Protein translocation across biological membranes

Wickner, William; Schekman, Randy

doi:10.1126/science.1113752

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

Protein translocation across biological membranes

Wickner, William, Schekman, Randy·2005·Science

DOI 10.1126/science.1113752

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?

Cargo protein with a classic NLS requires a direct interaction with importin-α to be transported through the nuclear pore complex.
“Cargo protein with a classic NLS requires a direct interaction with importin-α to be transported through the nuclear pore complex [31], [40], [45], [46], [47]”
From UV-Induced Nuclear Import of XPA Is Mediated by Importin-α4 in An ATR-Dependent Manner (2013) · cites this paper as [45]
Transportation of cargo protein in importin-α/−β protein complexes through the NPC requires energy derived from the activities of GTPases.
“Transportation of cargo protein in importin-α/−β protein complexes through the NPC requires energy derived from the activities of GTPases [40], [45] (Figure 2A).”
From UV-Induced Nuclear Import of XPA Is Mediated by Importin-α4 in An ATR-Dependent Manner (2013) · cites this paper as [45]

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 1,252 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 708 · see citing works
A membrane protein required for dislocation of misfolded proteins from the ER
Lilley, B. N., & Ploegh, H. L. (2004) · Nature · doi:10.1038/nature02592 · Cited by 674 · see citing works
Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
Görlich, D. (1993) · Cell · doi:10.1016/0092-8674(93)90483-7 · Cited by 674 · see citing works
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 669 · see citing works
A Possible Precursor of Immunoglobulin Light Chains
Milstein, C., Brownlee, G. G., Harrison, T. M., & Mathews, M. B. (1972) · Nature New Biology · doi:10.1038/newbio239117a0 · Cited by 603 · see citing works
The binding cascade of SecB to SecA to SecYE mediates preprotein targeting to the E. coli plasma membrane
Hartl, F.-U., Lecker, S., Schiebel, E., Hendrick, J. P., & Wickner, W. (1990) · Cell · doi:10.1016/0092-8674(90)90160-g · Cited by 562 · see citing works
Self-citation
Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
Plemper, R. K., Böhmler, S., Bordallo, J., Sommer, T., & Wolf, D. H. (1997) · Nature · doi:10.1038/42276 · Cited by 555 · see citing works
Synchronised transmembrane insertion and glycosylation of a nascent membrane protein
Rothman, J. E., & Lodish, H. F. (1977) · Nature · doi:10.1038/269775a0 · Cited by 531 · see citing works
Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum.
Walter, P., & Blobel, G. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.12.7112 · Cited by 513 · see citing works
The purified E. coli integral membrane protein is sufficient for reconstitution of SecA-dependent precursor protein translocation
Brundage, L., Hendrick, J. P., Schiebel, E., Driessen, A. J. M., & Wickner, W. (1990) · Cell · doi:10.1016/0092-8674(90)90111-q · Cited by 505 · see citing works
Self-citation
E. coli mutant pleiotropically defective in the export of secreted proteins
Oliver, D. B., & Beckwith, J. (1981) · Cell · doi:10.1016/0092-8674(81)90184-7 · Cited by 503 · see citing works
Protein Disulfide Isomerase Acts as a Redox-Dependent Chaperone to Unfold Cholera Toxin
Tsai, B., Rodighiero, C., Lencer, W. I., & Rapoport, T. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00289-6 · Cited by 484 · see citing works
Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor.
Gilmore, R., Walter, P., & Blobel, G. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.95.2.470 · Cited by 479 · see citing works
Role of EDEM in the Release of Misfolded Glycoproteins from the Calnexin Cycle
Molinari, M., Calanca, V., Galli, C., Lucca, P., & Paganetti, P. (2003) · Science · doi:10.1126/science.1079474 · Cited by 470 · see citing works
Contribution of the Endoplasmic Reticulum to Peroxisome Formation
Hoepfner, D., Schildknegt, D., Braakman, I., Philippsen, P., & Tabak, H. F. (2005) · Cell · doi:10.1016/j.cell.2005.04.025 · Cited by 463 · see citing works
Import of proteins into mitochondria: precursor forms of the extramitochondrially made F1-ATPase subunits in yeast.
Maccecchini, M. L., Rudin, Y., Blobel, G., & Schatz, G. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.1.343 · Cited by 453 · see citing works
EDEM As an Acceptor of Terminally Misfolded Glycoproteins Released from Calnexin
Oda, Y., Hosokawa, N., Wada, I., & Nagata, K. (2003) · Science · doi:10.1126/science.1079181 · Cited by 453 · see citing works
BiP Acts as a Molecular Ratchet during Posttranslational Transport of Prepro-α Factor across the ER Membrane
Matlack, K. E. S., Misselwitz, B., Plath, K., & Rapoport, T. A. (1999) · Cell · doi:10.1016/s0092-8674(00)80767-9 · Cited by 447 · see citing works
Evolutionary conservation of biogenesis of β-barrel membrane proteins
Paschen, S. A., Waizenegger, T., Stan, T., Preuss, M., Cyrklaff, M., Hell, K., Rapaport, D., & Neupert, W. (2003) · Nature · doi:10.1038/nature02208 · Cited by 431 · see citing works
A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum.
Deshaies, R. J., & Schekman, R. W. (1987) · The Journal of Cell Biology · doi:10.1083/jcb.105.2.633 · Cited by 425 · see citing works
Self-citation
Machinery for protein sorting and assembly in the mitochondrial outer membrane
Wiedemann, N., Kozjak‐Pavlovic, V., Chacińska, A., Schönfisch, B., Rospert, S., Ryan, M. T., Pfanner, N., & Meisinger, C. (2003) · Nature · doi:10.1038/nature01753 · Cited by 415 · see citing works
Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP.
McCracken, A. A., & Brodsky, J. L. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.132.3.291 · Cited by 409 · see citing works
Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation
Pilon, M., Schekman, R., & Römisch, K. (1997) · The EMBO Journal · doi:10.1093/emboj/16.15.4540 · Cited by 406 · see citing works
Self-citation
SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli.
Lill, R., Cunningham, K. W., Brundage, L., Ito, K., Oliver, D. B., & Wickner, W. T. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03458.x · Cited by 401 · see citing works
Self-citation
The Preprotein Translocation Channel of the Outer Membrane of Mitochondria
Künkele, K., Heins, S., Dembowski, M., Nargang, F. E., Benz, R., Thieffry, M., Walz, J. C., Lill, R., Nußberger, S., & Neupert, W. (1998) · Cell · doi:10.1016/s0092-8674(00)81206-4 · Cited by 399 · see citing works
The protein import motor of mitochondria
Neupert, W., & Brunner, M. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm878 · Cited by 394 · see citing works
Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p
Panzner, S., Dreier, L., Hartmann, E., Kostka, S., & Rapoport, T. A. (1995) · Cell · doi:10.1016/0092-8674(95)90077-2 · Cited by 393 · see citing works
Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast.
Knop, M., Finger, A. C., Braun, T., Hellmuth, K., & Wolf, D. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00411.x · Cited by 388 · see citing works
Post-translational transport into intact chloroplasts of a precursor to the small subunit of ribulose-1,5-bisphosphate carboxylase
Chua, N., & Schmidt, G. W. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.12.6110 · Cited by 384 · see citing works
Suppressor mutations that restore export of a protein with a defective signal sequence
Emr, S. D., Hanley-Way, S., & Silhavy, T. J. (1981) · Cell · doi:10.1016/0092-8674(81)90272-5 · Cited by 382 · see citing works
Biosynthesis of Serum Proteins and Ferritin by Free and Attached Ribosomes of Rat Liver
Redman, C. M. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94321-8 · Cited by 362 · see citing works
Import of carrier proteins into the mitochondrial inner membrane mediated by Tim22
Sirrenberg, C., Bauer, M. F., Guiard, B., Neupert, W., & Brunner, M. (1996) · Nature · doi:10.1038/384582a0 · Cited by 342 · see citing works
An oligomeric protein is imported into peroxisomes in vivo.
McNew, J. A., & Goodman, J. M. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.127.5.1245 · Cited by 339 · see citing works
The Protein Import Machinery of Mitochondria
Wiedemann, N., Frazier, A. E., & Pfanner, N. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.r400003200 · Cited by 336 · see citing works
A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum
Sommer, T., & Jentsch, S. (1993) · Nature · doi:10.1038/365176a0 · Cited by 334 · see citing works
In vitro protein translocation across the yeast endoplasmic reticulum: ATP-dependent post-translational translocation of the prepro-α-factor
Hansen, W., García, P. D., & Walter, P. (1986) · Cell · doi:10.1016/0092-8674(86)90325-9 · Cited by 333 · see citing works
The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins.
Ulbrandt, N. D., Newitt, J. A., & Bernstein, H. D. (1997) · Cell · doi:10.1016/s0092-8674(00)81839-5 · Cited by 332 · see citing works
Peroxisome Biogenesis
Purdue, P. E., & Lazarow, P. B. (2001) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.17.1.701 · Cited by 323 · see citing works
CONTROLLED PROTEOLYSIS OF NASCENT POLYPEPTIDES IN RAT LIVER CELL FRACTIONS
Sabatini, D. D., & Blobel, G. (1970) · The Journal of Cell Biology · doi:10.1083/jcb.45.1.146 · Cited by 317 · see citing works
The signal recognition particle in S. cerevisiae
Hann, B. C., & Walter, P. (1991) · Cell · doi:10.1016/0092-8674(91)90577-l · Cited by 305 · see citing works
Preferential Synthesis of Ferritin and Albumin by Different Populations of Liver Polysomes
Hicks, S. J., Drysdale, J., & Munro, H. N. (1969) · Science · doi:10.1126/science.164.3879.584 · Cited by 300 · see citing works
SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF
Economou, A., Pogliano, J. A., Beckwith, J. R., Oliver, D. B., & Wickner, W. T. (1995) · Cell · doi:10.1016/0092-8674(95)90143-4 · Cited by 295 · see citing works
Self-citation
The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter
Gohlke, U., Pullan, L., McDevitt, C. A., Porcelli, I., de Leeuw, E., Palmer, T., Saibil, H. R., & Berks, B. C. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503558102 · Cited by 277 · see citing works
Import of stably folded proteins into peroxisomes.
Walton, P. A., Hill, P. E., & Subramani, S. E. (1995) · Molecular Biology of the Cell · doi:10.1091/mbc.6.6.675 · Cited by 275 · see citing works
The E. coli ffh gene is necessary for viability and efficient protein export
Phillips, G. J., & Silhavy, T. J. (1992) · Nature · doi:10.1038/359744a0 · Cited by 269 · see citing works
Co-translocation of a Periplasmic Enzyme Complex by a Hitchhiker Mechanism through the Bacterial Tat Pathway
Rodrigue, A., Chanal, A., Beck, K., Müller, M. P., & Wu, L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.19.13223 · Cited by 268 · see citing works
GENETICS AND BIOGENESIS OF CHLOROPLASTS AND MITOCHONDRIA
Neupert, W., Sebald, W., & Werner, S. (1976) · Cited by 262 · see citing works
Htm1p, a mannosidase‐like protein, is involved in glycoprotein degradation in yeast
Jakob, C. A., Bodmer, D., Spirig, U., Bättig, P., Marcil, A., Dignard, D., Bergeron, J. J. M., Thomas, D. Y., & Aebi, M. (2001) · The EMBO Reports · doi:10.1093/embo-reports/kve089 · Cited by 252 · see citing works
Each of the activities of signal recognition particle (SRP) is contained within a distinct domain: Analysis of biochemical mutants of SRP
Siegel, V. (1988) · Cell · doi:10.1016/0092-8674(88)90529-6 · Cited by 248 · see citing works
Vectorial discharge of peptides released by puromycin from attached ribosomes.
Redman, C. M., & Sabatini, D. D. (1966) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.56.2.608 · Cited by 243 · see citing works
The pas8 mutant of Pichia pastoris exhibits the peroxisomal protein import deficiencies of Zellweger syndrome cells--the PAS8 protein binds to the COOH-terminal tripeptide peroxisomal targeting signal, and is a member of the TPR protein family [published erratum appears in J Cell Biol 1993 Sep;122(5):following 1143]
McCollum, D. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.121.4.761 · Cited by 243 · see citing works
The Human Peroxisomal Targeting Signal Receptor, Pex5p, Is Translocated into the Peroxisomal Matrix and Recycled to the Cytosol
Dammai, V., & Subramani, S. E. (2001) · Cell · doi:10.1016/s0092-8674(01)00310-5 · Cited by 241 · see citing works
Translocation of domains of nascent periplasmic proteins across the cytoplasmic membrane is independent of elongation.
Randall, L. L. (1983) · Cell · doi:10.1016/0092-8674(83)90352-5 · Cited by 234 · see citing works
SRP-mediated protein targeting: structure and function revisited
Luirink, J. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.03.013 · Cited by 231 · see citing works
Inversion of the Membrane Topology of SecG Coupled with SecA-Dependent Preprotein Translocation
Nishiyama, K., Suzuki, T., & Tokuda, H. (1996) · Cell · doi:10.1016/s0092-8674(00)81083-1 · Cited by 217 · see citing works
Escherichia coli YidC is a membrane insertase for Sec-independent proteins.
Serek, J., Bauer‐Manz, G., Struhalla, G., van den Berg, L., Kiefer, D., Dalbey, R., & Kuhn, A. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600063 · Cited by 211 · see citing works
British Optical Astronomy
Burbidge, G. R. (1972) · Nature · doi:10.1038/239117a0 · Cited by 204 · see citing works
Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases
Powers, T., & Walter, P. (1995) · Science · doi:10.1126/science.7660124 · Cited by 203 · see citing works
A novel signal recognition particle targets light-harvesting proteins to the thylakoid membranes
Schünemann, D., Gupta, S., Cartieaux, F., Klimyuk, V. I., Jones, J. D. G., Nussaume, L., & Hoffman, N. E. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.17.10312 · Cited by 200 · see citing works
Removal of the Alu structural domain from signal recognition particle leaves its protein translocation activity intact
Siegel, V., & Walter, P. (1986) · Nature · doi:10.1038/320081a0 · Cited by 179 · see citing works
Synthesis and assembly of the membrane proteins in E. coli
Ito, K., Sato, T., & Yura, T. (1977) · Cell · doi:10.1016/0092-8674(77)90073-3 · Cited by 179 · see citing works
In vitro translocation of bacterial proteins across the plasma membrane of Escherichia coli.
Müller, M. P., & Blobel, G. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.23.7421 · Cited by 174 · see citing works
Mechanisms of Protein Import and Routing in Chloroplasts
Jarvis, P., & Robinson, C. (2004) · Current Biology · doi:10.1016/j.cub.2004.11.049 · Cited by 174 · see citing works
Insertion into the mitochondrial inner membrane of a polytopic protein, the nuclear‐encoded Oxa1p
Herrmann, J. M., Neupert, W., & Stuart, R. A. (1997) · The EMBO Journal · doi:10.1093/emboj/16.9.2217 · Cited by 170 · see citing works
ATP is essential for protein translocation into Escherichia coli membrane vesicles.
Chen, L., & Tai, P. C. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.13.4384 · Cited by 165 · see citing works
Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY
Cannon, K. S., Or, E., Clemons, W., Shibata, Y., & Rapoport, T. A. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200412019 · Cited by 164 · see citing works
A signal sequence is not sufficient to lead β-galactosidase out of the cytoplasm
Moreno, F., Fowler, A. V., Hall, M. N., Silhavy, T. J., Zabin, I., & Schwartz, M. (1980) · Nature · doi:10.1038/286356a0 · Cited by 149 · see citing works
Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on theEscherichia coliribosome
Ullers, R. S., Houben, E. N. G., Raine, A., ten Hagen‐Jongman, C. M., Ehrenberg, M., Brunner, J., Oudega, B., Harms, N., & Luirink, J. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302130 · Cited by 142 · see citing works
In vitro SYNTHESIS OF DIFFERENT CATEGORIES OF SPECIFIC PROTEIN BY MEMBRANE-BOUND AND FREE RIBOSOMES
GANOZA, M. C., & Williams, C. A. (1969) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.63.4.1370 · Cited by 141 · see citing works
Identification and characterization of a membrane component essential for the translocation of nascent proteins across the membrane of the endoplasmic reticulum.
Meyer, D. I., & Dobberstein, B. (1980) · The Journal of Cell Biology · doi:10.1083/jcb.87.2.503 · Cited by 139 · see citing works
Empty Site Forms of the SRP54 and SRα GTPases Mediate Targeting of Ribosome–Nascent Chain Complexes to the Endoplasmic Reticulum
Rapiejko, P. J., & Gilmore, R. (1997) · Cell · doi:10.1016/s0092-8674(00)80253-6 · Cited by 134 · see citing works
Escherichia coli mutants accumulating the precursor of a secreted protein in the cytoplasm
Bassford, P. J., & Beckwith, J. (1979) · Nature · doi:10.1038/277538a0 · Cited by 132 · see citing works
Stepwise Movement of Preproteins in the Process of Translocation across the Cytoplasmic Membrane of Escherichia coli
Uchida, K., Mori, H., & Mizushima, S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.52.30862 · Cited by 127 · see citing works
Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase
Duong, F. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg418 · Cited by 127 · see citing works
Transport of Cytoplasmically Synthesized Proteins into the Mitochondria in a Cell Free System from Neurospora crassa
Harmey, M. A., Hallermayer, G., Korb, H., & Neupert, W. (1977) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1977.tb11979.x · Cited by 120 · see citing works
Uncoupling retro‐translocation and degradation in the ER‐associated degradation of a soluble protein
Lee, R. J., Liu, C., Harty, C., McCracken, A. A., Latterich, M., Römisch, K., Demartino, G., Thomas, P., & Brodsky, J. L. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600232 · Cited by 113 · see citing works
Peroxisomal Membrane Fusion Requires Two Aaa Family Atpases, Pex1p and Pex6p
Titorenko, V. I., & Rachubinski, R. A. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.4.881 · Cited by 113 · see citing works
Signal recognition particle receptor is important for cell growth and protein secretion in Saccharomyces cerevisiae.
Ogg, S. C., Poritz, M. A., & Walter, P. (1992) · Molecular Biology of the Cell · doi:10.1091/mbc.3.8.895 · Cited by 111 · see citing works
The protein translocation channel binds proteasomes to the endoplasmic reticulum membrane
Kalies, K., Allan, S., Sergeyenko, T. V., Kröger, H., & Römisch, K. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600731 · Cited by 110 · see citing works
Energetics of Protein Transport across Biological Membranes
Alder, N. N., & Theg, S. M. (2003) · Cell · doi:10.1016/s0092-8674(03)00032-1 · Cited by 109 · see citing works
Bacterial leader peptidase, a membrane protein without a leader peptide, uses the same export pathway as pre-secretory proteins
Wolfe, P. B., & Wickner, W. T. (1984) · Cell · doi:10.1016/0092-8674(84)90056-4 · Cited by 82 · see citing works
Self-citation
In vivo and in vitro analysis of ptl1, a yeast ts mutant with a membrane‐associated defect in protein translocation.
Toyn, J. H., Hibbs, A. R., Sanz, P., Crowe, J., & Meyer, D. I. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03333.x · Cited by 77 · see citing works
Evaluating the oligomeric state of SecYEG in preprotein translocase
Yahr, T. L., & Wickner, W. T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.16.4393 · Cited by 71 · see citing works
Self-citation
Inactivation of the endoplasmic reticulum protein translocation factor, Sec61p, or its homolog, Ssh1p, does not affect peroxisome biogenesis
South, S. T., Baumgart‐Vogt, E., & Gould, S. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.221289498 · Cited by 59 · see citing works
Structural insight into the protein translocation channel
Clemons, W., Ménétret, J., Akey, C. W., & Rapoport, T. A. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2004.07.006 · Cited by 57 · see citing works
Prepro-carboxypeptidase Y and a truncated form of pre-invertase, but not full-length pre-invertase, can be posttranslationally translocated across microsomal vesicle membranes from Saccharomyces cerevisiae.
Hansen, W., & Walter, P. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.106.4.1075 · Cited by 45 · see citing works
Translocation of a long amino‐terminal domain through ER membrane by following signal‐anchor sequence
Kida, Y., Mihara, K., & Sakaguchi, M. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600788 · Cited by 22 · see citing works
GENETICS AND BIOGENESIS OF CHLOROPLASTS AND
Neupert, W., Sebald, W., & Werner, S. (1976) · Cited by 18 · see citing works

Flagged first, then by citations

Sorted by citations

Importing Mitochondrial Proteins: Machineries and Mechanisms
Chacińska, A., Koehler, C., Milenkovic, D., Lithgow, T., & Pfanner, N. (2009) · Cell · doi:10.1016/j.cell.2009.08.005 · Cited by 1,446 · see citing works
Enzyme–MOF (metal–organic framework) composites
Lian, X., Fang, Y., Joseph, E. A., Wang, Q., Li, J., Banerjee, S., Lollar, C., Wang, X., & Zhou, H.-C. “. (2017) · Chemical Society Reviews · doi:10.1039/c7cs00058h · Cited by 1,391 · see citing works
Autophagy Counterbalances Endoplasmic Reticulum Expansion during the Unfolded Protein Response
Bernales, S., McDonald, K. L., & Walter, P. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040423 · Cited by 1,009 · see citing works
ER stress: Autophagy induction, inhibition and selection
Rashid, H.-O., Yadav, R. K., Kim, H., & Chae, H. (2015) · Autophagy · doi:10.1080/15548627.2015.1091141 · Cited by 796 · see citing works
The endosymbiotic origin, diversification and fate of plastids
Keeling, P. J. (2010) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2009.0103 · Cited by 753 · see citing works
Mistranslation of Membrane Proteins and Two-Component System Activation Trigger Antibiotic-Mediated Cell Death
Kohanski, M. A., Dwyer, D. J., Wierzbowski, J., Cottarel, G., & Collins, J. J. (2008) · Cell · doi:10.1016/j.cell.2008.09.038 · Cited by 576 · see citing works
Intracellular Signaling by the Unfolded Protein Response
Bernales, S., Papa, F. R., & Walter, P. (2006) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.21.122303.120200 · Cited by 543 · see citing works
The GET Complex Mediates Insertion of Tail-Anchored Proteins into the ER Membrane
Schuldiner, M., Metz, J., Schmid, V., Denic, V., Rakwalska, M., Schmitt, H. D., Schwappach, B., & Weissman, J. S. (2008) · Cell · doi:10.1016/j.cell.2008.06.025 · Cited by 522 · see citing works
Synthesis of Silica‐Coated Semiconductor and Magnetic Quantum Dots and Their Use in the Imaging of Live Cells
Selvan, S. T., Patra, P. K., Ang, C. Y., & Ying, J. Y. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200604245 · Cited by 507 · see citing works
The phagosome: compartment with a license to kill
Haas, A. (2007) · Traffic · doi:10.1111/j.1600-0854.2006.00531.x · Cited by 450 · see citing works
Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR.
Gelis, I., Bonvin, A. M. J. J., Keramisanou, D., Koukaki, M., Gouridis, G., Karamanou, S., Economou, A., & Kalodimos, C. G. (2007) · Cell · doi:10.1016/j.cell.2007.09.039 · Cited by 433 · see citing works
Protein localization in disease and therapy
Hung, M., & Link, W. (2011) · Journal of Cell Science · doi:10.1242/jcs.089110 · Cited by 430 · see citing works
Single-Molecule Protein Unfolding in Solid State Nanopores
Talaga, D. S., & Li, J. (2009) · Journal of the American Chemical Society · doi:10.1021/ja901088b · Cited by 414 · see citing works
How Can Proteins Enter the Interior of a MOF? Investigation of Cytochrome c Translocation into a MOF Consisting of Mesoporous Cages with Microporous Windows
Chen, Y., Lykourinou, V., Vetromile, C. M., Hoang, T., Ming, L., Larsen, R. W., & Ma, S. (2012) · Journal of the American Chemical Society · doi:10.1021/ja305144x · Cited by 369 · see citing works
Parallel genomic evolution and metabolic interdependence in an ancient symbiosis
McCutcheon, J. P., & Moran, N. A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708855104 · Cited by 349 · see citing works
The Bacterial Twin-Arginine Translocation Pathway
Lee, P. A., Tullman‐Ercek, D., & Georgiou, G. (2006) · Annual Review of Microbiology · doi:10.1146/annurev.micro.60.080805.142212 · Cited by 348 · see citing works
Roles for Synonymous Codon Usage in Protein Biogenesis
Chaney, J. L., & Clark, P. L. (2015) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-060414-034333 · Cited by 306 · see citing works
Fungal Melanin: What do We Know About Structure?
Nosanchuk, J. D., Stark, R. E., & Casadevall, A. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.01463 · Cited by 310 · see citing works
Unfolding of Proteins and Long Transient Conformations Detected by Single Nanopore Recording
Oukhaled, A., Mathé, J., Biance, A., Bacri, L., Betton, J., Lairez, D., Pelta, J., & Auvray, L. (2007) · Physical Review Letters · doi:10.1103/physrevlett.98.158101 · Cited by 309 · see citing works
Membrane Protein Insertion at the Endoplasmic Reticulum
Shao, S., & Hegde, R. S. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154125 · Cited by 287 · see citing works
Substrate-Specific Translocational Attenuation during ER Stress Defines a Pre-Emptive Quality Control Pathway
Kang, S., Rane, N. S., Kim, S. J., Garrison, J. L., Taunton, J., & Hegde, R. S. (2006) · Cell · doi:10.1016/j.cell.2006.10.032 · Cited by 290 · see citing works
Unraveling the Physiological Complexities of Antibiotic Lethality
Dwyer, D. J., Collins, J. J., & Walker, G. C. (2014) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010814-124712 · Cited by 279 · see citing works
Nitric oxide and mitochondrial biogenesis
Nisoli, E., & Carruba, M. O. (2006) · Journal of Cell Science · doi:10.1242/jcs.03062 · Cited by 278 · see citing works
Characterization of Yeast Extracellular Vesicles: Evidence for the Participation of Different Pathways of Cellular Traffic in Vesicle Biogenesis
Oliveira, D. L., Nakayasu, E. S., Joffe, L. S., Guimaraes, A. J., Sobreira, T. J. P., Nosanchuk, J. D., Cordero, R. J. B., Frasés, S., Casadevall, A., de Almeida, I. C., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011113 · Cited by 268 · see citing works
Rationalizing membrane protein overexpression
Wagner, S., Lerch, M., Drew, D., & Gier, J. D. (2006) · Trends in biotechnology · doi:10.1016/j.tibtech.2006.06.008 · Cited by 272 · see citing works
Mapping the Pathways to StaphylococcalPathogenesis by Comparative Secretomics
Sibbald, M. J. J. B., Ziebandt, A., Engelmann, S., Hecker, M., de Jong, A., Harmsen, H. J. M., Raangs, G. C., Stokroos, I., Arends, J. P., Dubois, J. Y. F., et al. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00008-06 · Cited by 267 · see citing works
Tail-anchored membrane protein insertion into the endoplasmic reticulum
Hegde, R. S., & Keenan, R. J. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3226 · Cited by 258 · see citing works
Characterization of PINK1 processing, stability, and subcellular localization
Lin, W., & Kang, U. J. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05398.x · Cited by 261 · see citing works
Common ground for protein translocation: access control for mitochondria and chloroplasts
Schleiff, E., & Becker, T. (2011) · Nature reviews. Molecular cell biology · doi:10.1038/nrm3027 · Cited by 269 · see citing works
Dynamics of Unfolded Protein Transport through an Aerolysin Pore
Pastoriza‐Gallego, M., Rabah, L., Gibrat, G., Thiébot, B., van der Goot, F. G., Auvray, L., Betton, J., & Pelta, J. (2011) · Journal of the American Chemical Society · doi:10.1021/ja1073245 · Cited by 240 · see citing works
HECTAR: A method to predict subcellular targeting in heterokonts
Gschloessl, B., Guermeur, Y., & Cock, J. M. (2008) · BMC Bioinformatics · doi:10.1186/1471-2105-9-393 · Cited by 237 · see citing works
C-Terminal Signal Sequence Promotes Virulence Factor Secretion in Mycobacterium tuberculosis
Champion, P. A. D., Stanley, S. A., Champion, M. M., Brown, E. J., & Cox, J. S. (2006) · Science · doi:10.1126/science.1131167 · Cited by 219 · see citing works
Stochastic mechano-chemical kinetics of molecular motors: A multidisciplinary enterprise from a physicist’s perspective
Chowdhury, D. (2013) · Physics Reports · doi:10.1016/j.physrep.2013.03.005 · Cited by 218 · see citing works
Polymers and nanoparticles: Intelligent tools for intracellular targeting?
Breunig, M., Bauer, S., & Göpferich, A. M. (2007) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2007.06.010 · Cited by 214 · see citing works
Tim50 Maintains the Permeability Barrier of the Mitochondrial Inner Membrane
Meinecke, M., Wagner, R., Kovermann, P., Guiard, B., Mick, D. U., Hutu, D. P., Voos, W., Truscott, K. N., Chacińska, A., Pfanner, N., et al. (2006) · Science · doi:10.1126/science.1127628 · Cited by 202 · see citing works
Autoubiquitination of the Hrd1 Ligase Triggers Protein Retrotranslocation in ERAD
Baldridge, R. D., & Rapoport, T. A. (2016) · Cell · doi:10.1016/j.cell.2016.05.048 · Cited by 198 · see citing works
Sensing Proteins through Nanopores: Fundamental to Applications
Oukhaled, A., Bacri, L., Pastoriza‐Gallego, M., Betton, J., & Pelta, J. (2012) · ACS Chemical Biology · doi:10.1021/cb300449t · Cited by 198 · see citing works
Motor-free mitochondrial presequence translocase drives membrane integration of preproteins
van der Laan, M., Meinecke, M., Dudek, J., Hutu, D. P., Lind, M., Perschil, I., Guiard, B., Wagner, R., Pfanner, N., & Rehling, P. (2007) · Nature Cell Biology · doi:10.1038/ncb1635 · Cited by 187 · see citing works
Role of the Sec61 Translocon in EGF Receptor Trafficking to the Nucleus and Gene Expression
Liao, H., & Carpenter, G. F. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-09-0802 · Cited by 187 · see citing works
RXLR effectors of plant pathogenic oomycetes
Morgan, W. R., & Kamoun, S. (2007) · Current Opinion in Microbiology · doi:10.1016/j.mib.2007.04.005 · Cited by 178 · see citing works
Quality Control of Orphaned Proteins
Juszkiewicz, S., & Hegde, R. S. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.07.001 · Cited by 165 · see citing works
Formation and function of bacterial organelles
Greening, C., & Lithgow, T. J. (2020) · Nature Reviews Microbiology · doi:10.1038/s41579-020-0413-0 · Cited by 165 · see citing works
Recognition of a Functional Peroxisome Type 1 Target by the Dynamic Import Receptor Pex5p
Stanley, W. A., Filipp, F. V., Kursula, P., Schüller, N., Erdmann, R., Schliebs, W., Sattler, M., & Wilmanns, M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.10.024 · Cited by 169 · see citing works
An energy transduction mechanism used in bacterial flagellar type III protein export
Minamino, T., Morimoto, Y. V., Hara, N., & Namba, K. (2011) · Nature Communications · doi:10.1038/ncomms1488 · Cited by 158 · see citing works
Engineering the Salmonella type III secretion system to export spider silk monomers
Widmaier, D. M., Tullman‐Ercek, D., Mirsky, E. A., Hill, R. M., Govindarajan, S., Minshull, J., & Voigt, C. A. (2009) · Molecular Systems Biology · doi:10.1038/msb.2009.62 · Cited by 156 · see citing works
Selective types of autophagy in yeast.
Kraft, C., Reggiori, F., & Peter, M. (2009) · Biochimica et Biophysica Acta · doi:10.1016/j.bbamcr.2009.02.006 · Cited by 158 · see citing works
Protein Misfolding and Cellular Stress: An Overview
Gregersen, N., & Bross, P. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-756-3_1 · Cited by 155 · see citing works
Crystal structures of the OmpF porin: function in a colicin translocon
Yamashita, E., Zhalnina, M. V., Zakharov, S. D., Sharma, O., & Cramer, W. A. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.137 · Cited by 152 · see citing works
Peroxisomal dynamics
Platta, H. W., & Erdmann, R. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.06.009 · Cited by 152 · see citing works
Protein export through the bacterial flagellar type III export pathway
Minamino, T. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.09.005 · Cited by 151 · see citing works
Protein Transport through a Narrow Solid-State Nanopore at High Voltage: Experiments and Theory
Cressiot, B., Oukhaled, A., Patriarche, G., Pastoriza‐Gallego, M., Betton, J., Auvray, L., Muthukumar, M., Bacri, L., & Pelta, J. (2012) · ACS Nano · doi:10.1021/nn301672g · Cited by 150 · see citing works
Mitochondrial trafficking of APP and alpha synuclein: Relevance to mitochondrial dysfunction in Alzheimer's and Parkinson's diseases
Devi, L., & Anandatheerthavarada, H. K. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.07.007 · Cited by 150 · see citing works
Thermal Unfolding of Proteins Probed at the Single Molecule Level Using Nanopores
Payet, L., Martinho, M., Pastoriza‐Gallego, M., Betton, J., Auvray, L., Pelta, J., & Mathé, J. (2012) · Analytical Chemistry · doi:10.1021/ac300129e · Cited by 149 · see citing works
Structural Basis for Detoxification and Oxidative Stress Protection in Membranes
Holm, P. J., Bhakat, P., Jegerschöld, C., Gyobu, N., Mitsuoka, K., Fujiyoshi, Y., Morgenstern, R., & Hebert, H. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.05.056 · Cited by 147 · see citing works
“Metabolic burden” explained: stress symptoms and its related responses induced by (over)expression of (heterologous) proteins in Escherichia coli
Snoeck, S., Guidi, C., & Mey, M. D. (2024) · Microbial Cell Factories · doi:10.1186/s12934-024-02370-9 · Cited by 145 · see citing works
The glycosidation of xenobiotics and endogenous compounds: Versatility and redundancy in the UDP glycosyltransferase superfamily
Meech, R., Miners, J. O., Lewis, B. C., & Mackenzie, P. I. (2012) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2012.01.009 · Cited by 143 · see citing works
Catalyzing the Translocation of Polypeptides through Attractive Interactions
Wolfe, A. J., Mohammad, Cheley, S., Bayley, H., & Movileanu, L. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0749340 · Cited by 143 · see citing works
Active remodelling of the TIM23 complex during translocation of preproteins into mitochondria
Popov‐Čeleketić, D., Mapa, K., Neupert, W., & Mokranjac, D. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.79 · Cited by 137 · see citing works
Peroxisome biogenesis in mammalian cells
Fujiki, Y., Okumoto, K., Mukai, S., Honsho, M., & Tamura, S. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00307 · Cited by 129 · see citing works
Genetically Programmable Pathogen Sense and Destroy
Gupta, S. K., Bram, E. E., & Weiss, R. (2013) · ACS Synthetic Biology · doi:10.1021/sb4000417 · Cited by 134 · see citing works
Delivery of drugs and macromolecules to the mitochondria for cancer therapy
Lu, P., Bruno, B. J., Rabenau, M., & Lim, C. S. (2015) · Journal of Controlled Release · doi:10.1016/j.jconrel.2015.10.023 · Cited by 131 · see citing works
Engineering a Rigid Protein Tunnel for Biomolecular Detection
Mohammad, M. M., Iyer, R., Howard, K. R., McPike, M. P., Borer, P. N., & Movileanu, L. (2012) · Journal of the American Chemical Society · doi:10.1021/ja3043646 · Cited by 128 · see citing works
Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers
Feld, G. K., Thoren, K. L., Kintzer, A. F., Sterling, H. J., Tang, I. I., Greenberg, S. G., Williams, E. R., & Krantz, B. A. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1923 · Cited by 120 · see citing works
Protein Secretion and Membrane Insertion Systems in Gram-Negative Bacteria
Saier, M. H. (2006) · The Journal of Membrane Biology · doi:10.1007/s00232-006-0049-7 · Cited by 121 · see citing works
Controlling a Single Protein in a Nanopore through Electrostatic Traps
Mohammad, Prakash, S., Matouschek, A. T., & Movileanu, L. (2008) · Journal of the American Chemical Society · doi:10.1021/ja710787a · Cited by 118 · see citing works
Synthesis of Silica‐Coated Semiconductor and Magnetic Quantum Dots and Their Use in the Imaging of Live Cells
Selvan, S. T., Patra, P. K., Ang, C. Y., & Ying, J. Y. (2007) · Angewandte Chemie · doi:10.1002/ange.200604245 · Cited by 117 · see citing works
LOXL2 drives epithelial-mesenchymal transition via activation of IRE1-XBP1 signalling pathway
Cuevas, E. P., Eraso, P., Mazón, M. J., Santos, V., Moreno‐Bueno, G., Cano, A., & Portillo, F. (2017) · Scientific Reports · doi:10.1038/srep44988 · Cited by 116 · see citing works
The role of ATP-binding cassette transporters in bacterial pathogenicity
Lewis, V. G., Ween, M. P., & McDevitt, C. A. (2012) · PROTOPLASMA · doi:10.1007/s00709-011-0360-8 · Cited by 110 · see citing works
Detecting Folding Intermediates of a Protein as It Passes through the Bacterial Translocation Channel
Kadokura, H., & Beckwith, J. (2009) · Cell · doi:10.1016/j.cell.2009.07.030 · Cited by 113 · see citing works
Mechanism of Threading a Polymer Through a Macrocyclic Ring
Deutman, A. B. C., Monnereau, C., Elemans, J. A. A. W., Ercolani, G., Nolte, R. J. M., & Rowan, A. E. (2008) · Science · doi:10.1126/science.1164647 · Cited by 113 · see citing works
On the mechanism of preprotein import by the mitochondrial presequence translocase.
van der Laan, M., Hutu, D., & Rehling, P. (2010) · Biochimica et Biophysica Acta · doi:10.1016/j.bbamcr.2010.01.013 · Cited by 114 · see citing works
The peroxisomal protein import machinery
Platta, H. W., & Erdmann, R. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.04.001 · Cited by 110 · see citing works
Protein Delivery into the Cell Cytosol using Non-Viral Nanocarriers
Lee, Y.-W., Luther, D. C., Kretzmann, J. A., Burden, A., Jeon, T., Zhai, S., & Rotello, V. M. (2019) · Theranostics · doi:10.7150/thno.34412 · Cited by 107 · see citing works
Vesicular Trans-Cell Wall Transport in Fungi: A Mechanism for the Delivery of Virulence-Associated Macromolecules?
Rodrigues, M. L., Nimrichter, L., Oliveira, D. L., Nosanchuk, J. D., & Casadevall, A. (2008) · Lipid Insights · doi:10.4137/lpi.s1000 · Cited by 108 · see citing works
Interaction mapping of endoplasmic reticulum ubiquitin ligases identifies modulators of innate immune signalling
Fenech, E. J., Lari, F., Charles, P. D., Fischer, R., Laétitia-Thézénas, M., Bagola, K., Paton, A. W., Paton, J. C., Gyrd‐Hansen, M., Kessler, B. M., et al. (2020) · eLife · doi:10.7554/elife.57306 · Cited by 104 · see citing works
RNA localization: Making its way to the center stage
Chin, A., & Lécuyer, É. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.06.011 · Cited by 103 · see citing works
Tim50’s presequence receptor domain is essential for signal driven transport across the TIM23 complex
Schulz, C., Lytovchenko, O., Melin, J., Chacińska, A., Guiard, B., Neumann, P., Ficner, R., Jahn, O., Schmidt, B., & Rehling, P. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201105098 · Cited by 101 · see citing works
Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks
Csermely, P., & VÃgh, L. (2007) · Springer eBooks · doi:10.1007/978-0-387-39975-1 · Cited by 99 · see citing works
Protein mislocalization: Mechanisms, functions and clinical applications in cancer
Wang, X., & Li, S. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.03.006 · Cited by 97 · see citing works
Attenuation of yeast UPR is essential for survival and is mediated by IRE1 kinase
Chawla, A., Chakrabarti, S., Ghosh, G., & Niwa, M. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201008071 · Cited by 96 · see citing works
The TIC complex uncovered: The alternative view on the molecular mechanism of protein translocation across the inner envelope membrane of chloroplasts
Nakai, M. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.02.011 · Cited by 88 · see citing works
Spatial association with PTEX complexes defines regions for effector export into Plasmodium falciparum-infected erythrocytes
Riglar, D. T., Rogers, K. L., Hanssen, E. G., Turnbull, L., Bullen, H. E., Charnaud, S. C., Przyborski, J. M., Gilson, P. R., Whitchurch, C. B., Crabb, B. S., et al. (2013) · Nature Communications · doi:10.1038/ncomms2449 · Cited by 92 · see citing works
Toc64 - A Preprotein-receptor at the Outer Membrane with Bipartide Function
Qbadou, S., Becker, T., Bionda, T., Reger, K., Ruprecht, M., Soll, J., & Schleiff, E. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.01.047 · Cited by 92 · see citing works
Versatility of Preprotein Transfer from the Cytosol to Mitochondria.
Becker, T., Song, J., & Pfanner, N. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.03.007 · Cited by 79 · see citing works
The Rate of Folding Dictates Substrate Secretion by the Escherichia coli Hemolysin Type 1 Secretion System
Bakkes, P. J., Jenewein, S., Smits, S. H. J., Holland, I. B., & Schmitt, L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.173658 · Cited by 91 · see citing works
Identification of Functional Tat Signal Sequences in Mycobacterium tuberculosis Proteins
McDonough, J. A., McCann, J. R., McElvania, E., Silverman, J. S., Rigel, N. W., & Braunstein, M. (2008) · Journal of Bacteriology · doi:10.1128/jb.00749-08 · Cited by 91 · see citing works
The process of folding proteins into membranes: Challenges and progress
Stanley, A. M., & Fleming, K. G. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.09.024 · Cited by 87 · see citing works
Folding at the rhythm of the rare codon beat
Marı́n, M. (2008) · Biotechnology Journal · doi:10.1002/biot.200800089 · Cited by 87 · see citing works
Comprehensive proteomic profiling of outer membrane vesicles from Campylobacter jejuni
Jang, K., Sweredoski, M. J., Graham, R. L. J., Hess, S. Y., & Clemons, W. (2014) · Journal of Proteomics · doi:10.1016/j.jprot.2013.12.014 · Cited by 86 · see citing works
KLF7 promotes pancreatic cancer growth and metastasis by up-regulating ISG expression and maintaining Golgi complex integrity
Gupta, R., Malvi, P., Parajuli, K. R., Janoštiak, R., Bugide, S., Cai, G., Zhu, L. J., Green, M. R., & Wajapeyee, N. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2005156117 · Cited by 85 · see citing works
Substrate-specific mediators of ER associated degradation (ERAD)
Brodsky, J. L., & Wojcikiewicz, R. J. H. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.04.006 · Cited by 82 · see citing works
Squeezing a single polypeptide through a nanopore
Movileanu, L. (2008) · Soft Matter · doi:10.1039/b719850g · Cited by 81 · see citing works
Curli Biogenesis: Bacterial Amyloid Assembly by the Type VIII Secretion Pathway
Bhoite, S. S., Gerven, N. V., Chapman, M. R., & Remaut, H. K. (2019) · EcoSal Plus · doi:10.1128/ecosalplus.esp-0037-2018 · Cited by 80 · see citing works
Independent gene duplications of the YidC/Oxa/Alb3 family enabled a specialized cotranslational function
Funes, S., Hasona, A., Bauerschmitt, H., Grubbauer, C., Kauff, F., Collins, R., Crowley, P. J., Palmer, S. R., Brady, L. J., & Herrmann, J. M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809951106 · Cited by 78 · see citing works
Excursion of a single polypeptide into a protein pore: simple physics, but complicated biology
Mohammad, M. M., & Movileanu, L. (2008) · European Biophysics Journal · doi:10.1007/s00249-008-0309-9 · Cited by 76 · see citing works
Nuclear EGFR as Novel Therapeutic Target
Dittmann, K., Mayer, C., & Rodemann, H. P. (2009) · Strahlentherapie und Onkologie · doi:10.1007/s00066-009-2026-4 · Cited by 76 · see citing works
Traffic-related particulate matter exposure induces nephrotoxicity in vitro and in vivo
Hsu, Y., Chuang, H., Lee, Y., Lin, Y., Chen, Y.-J., Hsiao, T.-C., Wu, M., & Chiu, H. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.03.008 · Cited by 74 · see citing works
Glycosylation of glycolipids in the Golgi complex
Maccioni, H. J. F. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04717.x · Cited by 72 · see citing works
Structural analysis of the Sil1–Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factor
Yan, M., Li, J., & Sha, B. (2011) · Biochemical Journal · doi:10.1042/bj20110500 · Cited by 71 · see citing works
Life and times: synthesis, trafficking, and evolution of VSG
Manna, P. T., Boehm, C., Leung, K. F., Natesan, S. K. A., & Field, M. C. (2014) · Trends in Parasitology · doi:10.1016/j.pt.2014.03.004 · Cited by 70 · see citing works

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

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks