Structure of a complex of the ATPase SecA and the protein-translocation channel.

[20] Processing of X-ray diffraction data collected in oscillation mode

Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475

The PyMOL Molecular Graphics System

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

The CCP4 suite: programs for protein crystallography

Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,317

Improved methods for building protein models in electron density maps and the location of errors in these models

Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,616

Automated MAD and MIR structure solution

Terwilliger, T. C., & Berendzen, J. (1999) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444999000839 · Cited by 3,032

Improved Fourier coefficients for maps using phases from partial structures with errors

Read, R. J. (1986) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767386099622 · Cited by 1,870

Likelihood-enhanced fast translation functions

McCoy, A. J., Grosse‐Kunstleve, R. W., Storoni, L. C., & Read, R. J. (2005) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444905001617 · Cited by 1,641

ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures

Landau, M., Mayrose, I., Rosenberg, Y., Glaser, F., Martz, E., Pupko, T., & Ben‐Tal, N. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki370 · Cited by 1,379

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

ConSurf: Identification of Functional Regions in Proteins by Surface-Mapping of Phylogenetic Information

Glaser, F., Pupko, T., Paz, I., Bell, R. E., Shental-Bechor, D., Martz, E., & Ben‐Tal, N. (2002) · Bioinformatics · doi:10.1093/bioinformatics/19.1.163 · Cited by 1,237

Fluorescent Biomarkers for Membrane Separation

Winther, A. R. (2015) · NORA - Norwegian Open Research Archives

Yeast Mitochondria as a Model System to Study the Biogenesis of Bacterial β-Barrel Proteins

Ulrich, T., Oberhettinger, P., Autenrieth, I. B., & Rapaport, D. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2871-2_2

Membrane Protein Biogenesis and Assembly at the Endoplasmic Reticulum Membrane

Bhanu, M. K., & Kendall, D. A. (2011) · CRC Press eBooks · doi:10.1201/b11018-11

Cryo-electron microscopy structures of large ribosomal subunit complexes: insights into biogenesis, evolution, and regulation of the ribosome

Greber, B. J. (2013) · Repository for Publications and Research Data (ETH Zurich) · doi:10.3929/ethz-a-009988681

BCL::Fold - De novo protein structure prediction by assembly of secondary structure elements

Karakaş, M. (2011)

Roles of periplasmic chaperones and BamA in outer membrane protein folding

Schiffrin, R. (2016) · White Rose eTheses Online (University of Leeds, The University of Sheffield, University of York)

Mechanisms of translocation-coupled protein unfolding using anthrax toxin as a model

Thoren, K. L. (2011) · eScholarship (California Digital Library)

Identification of the determinants of efficient Pestivirus replication

Risager, P. C., Belsham, G. J., & Rasmussen, T. B. (2013)

ATP-induced asymmetric pre-protein folding: a driver of protein translocation?Preprint

Corey, R. A., Allen, W. J., & Collinson, I. R. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/202150

Two SecA/SecY Systems with Distinct Roles in the Ecological Adaptations of BacteriaPreprint

Jiang, X., & Fares, M. A. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/202358

Structural Biology of Sec Translocon

Tsukazaki, T. (2018) · Seibutsu Butsuri · doi:10.2142/biophys.58.078

Interaction of the Motor Protein SecA and the Bacterial Protein Translocation Channel SecYEG in the Absence of ATPPreprint

Winkler, K., Karner, A., Hörner, A., Hannesschlaeger, C., Knyazev, D. G., Siligan, C., Zimmermann, M., Kuttner, R., Pohl, P., & Preiner, J. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/799247

Characterization of Structure and Function of SECA Domains

Huang, Y. (2022) · Digital Archive @ GSU · doi:10.57709/2384955

Refolding Recombinant Escherichia coli BamA: the integral membrane component of the BAM (Beta-barrel Assembly Machinery) complex

Fu, M. F. (2014) · Summit (Simon Fraser University)

Faculty Opinions recommendation of Heat shock transcription factor σ32 co-opts the signal recognition particle to regulate protein homeostasis in E. coli.

Pool, M. (2014) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.718214210.793489388

El efecto estérico del abarrotamiento intracelular dinámico sobre la translocación de cadenas peptídicas

Pérez, J. A. V. (2014) · doi:10.24275/uami.0r967385d

El fenómeno de la percepción en tres relatos y la condesa sangrienta de Alejandra Pizarnik

Pallares, M. S. (2014) · doi:10.24275/uami.ks65hc345

References

(2020) · Wiley eBooks · doi:10.1002/9781119309697.ref

Faculty Opinions recommendation of Structure of the SecY channel during initiation of protein translocation.

Wollert, T. (2014) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.718153956.793490518

Interaction of the SecYEG translocon with the SRP receptor and the ribosome

Draycheva, A. (2015) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-5058

Protein Folding, Structure, Confirmation, and Dynamics

Appasani, K., & Appasani, R. K. (2022) · Cambridge University Press eBooks · doi:10.1017/9781108525909.008

Faculty Opinions recommendation of Molecular Mimicry of SecA and Signal Recognition Particle Binding to the Bacterial Ribosome.

Bibi, E. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.736422813.793566881

Faculty Opinions recommendation of The molecular mechanism of cotranslational membrane protein recognition and targeting by SecA.

Bibi, E. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.736685805.793566880

Faculty Opinions recommendation of Applications of the molecular dynamics flexible fitting method.

Rohs, R., & Lasso, G. (2012) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.13488967.15267058

Faculty Opinions recommendation of Structure of the post-translational protein translocation machinery of the ER membrane.

Ito, K. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.734706632.793568686

Faculty Opinions recommendation of Structure of the post-translational protein translocation machinery of the ER membrane.

Römisch, K. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.734706632.793555525

The year in Nature

(2008) · Nature · doi:10.1038/456xiia

Faculty Opinions recommendation of Structure of the SecY channel during initiation of protein translocation.

Ito, K. (2013) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.718153956.793486159

Faculty Opinions recommendation of Structure of the post-translational protein translocation machinery of the ER membrane.

Zhang, Y. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.734706632.793556355

Investigation of the Oligomeric State of Membrane-Bound SecA Using Förster Resonance Energy Transfer

Northrop, J. (2022) · doi:10.14418/wes01.2.365

Uncovering the Membrane-Integrated Secan Protein and its Role as a Protein Conducting Channel

Jin, F., & Chang, Z. (2022) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2022.140865

The Relative Distance Prediction of Transmembrane Protein Surface Residue Based on Improved Residual Networks

Chen, Q., Guo, Y., Jiang, J., Qu, J., Zhang, L., & Wang, H. (2023) · Mathematics · doi:10.3390/math11030642

Structural analysis of the dynamic ribosome-translocon complex

Lewis, A. J. O., Zhong, F., Keenan, R. J., & Hegde, R. S. (2023) · doi:10.1101/2023.12.22.572959

Comparison of In Silico Signal Sequence-Phospholipid Results with Described In Vitro and In Vivo Protein Translocation Studies Seems to Underscore the Significance of Phospholipids

Keller, R. C. A. (2024) · Lipidology · doi:10.3390/lipidology1010002

Bacterial Protein Transport Pathways and Analogous Conserved Pathways in Eukaryotes

Kauffman, P., Kaushik, S., Kühn, A., & Dalbey, R. (2024) · Springer eBooks · doi:10.1007/978-3-031-57446-7_10

Translation arrest cancellation of VemP, a secretion monitor in Vibrio, is regulated by multiple cis and trans factors, including SecY

Ikeda, Y., Miyazaki, R., Tsukazaki, T., Akiyama, Y., & Mori, H. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107735 · Cited by 1

A bio-informatics approach to identify new drug targets in multidrug-resistant bacteriaPreprint

Ramsden, I., Chiam, A., Hoogland, D., & Ulmschneider, M. B. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.31.657076

Automated registration and clustering for enhanced localization atomic force microscopy of flexible membrane proteins

Lisowski, C. M., King, G. M., & Kosztin, I. (2025) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1013277

Not All SecA Proteins Are Created Equal: A Study of the SecA1 and SecA2 Proteins of Mycobacterium tuberculosis.

D’Lima, N. G. (2014) · OpenCommons - UConn (University of Connecticut)

Membrane protein topogenesis

Öjemalm, K. (2015) · KTH Publication Database DiVA (KTH Royal Institute of Technology)

Dual-topology membrane proteins in Escherichia coli

Seppälä, S. (2011) · DiVA (Stockholm University)

Translocation of proteins into and across the bacterial and mitochondrial inner membranes

Botelho, S. C. (2012)

Etude Structurale par RMN hétéronucléaire du pseudopilus de Pseudomonas aeruginosa, un composant essentiel de la machinerie de sécrétion de Type II : le paradigme pseudopilus/piston

Alphonse, S. (2010) · doi:10.70675/fc16506czf35fz4fb6z966czb84ae190eaf5

PA 7, souche atypique de Pseudomonas aeruginosa : Etude transcriptomique et caractérisation d'un troisième système de sécrétion de type II fonctionnel, Txc

Cadoret, F. (2014) · theses.fr (ABES) · doi:10.70675/4c0e5d36zbb4fz400az8c54z1d227a03bd13

Post-transcriptional regulation of porin expression in Escherichia coli and its impact on antibiotic resistance

Dam, S. (2018) · theses.fr (ABES) · doi:10.70675/5ec431e0zc1f1z4741zae61zef885a2656d0

Freeze–Thaw Cycles Greatly Affect the Conjugative Transfer of Antibiotic-Resistant Genes: Effects of the Secretion of Extracellular Polymeric Substances

Li, Z., Qin, J., He, L., Nie, C., Liu, F., Hou, Y., & Tong, M. (2026) · Environmental Science & Technology · doi:10.1021/acs.est.6c06057

Bacterial Surfaces and Barriers: Biogenesis and Pathogen–Host Interactions

Bartholomew-Schoch, J., Finnie, J. K., Gahlmann, A., & Columbus, L. M. (2026) · Chemical Reviews · doi:10.1021/acs.chemrev.5c01068

MifM, a Regulatory Nascent Chain That Monitors Membrane Protein Integration

Chiba, S. (2014) · Springer eBooks · doi:10.1007/978-4-431-55052-5_15

From protein production to genome evolution in Escherichia coli

Schlegel, S. (2013) · KTH Publication Database DiVA (KTH Royal Institute of Technology)

Electrophysiological Characterization of SecA-dependent Protein-conducting Channel

Hsieh, Y. (2022) · Digital Archive @ GSU · doi:10.57709/2385051

Mass Spectrometry-Based Strategies for Biomolecular Structure Analysis: Steroid Metabolites Structures and Protein-Protein Interactions

Yan, Y. (2015) · Open Scholarship Institutional Repository (Washington University in St. Louis) · doi:10.7936/k7fj2dz2

A role for the two-helix finger of the SecA ATPase in protein translocation

Erlandson, K. J., Miller, S. B. M., Nam, Y., Osborne, A. R., Zimmer, J., & Rapoport, T. A. (2008) · Nature · doi:10.1038/nature07439 · Cited by 140

Conformational transition of Sec machinery inferred from bacterial SecYE structures

Tsukazaki, T., Mori, H., Fukai, S., Ishitani, R., Mori, T., Dohmae, N., Perederina, A. A., Sugita, Y., Vassylyev, D. G., Ito, K., et al. (2008) · Nature · doi:10.1038/nature07421 · Cited by 219

Structure of the substrate-engaged SecA-SecY protein translocation machine

Ma, C., Wu, X., Sun, D., Park, E., Catipovic, M. A., Rapoport, T. A., Gao, N., & Li, L. (2019) · Nature Communications · doi:10.1038/s41467-019-10918-2 · Cited by 74

Crystal structure of a substrate-engaged SecY protein-translocation channel

Li, L., Park, E., Ling, J. J., Ingram, J. R., Ploegh, H. L., & Rapoport, T. A. (2016) · Nature · doi:10.1038/nature17163 · Cited by 186

Clamour for a kiss

Economou, A. (2008) · Nature · doi:10.1038/455879a · Cited by 9