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

Information processing in the CNS: a supramolecular chemistry?

Tozzi, A. (2015) · Cognitive Neurodynamics · doi:10.1007/s11571-015-9337-1 · Cited by 32

Exploiting E. coli auxotrophs for leucine, valine, and threonine specific methyl labeling of large proteins for NMR applications

Monneau, Y. R., Ishida, Y., Rossi, P., Saio, T., Tzeng, S., Inouye, M., & Kalodimos, C. G. (2016) · Journal of Biomolecular NMR · doi:10.1007/s10858-016-0041-1 · Cited by 31

Capturing a Dynamic Chaperone–Substrate Interaction Using NMR-Informed Molecular Modeling

Salmon, L., Ahlstrom, L. S., Horowitz, S. A., Dickson, A., Brooks, C. L., & Bardwell, J. C. A. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b02382 · Cited by 31

Co-translational binding of importins to nascent proteins

Seidel, M., Romanov, N., Obarska-Kosińska, A., Becker, A., de Azevedo, N. T. D., Provaznik, J., Nagaraja, S. R., Landry, J. J. M., Beneš, V., & Beck, M. (2023) · Nature Communications · doi:10.1038/s41467-023-39150-9 · Cited by 27

Methyl group reorientation under ligand binding probed by pseudocontact shifts

Lescanne, M., Ahuja, P., Blok, A. J., Timmer, M., Åkerud, T., & Ubbink, M. (2018) · Journal of Biomolecular NMR · doi:10.1007/s10858-018-0190-5 · Cited by 29

Regulation of chaperone function by coupled folding and oligomerization

Mas, G., Burmann, B. M., Sharpe, T., Claudi, B., Bumann, D., & Hiller, S. (2020) · Science Advances · doi:10.1126/sciadv.abc5822 · Cited by 29

Visualization of structural dynamics of protein disulfide isomerase enzymes in catalysis of oxidative folding and reductive unfolding

Okumura, M., Noi, K., & Inaba, K. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.10.004 · Cited by 29

Intrinsic structural dynamics dictate enzymatic activity and inhibition

Shukla, V. K., Siemons, L., & Hansen, D. F. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2310910120 · Cited by 25

The chaperone toolbox at the single‐molecule level: From clamping to confining

Avellaneda, M. J., Koers, E. J., Naqvi, M. M., & Tans, S. J. (2017) · Protein Science · doi:10.1002/pro.3161 · Cited by 29

Conformational flexibility within the nascent polypeptide–associated complex enables its interactions with structurally diverse client proteins

Martin, E. M., Jackson, M. P., Gamerdinger, M., Gense, K., Karamanos, T. K., Humes, J. R., Deuerling, E., Ashcroft, A. E., & Radford, S. E. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.001568 · Cited by 27

Cryo-EM Structures Reveal Relocalization of MetAP in the Presence of Other Protein Biogenesis Factors at the Ribosomal Tunnel Exit

Bhakta, S., Akbar, S., Sengupta, J., & Sengupta, J. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.02.002 · Cited by 28

A network of cytosolic (co)chaperones promotes the biogenesis of mitochondrial signal-anchored outer membrane proteins

Drwesh, L., Heim, B., Graf, M., Kehr, L., Hansen-Palmus, L., Franz‐Wachtel, M., Maček, B., Kalbacher, H., Büchner, J., & Rapaport, D. (2022) · eLife · doi:10.7554/elife.77706 · Cited by 28

The Role of Plastidic Trigger Factor Serving Protein Biogenesis in Green Algae and Land Plants

Rohr, M., Ries, F., Herkt, C., Gotsmann, V. L., Westrich, L. D., Gries, K., Trösch, R., Christmann, J., Chaux, F., Jung, M., et al. (2019) · PLANT PHYSIOLOGY · doi:10.1104/pp.18.01252 · Cited by 27

Structural insight into proline cis/trans isomerization of unfolded proteins catalyzed by the trigger factor chaperone

Kawagoe, S., Nakagawa, H., Kumeta, H., Ishimori, K., & Saio, T. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003579 · Cited by 27

Involvement of PpiD in Sec-dependent protein translocation.

Fürst, M., Zhou, Y., Merfort, J., & Müller, M. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.10.012 · Cited by 26

Structural Basis of the Subcellular Topology Landscape of Escherichia coli

Loos, M. S., Ramakrishnan, R., Vranken, W., Tsirigotaki, A., Tsare, E.-P., Zorzini, V., Geyter, J. D., Yuan, B., Tsamardinos, I., Klapa, M. I., et al. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.01670 · Cited by 23

Co-Translational Protein Folding and Sorting in Chloroplasts

Ries, F., Herkt, C., & Willmund, F. (2020) · Plants · doi:10.3390/plants9020214 · Cited by 25

How do Chaperones Bind (Partly) Unfolded Client Proteins?

Sučec, I., Bersch, B., & Schanda, P. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.762005 · Cited by 27

The Rrp4–exosome complex recruits and channels substrate RNA by a unique mechanism

Cvetkovic, M. A., Wurm, J. P., Audin, M., Schütz, S., & Sprangers, R. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2328 · Cited by 26

Preprotein Conformational Dynamics Drive Bivalent Translocase Docking and Secretion

Sardis, M. F., Tsirigotaki, A., Chatzi, K. E., Portaliou, A. G., Gouridis, G., Spyridoula Karamanou, A., & Economou, A. (2017) · Structure · doi:10.1016/j.str.2017.05.012 · Cited by 25

The dynamic triage interplay of Hsp90 with its chaperone cycle and client binding

Qu, X., Wang, S., Zhao, S., Wan, C., Xu, W., & Huang, C. (2024) · Nature Communications · doi:10.1038/s41467-024-55026-y · Cited by 24

Redefining Molecular Chaperones as Chaotropes

Macošek, J., Mas, G., & Hiller, S. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.683132 · Cited by 24

Reversible Interactions of Proteins with Mixed Shell Polymeric Micelles: Tuning the Surface Hydrophobic/Hydrophilic Balance toward Efficient Artificial Chaperones

Wang, J., Song, Y., Sun, P., An, Y., Zhang, Z., & Shi, L. (2016) · Langmuir · doi:10.1021/acs.langmuir.6b00356 · Cited by 25

Structural and molecular comparison of bacterial and eukaryotic trigger factors

Ries, F., Carius, Y., Rohr, M., Gries, K., Keller, S., Lancaster, C. R. D., & Willmund, F. (2017) · Scientific Reports · doi:10.1038/s41598-017-10625-2 · Cited by 25

Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex

Rizzolo, K., Yu, A. Y. H., Ologbenla, A., Kim, S. R., Zhu, H., Ishimori, K., Thibault, G., Leung, E., Zhang, Y. W., Teng, M., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-20553-x · Cited by 21

A Balance Between Capture and Release: How Nanochaperones Regulate Refolding of Thermally Denatured Proteins

Ma, F., Wu, X., Li, A., Xu, L., An, Y., & Shi, L. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202101462 · Cited by 24

Sequence features governing aggregation or degradation of prion-like proteins

Cascarina, S. M., Paul, K. R., Machihara, S., & Ross, E. D. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007517 · Cited by 22

Toolkit for NMR Studies of Methyl-Labeled Proteins

Rossi, P., Monneau, Y. R., Xia, Y., Ishida, Y., & Kalodimos, C. G. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.08.036 · Cited by 22

Molecular insights into the interaction of Hsp90 with allosteric inhibitors targeting the C-terminal domain

Vasantha Kumar, M. V., Noor, R. E., Davis, R. E., Zhang, Z., Sipavicius, E., Keramisanou, D., Blagg, B. S. J., & Gelis, I. (2018) · MedChemComm · doi:10.1039/c8md00151k · Cited by 21

Molecular modeling of apoE in complexes with Alzheimer’s amyloid-β fibrils from human brain suggests a structural basis for apolipoprotein co-deposition with amyloids

Lewkowicz, E., Nakamura, M. N., Rynkiewicz, M. J., & Gursky, O. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-05026-w · Cited by 21

Assigning methyl resonances for protein solution-state NMR studies

Gorman, S. D., Sahu, D., O’Rourke, K. F., & Boehr, D. D. (2018) · Methods · doi:10.1016/j.ymeth.2018.06.010 · Cited by 21

Structural Basis for the Inhibition of the Autophosphorylation Activity of HK853 by Luteolin

Zhou, Y., Huang, L., Ji, S., Shi, H., Luo, L., Li, C., Liu, M., Liu, Y., & Jiang, L. (2019) · Molecules · doi:10.3390/molecules24050933 · Cited by 21

Simultaneous sensing and imaging of individual biomolecular complexes enabled by modular DNA–protein coupling

Avellaneda, M. J., Koers, E. J., Minde, D., Šunderlíková, V., & Tans, S. J. (2020) · Communications Chemistry · doi:10.1038/s42004-020-0267-4 · Cited by 21

Chaperone–client complexes: A dynamic liaison

Hiller, S., & Burmann, B. M. (2018) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2017.12.008 · Cited by 21

Hsp104 N‐terminal domain interaction with substrates plays a regulatory role in protein disaggregation

Harari, A., Zoltsman, G., Levin, T., & Rosenzweig, R. (2022) · FEBS Journal · doi:10.1111/febs.16441 · Cited by 20

Secretome Dynamics in a Gram-Positive Bacterial Model

Tsolis, K. C., Hamed, M. B., Simoens, K., Koepff, J., Busche, T., Rückert, C., Oldiges, M., Kalinowski, J., Anné, J., Kormanec, J., et al. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra118.000899 · Cited by 19

Frustrated Interfaces Facilitate Dynamic Interactions between Native Client Proteins and Holdase Chaperones

He, L., & Hiller, S. (2019) · ChemBioChem · doi:10.1002/cbic.201900215 · Cited by 18

Large Chaperone Complexes Through the Lens of Nuclear Magnetic Resonance Spectroscopy

Karamanos, T. K., & Clore, G. M. (2022) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-090921-120150 · Cited by 20

The Principles of Protein Targeting and Transport Across Cell Membranes

Chen, Y., Shanmugam, S. K., & Dalbey, R. (2019) · The Protein Journal · doi:10.1007/s10930-019-09847-2 · Cited by 19

Structural basis for the dynamic chaperoning of disordered clients by Hsp90

Qu, X., Zhao, S., Wan, C., Zhu, L., Ji, T., Rossi, P., Wang, J., Kalodimos, C. G., Wang, C., Xu, W., et al. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01337-z · Cited by 20

HdeB chaperone activity is coupled to its intrinsic dynamic properties

Ding, J., Yang, C., Niu, X., Hu, Y., & Jin, C. (2015) · Scientific Reports · doi:10.1038/srep16856 · Cited by 19

E. coli metabolic protein aldehyde-alcohol dehydrogenase-E binds to the ribosome: a unique moonlighting action revealed

Shasmal, M., Dey, S., Shaikh, T. R., Bhakta, S., & Sengupta, J. (2016) · Scientific Reports · doi:10.1038/srep19936 · Cited by 18

Precursor-Based Selective Methyl Labeling of Cell-Free Synthesized Proteins

Lazarova, M., Löhr, F., Rues, R.-B., Kleebach, R., Dötsch, V., & Bernhard, F. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00338 · Cited by 18

Assignment of methyl NMR resonances of a 52 kDa protein with residue-specific 4D correlation maps

Mishra, S. H., & Frueh, D. P. (2015) · Journal of Biomolecular NMR · doi:10.1007/s10858-015-9943-6 · Cited by 18

Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone

Yu, X.-C., Hu, Y., Ding, J., Li, H., & Jin, C. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006398 · Cited by 18

Bioactive Assembly Cofactor-Assisted Ursolic Acid Helix for Enhanced Anticancer Efficacy via In Situ Virus-like Transition

Lin, M., Liu, D., Gong, Y., Shu, L., Wang, H., Zhang, G., Li, J., Gao, Z., Sun, J., & Chen, X. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c01214 · Cited by 17

Extending the Applicability of Exact Nuclear Overhauser Enhancements to Large Proteins and RNA

Nichols, P. J., Born, A., Henen, M. A., Strotz, D., Celestine, N., Güntert, P., & Vögeli, B. (2018) · ChemBioChem · doi:10.1002/cbic.201800237 · Cited by 17

Navigating the complexities of multi-domain protein folding

Rajasekaran, N., & Kaiser, C. (2024) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2024.102790 · Cited by 17

Current Understanding of Protein Aggregation in Neurodegenerative Diseases

Hu, C., Lin, M., Wang, C., & Zhang, S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262110568 · Cited by 21

The Hsp90 Cochaperones Cpr6, Cpr7, and Cns1 Interact with the Intact Ribosome

Tenge, V. R., Zuehlke, A. D., Shrestha, N., & Johnson, J. L. (2014) · Eukaryotic Cell · doi:10.1128/ec.00170-14 · Cited by 16

Analysis of Translocation-Competent Secretory Proteins by HDX-MS

Tsirigotaki, A., Papanastasiou, M., Trelle, M. B., Jørgensen, T. J. D., & Economou, A. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.09.028 · Cited by 16

Monitoring Protein Secretion in Streptomyces Using Fluorescent Proteins

Hamed, M. B., Vrancken, K., Bilyk, B. L., Koepff, J., Nováková, R., Mellaert, L. V., Oldiges, M., Luzhetskyy, A. N., Kormanec, J., Anné, J., et al. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.03019 · Cited by 16

Structural insights into the interplay of protein biogenesis factors with the 70S ribosome

Akbar, S., Bhakta, S., & Sengupta, J. (2021) · Structure · doi:10.1016/j.str.2021.03.005 · Cited by 15

Thermodynamics of co-translational folding and ribosome–nascent chain interactions

Waudby, C. A., Burridge, C., Cabrita, L. D., & Christodoulou, J. C. (2022) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2022.102357 · Cited by 15

Enzymatic and synthetic regulation of polypeptide folding

Muraoka, T., Okumura, M., & Saio, T. (2024) · Chemical Science · doi:10.1039/d3sc05781j · Cited by 15

Proteome-wide determinants of co-translational chaperone binding in bacteria

Galmozzi, C. V., Tippmann, F., Wruck, F., Auburger, J. J., Kats, I., Günnigmann, M., Till, K., O’Brien, E. P., Tans, S. J., Krämer, G., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59067-9 · Cited by 15

Structural Dynamics of the Functional Nonameric Type III Translocase Export Gate

Yuan, B., Portaliou, A. G., Parakra, R., Smit, J. H., Wald, J., Li, Y., Srinivasu, B. Y., Loos, M. S., Dhupar, H. S., Fahrenkamp, D., et al. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167188 · Cited by 14

Molecular Characterization of an Intrinsically Disordered Chaperone Reveals Net-Charge Regulation in Chaperone Action

Ren, C., Zheng, Y., Liu, C., Mencius, J., Wu, Z., & Quan, S. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167405 · Cited by 14

Update on the Protein Homeostasis Network in Bacillus subtilis

Matavacas, J., & von Wachenfeldt, C. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.865141 · Cited by 16

Identification of an endoplasmic reticulum proteostasis modulator that enhances insulin production in pancreatic β cells

Miyake, M., Sobajima, M., Kurahashi, K., Shigenaga, A., Denda, M., Otaka, A., Saio, T., Sakane, N., Kosako, H., & Oyadomari, S. (2022) · Cell chemical biology · doi:10.1016/j.chembiol.2022.01.002 · Cited by 12

Evolutionary adaptation of the protein folding pathway for secretability

Smets, D., Tsirigotaki, A., Smit, J. H., Krishnamurthy, S., Portaliou, A. G., Vorobieva, A. A., Vranken, W., Karamanou, S., & Economou, A. (2022) · The EMBO Journal · doi:10.15252/embj.2022111344 · Cited by 14

NMR Lineshape Analysis of Intrinsically Disordered Protein Interactions

Waudby, C. A., & Christodoulou, J. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0524-0_24 · Cited by 14

F 1 F 2-selective NMR spectroscopy

Walinda, E., Morimoto, D., Shirakawa, M., & Sugase, K. (2017) · Journal of Biomolecular NMR · doi:10.1007/s10858-017-0113-x · Cited by 13

Redox-active chemical chaperones exhibiting promiscuous binding promote oxidative protein folding under condensed sub-millimolar conditions

Suzuki, K., Nojiri, R., Matsusaki, M., Mabuchi, T., Kanemura, S., Ishii, K., Kumeta, H., Okumura, M., Saio, T., & Muraoka, T. (2024) · Chemical Science · doi:10.1039/d4sc02123a · Cited by 12

Ca2+-driven PDIA6 biomolecular condensation ensures proinsulin folding

Lee, Y., Saio, T., Watabe, M., Matsusaki, M., Kanemura, S., Lin, Y., Mannen, T., Kuramochi, T., Kamada, Y., Iuchi, K., et al. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01794-8 · Cited by 12

Signal Peptide-rheostat Dynamics Delay Secretory Preprotein Folding

Smets, D., Smit, J. H., Xu, Y., Spyridoula Karamanou, A., & Economou, A. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167790 · Cited by 12

Selective Methyl Labeling of Proteins: Enabling Structural and Mechanistic Studies As Well As Drug Discovery Applications by Solution-State NMR

Proudfoot, A., Frank, A. O., Frommlet, A., & Lingel, A. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.08.035 · Cited by 12

Cotranslational folding of alkaline phosphatase in the periplasm of Escherichia coli

Elfageih, R., Karyolaimos, A., Kemp, G., Gier, J. D., von HEIJNE, G., & Kudva, R. (2020) · Protein Science · doi:10.1002/pro.3927 · Cited by 12

Conformational Dynamics of the Periplasmic Chaperone SurA

Jia, M., Wu, B., Yang, W., Chen, C., Zhao, M., Hou, X., Niu, X., Jin, C., & Hu, Y. (2020) · Biochemistry · doi:10.1021/acs.biochem.0c00507 · Cited by 12

NMR in structure-based drug design

Carneiro, M. G., Eiso, A. B., Theisgen, S., & Siegal, G. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170037 · Cited by 12

Isolation and characterization of a 17-kDa FKBP-type peptidyl-prolyl cis/trans isomerase from Vibrio anguillarum

Jo, G.-A., Lee, J. M., No, G., Kang, D. S., Kim, S., Ahn, S. H., & Kong, I. (2015) · Protein Expression and Purification · doi:10.1016/j.pep.2015.02.019 · Cited by 11

Bayesian reweighting of biomolecular structural ensembles using heterogeneous cryo-EM maps with the cryoENsemble method

Włodarski, T., Streit, J. O., Mitropoulou, A. N., Cabrita, L. D., Vendruscolo, M., & Christodoulou, J. (2024) · Scientific Reports · doi:10.1038/s41598-024-68468-7 · Cited by 14

Mechanisms of assembly and function of the Hsp70-Hsp40 chaperone machinery

Jiang, Y., Ibrahim, Z., Xia, Y., Clay, M. C., Myasnikov, A. G., Immadisetty, K., Xia, Z., Tang, L., Rossi, P., Ganguly, P., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.09.023 · Cited by 10

Efficient production of 2H, 13C, 15N-enriched industrial enzyme Rhizopus chinensis lipase with native disulfide bonds

Zhang, M., Yu, X., Swapna, G. V. T., Xiao, R., Zheng, H., Sha, C., Xu, Y., & Montelione, G. T. (2016) · Microbial Cell Factories · doi:10.1186/s12934-016-0522-7 · Cited by 10

Conformational dynamics of bacterial trigger factor in apo and ribosome-bound states

Can, M. T., Kurkcuoglu, Z., Ezeroglu, G., Uyar, A., Kürkçüoğlu, Ö., & Doruker, P. (2017) · PLoS ONE · doi:10.1371/journal.pone.0176262 · Cited by 10

NMR assignments of the peptidyl-prolyl cis–trans isomerase domain of trigger factor from E. coli

Huang, C., & Hsu, S. D. (2015) · Biomolecular NMR Assignments · doi:10.1007/s12104-015-9655-6 · Cited by 9

Activation dynamics of ubiquitin-specific protease 7

Valles, G. J., Korchak, E. J., Geddes-Buehre, D. H., Jaiswal, N., Korzhnev, D. M., & Bezsonova, I. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2426632122 · Cited by 9

Structural and Kinetic Views of Molecular Chaperones in Multidomain Protein Folding

Kawagoe, S., Ishimori, K., & Saio, T. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052485 · Cited by 9

Trigger Factor Flexibility

Gamerdinger, M., & Deuerling, E. (2014) · Science · doi:10.1126/science.1254064 · Cited by 9

Progress toward automated methyl assignments for methyl-TROSY applications

Clay, M. C., Saleh, T., Kamatham, S., Rossi, P., & Kalodimos, C. G. (2022) · Structure · doi:10.1016/j.str.2021.11.009 · Cited by 9

Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity

Hu, H., Wang, Q., Du, J., Liu, Z., Ding, Y., Xue, H., Zhou, C., Feng, L., & Zhang, N. (2021) · Molecules · doi:10.3390/molecules26071943 · Cited by 8

Molecular chaperones and their denaturing effect on client proteins

Hiller, S. (2020) · Journal of Biomolecular NMR · doi:10.1007/s10858-020-00353-7 · Cited by 8

Structural and functional aspects of the interaction partners of the small heat-shock protein in Synechocystis

Marklund, E. G., Zhang, Y., Basha, E., Benesch, J. L. P., & Vierling, E. (2018) · Cell Stress and Chaperones · doi:10.1007/s12192-018-0884-3 · Cited by 8

Methyl NMR spectroscopy: Measurement of dynamics in viral RNA-directed RNA polymerases

Alphonse, S., & Ghose, R. (2018) · Methods · doi:10.1016/j.ymeth.2018.05.021 · Cited by 8

Bio-inspired multiscale design for perovskite solar cells

Duan, T., Guo, P., Feldmann, S., Sutter‐Fella, C. M., & Zhou, Y. (2025) · Nature Reviews Clean Technology · doi:10.1038/s44359-025-00086-6 · Cited by 7

Trigger factor accelerates nascent chain compaction and folding

Till, K., Seinen, A., Wruck, F., Šunderlíková, V., Galmozzi, C. V., Katranidis, A., Bukau, B., Krämer, G., & Tans, S. J. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2422678122 · Cited by 7

Bacillus subtilis forms twisted cells with cell wall integrity defects upon removal of the molecular chaperones DnaK and trigger factor

Matavacas, J., Hällgren, J., & von Wachenfeldt, C. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.988768 · Cited by 6

Structural analysis of extracellular ATP-independent chaperones of streptococcal species and protein substrate interactions

Agbavor, C., Torres, M., Inniss, N. L., Latimer, S., Minasov, G., Shuvalova, L., Wawrzak, Z., Borek, D., Otwinowski, Z., Stogios, P. J., et al. (2025) · mSphere · doi:10.1128/msphere.01078-24 · Cited by 7

Global Analysis of the Impact of Deleting Trigger Factor on the Transcriptome Profile of Escherichia coli

Fan, D., Liu, L.-S., Zhu, L., Peng, F., Zhou, Q., & Liu, C. (2016) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25620 · Cited by 7

Hydrophobic residues of melittin mediate its binding to αA−crystallin

Ramirez, L. M., Shekhtman, A. G., & Pande, J. (2019) · Protein Science · doi:10.1002/pro.3792 · Cited by 7

Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding

Matsusaki, M., Okada, R., Tanikawa, Y., Kanemura, S., Ito, D., Lin, Y., Watabe, M., Yamaguchi, H., Saio, T., Lee, Y., et al. (2021) · Biology · doi:10.3390/biology10111112 · Cited by 7

SAXS Data Based Global Shape Analysis of Trigger Factor (TF) Proteins from E. coli, V. cholerae, and P. frigidicola: Resolving the Debate on the Nature of Monomeric and Dimeric Forms

Rathore, Y. S., Dhoke, R. R., Badmalia, M. D., Sagar, A., & Ashish (2015) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5b00759 · Cited by 7

Sandwiched‐fusion strategy facilitates recombinant production of small labile proteins

Huang, L., Qu, X., Chen, Y., Xu, W., & Huang, C. (2021) · Protein Science · doi:10.1002/pro.4024 · Cited by 6

Rotational restriction of nascent peptides as an essential element of co-translational protein folding: possible molecular players and structural consequences

Sorokina, I., & Mushegian, A. R. (2017) · Biology Direct · doi:10.1186/s13062-017-0186-1 · Cited by 7

Ligand Binding Site Structure Shapes Folding, Assembly and Degradation of Homomeric Protein Complexes

Abrusán, G., & Marsh, J. A. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.07.014 · Cited by 7

UNC-45 assisted myosin folding depends on a conserved FX3HY motif implicated in Freeman Sheldon Syndrome

Vogel, A., Arnese, R., Carrillo, R. M. G., Sehr, D., Deszcz, L., Bylicki, A., Meinhart, A., & Clausen, T. (2024) · Nature Communications · doi:10.1038/s41467-024-50442-6 · Cited by 6

Fundamentals of spectroscopy for biomolecular structure and dynamics

Nag, N., Sasidharan, S., Saudagar, P., & Tripathi, T. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-99127-8.00002-7 · Cited by 6

Confirmation for conformational selection

Jiang, Y., & Kalodimos, C. G. (2018) · eLife · doi:10.7554/elife.34923 · Cited by 6

Protein and RNA chaperones

Sahoo, B. R., & Bardwell, J. C. A. (2025) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2025.101384 · Cited by 5

Utility of methyl side chain probes for solution NMR studies of large proteins

McShan, A. C. (2022) · Journal of Magnetic Resonance Open · doi:10.1016/j.jmro.2022.100087 · Cited by 5

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