73

Exploring the roles of substrate‐binding surface of the chaperone site in the chaperone activity of trigger factor

Fan, D., Cao, S., Zhou, Q., Zhang, Y., Yue, L., Han, C. L., Yang, B., Wang, Y., Ma, Z., Zhu, L., et al. (2018) · The FASEB Journal · doi:10.1096/fj.201701576 · Cited by 2