Cited by 460Cellular transport and secretionRNA and protein synthesis mechanismsNuclear Structure and Function

The DOI matches its Crossref record; 96 of the 96 references it cites were found in a registry or an index.

Protein Translocation Across Biological Membranes

Wickner, William, Schekman, Randy·2005·Science

Open this paper in CoChat — free account

Abstract

Subcellular compartments have unique protein compositions, yet protein synthesis only occurs in the cytosol and in mitochondria and chloroplasts. How do proteins get where they need to go? The first steps are targeting to an organelle and efficient translocation across its limiting membrane. Given that most transport systems are exquisitely substrate specific, how are diverse protein sequences recognized for translocation? Are they translocated as linear polypeptide chains or after folding? During translocation, how are diverse amino acyl side chains accommodated? What are the proteins and the lipid environment that catalyze transport and couple it to energy? How is translocation coordinated with protein synthesis and folding, and how are partially translocated transmembrane proteins released into the lipid bilayer? We review here the marked progress of the past 35 years and salient questions for future work. Subcellular compartments have unique protein compositions, yet protein synthesis only occurs in the cytosol and in mitochondria and chloroplasts. How do proteins get where they need to go? The first steps are targeting to an organelle and efficient translocation across its limiting membrane. Given that most transport systems are exquisitely substrate specific, how are diverse protein sequences recognized for translocation? Are they translocated as linear polypeptide chains or after folding? During translocation, how are diverse amino acyl side chains accommodated? What are the proteins and the lipid environment that catalyze transport and couple it to energy? How is translocation coordinated with protein synthesis and folding, and how are partially translocated transmembrane proteins released into the lipid bilayer? We review here the marked progress of the past 35 years and salient questions for future work.

Integrity signals

Registry

Crossref · 10.1126/science.1113752

Cites

96 of 96 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

X-ray structure of a protein-conducting channel
van den Berg, B., Clemons, W., Collinson, I. R., Modis, Y., Hartmann, E., Harrison, S. C., & Rapoport, T. A. (2003) · Nature · doi:10.1038/nature02218 · Cited by 1,236
ERAD: the long road to destruction
Meusser, B., Hirsch, C., Jarosch, E., & Sommer, T. (2005) · Nature Cell Biology · doi:10.1038/ncb0805-766 · Cited by 1,221
Transfer of proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components.
Blobel, G., & Dobberstein, B. (1975) · The Journal of Cell Biology · doi:10.1083/jcb.67.3.852 · Cited by 1,173
A conserved tripeptide sorts proteins to peroxisomes.
Gould, S. J., Keller, G. A., Hosken, N. A., Wilkinson, J. Q., & Subramani, S. E. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.108.5.1657 · Cited by 1,107
A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
Ye, Y., Shibata, Y., Yun, C., Ron, D., & Rapoport, T. A. (2004) · Nature · doi:10.1038/nature02656 · Cited by 963
Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes.
Walter, P., & Blobel, G. (1981) · The Journal of Cell Biology · doi:10.1083/jcb.91.2.557 · Cited by 810
Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulum
Walter, P., & Blobel, G. (1982) · Nature · doi:10.1038/299691a0 · Cited by 779
Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria
Eilers, M., & Schatz, G. (1986) · Nature · doi:10.1038/322228a0 · Cited by 725
ER Degradation of a Misfolded Luminal Protein by the Cytosolic Ubiquitin-Proteasome Pathway
Hiller, M. M., Finger, A., Schweiger, M. W., & Wolf, D. H. (1996) · Science · doi:10.1126/science.273.5282.1725 · Cited by 706
A common export pathway for proteins binding complex redox cofactors?
Berks, B. C. (1996) · Molecular Microbiology · doi:10.1046/j.1365-2958.1996.00114.x · Cited by 685

Show all 96 references

Research works printed but not linked: 2

C. Milstein, G. G. Brownlee, T. M. Harrison, M. B. Mathews, Nature New Biol239, 117 (1972).
J. Luirink, I. Sinning, Biochim. Biophys. Acta1694, 17 (2004).

Sorted by citations

Items 301–400 of 460

Curli Biogenesis: Bacterial Amyloid Assembly by the Type VIII Secretion Pathway
Bhoite, S. S., Gerven, N. V., Chapman, M. R., & Remaut, H. K. (2019) · ASM Press eBooks · doi:10.1128/9781683670285.ch14 · Cited by 7
Density Gradient Enrichment of Escherichia coli Conditional msbA Mutants
Doerrler, W. T. (2007) · Applied and Environmental Microbiology · doi:10.1128/aem.01992-07 · Cited by 7
Convective flow driven by a chemical nanopump
Ding, Y., Cartwright, J. H. E., & Cardoso, S. S. S. (2020) · Physical Review Fluids · doi:10.1103/physrevfluids.5.082201 · Cited by 7
Regulation of Nucleocytoplasmic Transport by ADP-Ribosylation: The Emerging Role of Karyopherin-β1 Mono-ADP-Ribosylation by ARTD15
Girolamo, M. D. (2014) · Current topics in microbiology and immunology · doi:10.1007/82_2014_421 · Cited by 7
Bacterial Glycolipid Acting on Protein Transport Across Membranes
Mori, S., Shionyu, M., Shimamoto, K., & Nomura, K. (2024) · ChemBioChem · doi:10.1002/cbic.202300808 · Cited by 6
The transmembrane supercomplex mediating the biogenesis of OMPs in Gram‐negative bacteria assumes a circular conformational change upon activation
Jin, F. (2020) · FEBS Open Bio · doi:10.1002/2211-5463.12922 · Cited by 5
Genomic insights revealed the environmental adaptability of Planococcus halotolerans Y50 isolated from petroleum-contaminated soil on the Qinghai-Tibet Plateau
Yang, R., Zhang, B., Xu, Y., Zhang, G., Liu, Y., Zhang, D., Zhang, W. Y., Chen, T., & Liu, G. (2022) · Gene · doi:10.1016/j.gene.2022.146368 · Cited by 6
Emergence of Animals from Heat Engines – Part 1. Before the Snowball Earths
Muller, A. W. J. (2009) · Entropy · doi:10.3390/e11030463 · Cited by 7
Wechselwirkungen der hydrophoben Cluster im entfalteten Membranprotein OmpX in Harnstofflösung
Hiller, S., Wider, G., Imbach, L., & Kurt Wüthrich, A. (2007) · Angewandte Chemie · doi:10.1002/ange.200703367 · Cited by 6
Protein Import into Hydrogenosomes and Mitosomes
Dyall, S. D., & Doležal, P. (2007) · Springer eBooks · doi:10.1007/7171_2007_105 · Cited by 6
Lipid insertion domain unfolding regulates protein orientational transition behavior in a lipid bilayer
Cheng, K. H., Qiu, L., Cheng, S. Y., & Vaughn, M. W. (2015) · Biophysical Chemistry · doi:10.1016/j.bpc.2015.06.011 · Cited by 6
Management of microbial communities to improve growth of chloroethene-respiring Dehalococcoides
Delgado, A. G. (2013) · Cited by 6
Protein Structure Analysis
Gromiha, M. M. (2010) · Elsevier eBooks · doi:10.1016/b978-8-1312-2297-3.50003-5 · Cited by 7
Dbi1 is an oxidoreductase and an assembly chaperone for mitochondrial inner membrane proteins
Badrie, S., Hell, K., & Mokranjac, D. (2025) · EMBO Reports · doi:10.1038/s44319-024-00349-6 · Cited by 5
Differential Proteomics of Helicobacter pylori Isolates from Gastritis, Ulcer, and Cancer Patients: First Study from Northwest Pakistan
Shah, S. A. R., Rahman, H., Qasim, M., Akram, M. S., Saygıdeğer, Y., Puspita, N., Demir, B. S., Alzahrani, K. J., Rehman, M. F. U., Alzahrani, F. M., et al. (2022) · Medicina · doi:10.3390/medicina58091168 · Cited by 5
Protein translocation through α-helical channels and insertases
Chen, J., Zhou, X., Yang, Y., & Li, L. (2024) · Structure · doi:10.1016/j.str.2024.10.032 · Cited by 5
Evaluating the Energy-Dependent “Binding” in the Early Stage of Protein Import into Chloroplasts
Akita, M., & Inoue, H. (2009) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(09)66003-1 · Cited by 5
An Unusual TOM20/TOM22 Bypass Mechanism for the Mitochondrial Targeting of Cytochrome P450 Proteins Containing N-terminal Chimeric Signals
Anandatheerthavarada, H. K., Sepuri, N. B. V., Biswas, G., & Avadhani, N. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801464200 · Cited by 5
Retracted
Analysis of Protein Interactions at Native Chloroplast Membranes by Ellipsometry
Kriechbaumer, V., Nabok, A. V., Mustafa, M. K., Al-Ammar, R., Lishchuk, A., Smith, D. P., & Abell, B. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034455 · Cited by 5
Scaling and alpha-helix regulation of protein relaxation in a lipid bilayer
Qiu, L., Buie, C., Cheng, K. H., & Vaughn, M. W. (2014) · The Journal of Chemical Physics · doi:10.1063/1.4902229 · Cited by 5
Steric contribution of macromolecular crowding to the time and activation energy for preprotein translocation across the endoplasmic reticulum membrane
Pérez, J. A. V., Guzmán, O., & Navarro‐García, F. (2013) · Physical Review E · doi:10.1103/physreve.88.012725 · Cited by 5
The incoherence of the vesicle theory of protein secretion
Rothman, S. S. (2006) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2006.10.004 · Cited by 5
Using toponomics to characterize phenotypic diversity in alveolar macrophages from male mice treated with exogenous SP-A1
Phelps, D. S., Chinchilli, V. M., Weisz, J., Shearer, D. A., Zhang, X., & Floros, J. (2020) · Biomarker Research · doi:10.1186/s40364-019-0181-z · Cited by 5
Characterization of a membrane protein (VP001L) from infectious spleen and kidney necrosis virus (ISKNV)
Xu, X., Lü, J., Lu, Q., Zhong, H., Weng, S., & He, J. (2007) · Virus Genes · doi:10.1007/s11262-007-0177-x · Cited by 5
Submucosal hypoganglionosis causing chronic idiopathic intestinal pseudo-obstruction.
von Boyen, G. B. T., von der Ohe, M., Krammer, H.-J., & Singer, M. V. (2002) · PubMed · Cited by 5
Mitochondrial presequences are more than just address labels
Heller, E. M., Lenhard, S., Rapaport, D., & Herrmann, J. (2026) · Protein Science · doi:10.1002/pro.70491 · Cited by 5
Role of extracellular cations in cell motility, polarity, and chemotaxis
Soll, D. R., Soll, D. R., Wessels, Lusche, Kuhl, & Scherer (2011) · Research and Reports in Biology · doi:10.2147/rrb.s13701 · Cited by 4
Translocation of alkane through graphene nanopore: A molecular dynamics simulation study
Li, J.-Y., Yang, H. S., Sheng, Y.-Z., Zhao, X.-T., & Sun, M. (2014) · Russian Journal of Physical Chemistry A · doi:10.1134/s0036024414120115 · Cited by 4
Mechanism of Action of Monoclonal Antibodies That Block the Activity of the Lethal Toxin of Bacillus Anthracis
Romanenko, Y. O., Рябко, А. К., Marin, M. A., Kartseva, A. S., Silkina, M. V., Shemyakin, I. G., & Firstova, V. V. (2021) · Acta Naturae · doi:10.32607/actanaturae.11387 · Cited by 4
Peroxisomal Disorders
Pennesi, M. E., & Weleber, R. G. (2012) · Oxford University Press eBooks · doi:10.1093/med/9780195326147.003.0044 · Cited by 4
Dual targeting agent Thiotert inhibits the progression of glioblastoma by inducing ER stress-dependent autophagy
Dong, J., Qian, Y., Zhang, W., Wang, Q., Jia, M., Yue, J., Fan, Z., Jiang, Y., Wang, L., Wang, Y., et al. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115867 · Cited by 4
Capturing the bacterial holo-complex
Duong, F. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402139111 · Cited by 3
Regulation of Cell Death by c-FLIP Phosphorylation
Asaoka, T., Kaunisto, A., & Eriksson, J. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-6612-4_66 · Cited by 4
The Role of the TIM23 Complex and Its Associated Motor Complex in Mitochondrial Protein Import
Dudek, J., Guiard, B., & Rehling, P. (2007) · The Enzymes · doi:10.1016/s1874-6047(07)25015-2 · Cited by 4
Comparing cytosolic expression to peroxisomal targeting of the chimeric L1/L2 (ChiΔH‐L2) gene from human papillomavirus type 16 in the methylotrophic yeasts Pichia pastoris and Hansenula polymorpha
Smith, J. J., Burke, A., Bredell, H., van Zyl, W. H., & Görgens, J. F. (2012) · Yeast · doi:10.1002/yea.2917 · Cited by 4
Formalizing Spherical Membrane Structures and Membrane Proteins Populations
Besozzi, D., & Rozenberg, G. (2006) · Lecture notes in computer science · doi:10.1007/11963516_2 · Cited by 4
Gene- and cell-based therapy of diabetes: between bench and bedside.
Kofman, A. V., Kharazova, A., & Pinaev, G. P. (2002) · PubMed · Cited by 4
The Structure and Function of the Chloroplast Import Apparatus.
Jin, Z., & Yan, Z. (2026) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-062325-090826
In silico analysis and experimental validation of lipoprotein and novel Tat signal peptides processing in Anabaena sp. PCC7120
Kumari, S., & Chaurasia, A. K. (2015) · The Journal of Microbiology · doi:10.1007/s12275-015-5281-3 · Cited by 3
Translocation Pathway‐Dependent Assembly of Streptavidin‐ and Antibody‐Binding Filamentous Virus‐Like Particles
Kim, E. J., Jeon, C. S., Hwang, I., & Chung, T. D. (2016) · Small · doi:10.1002/smll.201601693 · Cited by 3
Voltage-gated nanofluidic devices for protein capture, concentration, and release
Rangharajan, K. K., & Prakash, S. (2022) · The Analyst · doi:10.1039/d2an00745b · Cited by 3
Protein Import into Hydrogenosomes and Mitosomes
Doležal, P., Makki, A., & Dyall, S. D. (2019) · Microbiology monographs · doi:10.1007/978-3-030-17941-0_3 · Cited by 3
Enhanced assay of endothelial exocytosis using extracellular matrix components
LoMonaco, M. B., & Lowenstein, C. J. (2014) · Analytical Biochemistry · doi:10.1016/j.ab.2014.02.015 · Cited by 3
Localization Prediction and Structure-Based In Silico Analysis of Bacterial Proteins: With Emphasis on Outer Membrane Proteins
Imai, K., Hayat, S., Sakiyama, N., Fujita, N., Tomii, K., Elofsson, A., & Horton, P. (2012) · Methods in molecular biology · doi:10.1007/978-1-62703-107-3_10 · Cited by 3
Trusting Your Gut, Among Other Things: Digestive Enzyme Secretion, Intuition, and the History of Science
Isenman, L. D. (2009) · Foundations of Science · doi:10.1007/s10699-009-9164-0 · Cited by 3
Conformational Effects on the Threading Kinetics of Dumbbell‐Shaped Guests into the Cavity of Oxatub[4]arene
Jia, F., Li, D., He, S., Yang, L., & Jiang, W. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202212305 · Cited by 3
Organelle Structure and Function
(2008) · Elsevier eBooks · doi:10.1016/b978-0-12-370458-0.50009-8 · Cited by 3
Structural insights into the mechanism of a novel protein targeting pathway in Gram‐negative bacteria
Jin, F. (2020) · FEBS Open Bio · doi:10.1002/2211-5463.12813 · Cited by 3
The IQ ‐compete assay for measuring mitochondrial protein import efficiencies in living yeast cells
Hoffman, Y., Egeler, A., Rödl, S., & Herrmann, J. M. (2025) · FEBS Letters · doi:10.1002/1873-3468.70206 · Cited by 2
Structural evolution of the MTCH family of mitochondrial insertases
Stevens, T. A., Luo, Z., Lee, C., Hazu, M., Galatis, E. G., Inglis, A. J., Guna, A., & Voorhees, R. M. (2026) · Science Advances · doi:10.1126/sciadv.aeh2957 · Cited by 2
Conformational Transduction Amplification in a Biomimetic Polyelectrolyte for Ultrasensitive Imaging of Iron Metabolism
Zhou, Y., Yang, D., Wang, Y., Li, S., Fan, F., Zou, J., Zhang, C. P., Liu, Y., Tan, H. S., & Ding, M. (2026) · Advanced Science · doi:10.1002/advs.76185 · Cited by 2
On Message Ribonucleic Acids Targeting to Mitochondria
Ding, D., Dave, K. R., & Bhattacharya, S. K. (2009) · Biochemistry Insights · doi:10.4137/bci.s3745 · Cited by 2
Channel-facilitated molecular transport: The role of strength and spatial distribution of interactions
Uppulury, K., & Kolomeisky, A. B. (2016) · Chemical Physics · doi:10.1016/j.chemphys.2016.06.012 · Cited by 2
RNA-seq revealed the effects of heat stress on different brain regions of Leiocassis longirostris
Liu, S., Li, R. Q., Deng, Y., Wang, Z., Feng, Y., Zhao, H., Zhao, Z., Zhang, L., Duan, Y., Huang, Z., et al. (2025) · Frontiers in Physiology · doi:10.3389/fphys.2025.1579499 · Cited by 2
Protein Translocation Acquires Substrate Selectivity Through ER Stress-Induced Reassembly of Translocon Auxiliary Components
Lee, S., Shin, Y., Kim, K., Song, Y., Kim, Y., & Kang, S. (2020) · Cells · doi:10.3390/cells9020518 · Cited by 2
The Ins and Outs of Chloroplast Protein Transport
Ling, Q., Trösch, R., & Jarvis, P. (2013) · Advances in photosynthesis and respiration · doi:10.1007/978-94-007-5724-0_12 · Cited by 2
Internalization of exogenous ADP-ribosylation factor 6 (Arf6) proteins into cells
Afroze, S. H., Uddin, M. N., Cao, X. X., Asea, A. A. A., & Gizachew, D. (2011) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-011-0829-y · Cited by 2
Digestive Enzyme Secretion, Intuition, and the History of Science: Part II
Isenman, L. D. (2009) · Foundations of Science · doi:10.1007/s10699-009-9163-1 · Cited by 2
Energy Requirements for Protein Secretion via the Flagellar Type III Secretion System
Erhardt, M. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7033-9_30 · Cited by 2
1 Freight Management in the Cell: Current Aspects of Intracellular Membrane Trafficking
Herrmann, J. M., & Spang, A. (2008) · Methods in molecular biology · doi:10.1007/978-1-59745-261-8_1 · Cited by 2
Monitoring Endocytic Trafficking of Anthrax Lethal Factor by Precise and Quantitative Protein Labeling
Zheng, S., Zhang, G., Li, J., & Chen, P. R. (2014) · Angewandte Chemie · doi:10.1002/ange.201403945 · Cited by 2
Endoplasmic Reticulum Stress and Emerging Therapeutic Targets in Cancer
Yeap, J. W., & Tan, M. (2023) · Springer eBooks · doi:10.1007/978-3-030-80962-1_271-1 · Cited by 2
Quantifying Substrate Protein Secretion via the Type III Secretion System of the Bacterial Flagellum
Einenkel, R., Halte, M., & Erhardt, M. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3445-5_36 · Cited by 2
Electron Paramagnetic Resonance Spectroscopy
Yang, Z., & Feng, L. (2023) · ACS in focus · doi:10.1021/acsinfocus.7e7031 · Cited by 2
Preliminary X-ray crystallographic studies of yeast Get3
Hu, J., Li, J., Qian, X., Jin, Z., Fu, Z., & Sha, B. (2009) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309109012317 · Cited by 2
Measurement of the Energetics of Protein Transport Across the Chloroplast Thylakoid Membrane
Theg, S. M. (2010) · Methods in molecular biology · doi:10.1007/978-1-60327-412-8_19 · Cited by 2
Mitochondria‐Targeted Cytochromes P450 Modulate Adverse Drug Metabolism and Xenobiotic‐Induced Toxicity
Raza, H., Guengerich, F. P., & Avadhani, N. G. (2018) · Wiley eBooks · doi:10.1002/9781119329725.ch4 · Cited by 2
A Transfer Matrix Approach to Studying the Entanglement Complexity of Self-Avoiding Polygons in Lattice Tubes
Eng, J. (2020) · HARVEST (University of Saskatchewan) · Cited by 2
The ER transmembrane complex (EMC) can functionally replace the Oxa1 insertase in mitochondriaPreprint
Güngör, B., Flohr, T., Garg, S. G., & Herrmann, J. M. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.08.02.454725 · Cited by 2
The Pathogenesis of Preeclampsia: Hypoxia and the Unfolded Protein Response
Yildiz, N., & Ekmekçi, H. (2026) · Reproductive Sciences · doi:10.1007/s43032-026-02135-2 · Cited by 1
The Giardia Mitosomes
Tachezy, J., & Doležal, P. (2011) · Springer eBooks · doi:10.1007/978-3-7091-0198-8_11 · Cited by 1
A screen for over-secretion of proteins by yeast based on a dual component cellular phosphatase and immuno-chromogenic stain for exported bacterial alkaline phosphatase reporter
Nallaseth, F. S., & Anderson, S. (2013) · Microbial Cell Factories · doi:10.1186/1475-2859-12-36 · Cited by 1
Lipids Guide the Way: Targeting Proteins to the Chloroplast Outer Envelope Membrane
Richardson, L. G. L., Paila, Y. D., & Schnell, D. J. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.08.017 · Cited by 1
Recombinant protein secretion via the type III secretion system
Vo, L. T. D., & Hong, S. H. (2011) · Korean Journal of Chemical Engineering · doi:10.1007/s11814-011-0024-6 · Cited by 1
Structure and Function of RXLR Effectors of Plant Pathogenic Oomycetes
Morgan, W. R., Bos, J. I. B., Bruce, C. R., Lee, M., Liu, H., Oh, S., Song, J. K., Win, J., Young, C. A., & Kamoun, S. (2008) · Springer eBooks · doi:10.1007/978-0-387-76723-9_12 · Cited by 1
Translocation process of structured polypeptides across nanopores
Fabio Cecconi, A., Marconi, U. M. B., & Vulpiani, A. (2010) · Spectroscopy An International Journal · doi:10.1155/2010/794318 · Cited by 1
Mitochondria and Diseases
(2020) · Elsevier eBooks · doi:10.1016/b978-0-12-817927-7.00005-3 · Cited by 1
Conformational Effects on the Threading Kinetics of Dumbbell‐Shaped Guests into the Cavity of Oxatub[4]arene
Jia, F., Li, D., He, S., Yang, L., & Jiang, W. (2022) · Angewandte Chemie · doi:10.1002/ange.202212305 · Cited by 1
Biotechnological Implications of Extracellular Vesicles
Avellán‐Llaguno, R. D., Zhu, L., Huang, H., Xu, X., & Huang, Q. (2023) · Environmental and microbial biotechnology · doi:10.1007/978-981-99-2808-8_16 · Cited by 1
Mitochondria, Peroxisomes and Beyond—How Dual Targeting Regulates Organelle Tethering
Freitag, J., Stehlik, T., & Bange, G. (2024) · Contact · doi:10.1177/25152564241264254 · Cited by 1
The basic genetic toolkit to move in with your photosynthetic partner
Reyes‐Prieto, A. (2015) · Frontiers in Ecology and Evolution · doi:10.3389/fevo.2015.00100 · Cited by 1
An improvement of the sequential algorithm for modeling the chain-like-bodies motion
Bartłomiejczyk, K. (2018) · Journal of Applied Mathematics and Computational Mechanics · doi:10.17512/jamcm.2018.2.01 · Cited by 1
Determination of the Stability and Intracellular (Intra-Nuclear) Targeting and Recruitment of Pre-HAC1 mRNA in the Saccharomyces cerevisiae During the Activation of UPR
Paira, S., & Das, B. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-1732-8_9 · Cited by 1
Cloning and Functional Identification of Yunwu Tribute Tea CsPPO Gene
Wang, Y., Li, L., Wan, C., Li, Y., & Zhao, D. (2023) · Russian Journal of Plant Physiology · doi:10.1134/s1021443723600502 · Cited by 1
From Biogenesis to Overexpression of Membrane Proteins in Escherichia coli
Wagner, S. (2008) · KTH Publication Database DiVA (KTH Royal Institute of Technology) · Cited by 1
Can we build a conscious machine?Preprint
Aur, D. (2014) · arXiv (Cornell University) · doi:10.13140/2.1.2286.5608 · Cited by 2
Resource Letter: Bio-molecular Nano-machines: where Physics, Chemistry, Biology and Technology meetPreprint
Chowdhury, D. (2008) · arXiv (Cornell University) · doi:10.48550/arxiv.0807.2731 · Cited by 2
Membrane Insertion of Tail‐anchored Proteins
Schuldiner, M., Schwappach, B., & Weissman, J. S. (2010) · Encyclopedia of Life Sciences · doi:10.1002/9780470015902.a0021876 · Cited by 1
Co-and Posttranslational Protein Targeting to the SecYEG Translocon inEscherichia coli
Bibi, E. (2014) · ASM Press eBooks · doi:10.1128/9781555815806.ch1 · Cited by 1
Cytotoxicity of Aberrant Proteins
Ashok, A., & Hegde, R. S. (2008) · Wiley eBooks · doi:10.1002/9780470015902.a0020887 · Cited by 1
The Biosynthesis of Proteins
Langel, U., Cravatt, B. F., Gräslund, A., von Heijne, N. G. H., Zorko, M., Land, T., & Niessen, S. (2009) · CRC Press eBooks · doi:10.1201/b15106-10 · Cited by 1
Revelation of a Novel Protein Translocon in Bacterial Plasma MembranePreprint
Jin, F., & Chang, Z. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/121335 · Cited by 1
Genetically Programmable Pathogen Sense and Destroy
Gupta, S., & Weiss, R. (2010) · SciVee · doi:10.4016/18510.01 · Cited by 1
The Translocation Apparatus of the Endoplasmic Reticulum
Alken, M., & Hegde, R. S. (2007) · The Enzymes · doi:10.1016/s1874-6047(07)25009-7 · Cited by 1
Organelle Structure and Function
(2020) · Elsevier eBooks · doi:10.1016/b978-0-12-817927-7.00004-1 · Cited by 1
Stress, mixed messages, and hormone signaling : regulation of translation and the unfolded protein response in pituitary gonadotropes
Minh‐Ha, T. (2008)
Charakterisierung Subtyp-spezifischer Autophagieproteine
Tolstrup, J. (2009) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-1361
Role of Deimination for Protein Synthesis in Neuronal Cells
Ding, D. (2012)
Protein Import into the Yeast Endoplasmic Reticulum: Methods
Brodsky, J. L., & Morrow, M. W. (2010) · Encyclopedia of Life Sciences · doi:10.1002/9780470015902.a0002619.pub3
Basics of Molecular Biology, Genetic Engineering, and Metabolic Engineering
Wang, M., & Shi, H. (2009) · doi:10.1002/9780470437988.ch2

Authors: Wickner, W., & Schekman, R.
Affiliations: Dartmouth College (US)
Corresponding author: Wickner, William
Schekman, Randy
ORCID: Wickner, William
Schekman, Randy
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2005-12-02
Volume: 310
Issue: 5753
Pages: 1452-1456
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.1113752
OpenAlex: W2021288400
Cited by: 458
References: 96
Citations by year: 2026: 7 · 2025: 13 · 2024: 10 · 2023: 13 · 2022: 20 · 2021: 20 · 2020: 25 · 2019: 13 · 2018: 13 · 2017: 16 · 2016: 18 · 2015: 18 · 2014: 35 · 2013: 19 · 2012: 28
FWCI: 2.36
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
Keywords: protein translocation, biological membranes, organelle targeting, mitochondrial protein import, chloroplast protein import, substrate specificity, membrane lipid environment, energy coupling, subcellular compartmentalization
MeSH terms: Carrier Proteins, Endoplasmic Reticulum, Intracellular Membranes, Mitochondria, Protein Biosynthesis, Protein Folding, Peroxisomes, Protein Transport

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Protein Translocation Across Biological Membranes

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks