Shan, Shu-ou

Combined from CaltechAUTHORS

• Cho, Hyunju and Liu, Yumeng, et el. (2024) Dynamic stability of Sgt2 enables selective and privileged client handover in a chaperone triad; Nature Communications; Vol. 15; 134; PMCID PMC10761869; 10.1038/s41467-023-44260-5
• Gupta, Arpit and Lentzsch, Alfred M., et el. (2023) Dodecamer assembly of a metazoan AAA⁺ chaperone couples substrate extraction to refolding; Science Advances; Vol. 9; No. 19; Art. No. eadf5336; PMCID PMC10171807; 10.1126/sciadv.adf5336
• Shan, Shu-ou (2023) Role of Hsp70 in Post-Translational Protein Targeting: Tail-Anchored Membrane Proteins and Beyond; International Journal of Molecular Sciences; Vol. 24; No. 2; Art. No. 1170; PMCID PMC9866221; 10.3390/ijms24021170
• Yang, Chien-I and Zhu, Zikun, et el. (2022) System-wide analyses reveal essential roles of N-terminal protein modification in bacterial membrane integrity; iScience; Vol. 25; No. 8; Art. No. 104756; PMCID PMC9356101; 10.1016/j.isci.2022.104756
• Zhu, Zikun and Wang, Shuai, et el. (2022) Ribosome profiling reveals multiple roles of SecA in cotranslational protein export; Nature Communications; Vol. 13; Art. No. 3393; PMCID PMC9192764; 10.1038/s41467-022-31061-5
• Yang, Chien-I and Kim, Jiwoo, et el. (2022) Ribosome-nascent Chain Interaction Regulates N-terminal Protein Modification; Journal of Molecular Biology; Vol. 434; No. 9; Art. No. 167535; PMCID PMC9126151; 10.1016/j.jmb.2022.167535
• Jomaa, Ahmad and Gamerdinger, Martin, et el. (2022) Mechanism of signal sequence handover from NAC to SRP on ribosomes during ER-protein targeting; Science; Vol. 375; No. 6583; 839-844; PMCID PMC7612438; 10.1126/science.abl6459
• Hsieh, Hao-Hsuan and Shan, Shu-ou (2022) Fidelity of Cotranslational Protein Targeting to the Endoplasmic Reticulum; International Journal of Molecular Sciences; Vol. 23; No. 1; Art. No. 281; PMCID PMC8745203; 10.3390/ijms23010281
• Chio, Un Seng and Liu, Yumeng, et el. (2021) Subunit cooperation in the Get1/2 receptor promotes tail-anchored membrane protein insertion; Journal of Cell Biology; Vol. 220; No. 11; Art. No. e202103079; 10.1083/jcb.202103079
• Ji, Shuiling and Siegel, Alex, et el. (2021) Chloroplast SRP43 autonomously protects chlorophyll biosynthesis proteins against heat shock; Nature Plants; Vol. 7; No. 10; 1420-1432; PMCID PMC8879858; 10.1038/s41477-021-00994-y
• Jomaa, Ahmad and Eitzinger, Simon, et el. (2021) Molecular mechanism of cargo recognition and handover by the mammalian signal recognition particle; Cell Reports; Vol. 36; No. 2; Art. No. 109350; PMCID PMC8330425; 10.1016/j.celrep.2021.109350
• Lee, Jae Ho and Jomaa, Ahmad, et el. (2021) Receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER; Science Advances; Vol. 7; No. 21; Art. No. eabg0942; PMCID PMC8139590; 10.1126/sciadv.abg0942
• Cho, Hyunju and Shim, Woo Jun, et el. (2021) J-domain proteins promote client relay from Hsp70 during tail-anchored membrane protein targeting; Journal of Biological Chemistry; Vol. 296; Art. No. 100546; 10.1016/j.jbc.2021.100546
• Siegel, Alex and McAvoy, Camille Z., et el. (2020) A Disorder-to-Order Transition Activates an ATP-Independent Membrane Protein Chaperone; Journal of Molecular Biology; Vol. 432; No. 24; Art. No. 166708; PMCID PMC7780713; 10.1016/j.jmb.2020.11.007
• Hsieh, Hao-Hsuan and Lee, Jae Ho, et el. (2020) A ribosome-associated chaperone enables substrate triage in a cotranslational protein targeting complex; Nature Communications; Vol. 11; Art. No. 5840; PMCID PMC7673040; 10.1038/s41467-020-19548-5
• Shan, Shu-ou and Wang, Shuai, et el. (2020) Nascent Protein Selection and Triage at the Ribosome Exit Site; FASEB Journal; Vol. 34; No. S1; 1-1; 10.1096/fasebj.2020.34.s1.00156
• Yang, Chien-I and Hsieh, Hao-Hsuan, et el. (2020) Timing and Specificity of Cotranslational Nascent Protein Modification in Bacteria; FASEB Journal; Vol. 34; No. S1; 1; 10.1096/fasebj.2020.34.s1.04322
• Yang, Chien-I and Hsieh, Hao-Hsuan, et el. (2019) Timing and specificity of cotranslational nascent protein modification in bacteria; Proceedings of the National Academy of Sciences of the United States of America; Vol. 116; No. 46; 23050-23060; PMCID PMC6859321; 10.1073/pnas.1912264116
• Shan, Shu-ou (2019) Guiding tail-anchored membrane proteins to the endoplasmic reticulum in a chaperone cascade; Journal of Biological Chemistry; Vol. 294; No. 45; 16577-16586; PMCID PMC6851334; 10.1074/jbc.rev119.006197
• Hwang Fu, Yu-Hsien and Chandrasekar, Sowmya, et el. (2019) A molecular recognition feature mediates ribosome-induced SRP-receptor assembly during protein targeting; Journal of Cell Biology; Vol. 218; No. 10; 3307-3319; PMCID PMC6781444; 10.1083/jcb.201901001
• Wang, Shuai and Jomaa, Ahmad, et el. (2019) The molecular mechanism of cotranslational membrane protein recognition and targeting by SecA; Nature Structural & Molecular Biology; Vol. 26; No. 10; 919-929; PMCID PMC6858539; 10.1038/s41594-019-0297-8
• Chio, Un Seng and Chung, SangYoon, et el. (2019) A Chaperone Lid Ensures Efficient and Privileged Client Transfer during Tail-Anchored Protein Targeting; Cell Reports; Vol. 26; No. 1; 37-44; PMCID PMC6689467; 10.1016/j.celrep.2018.12.035
• Cho, Hyunju and Chio, Un Seng, et el. (2018) In vitro Assays for Targeting and Insertion of Tail‐Anchored Proteins Into the ER Membrane; Current Protocols in Cell Biology; Vol. 81; No. 1; Art. No. e63; PMCID PMC6263799; 10.1002/cpcb.63
• Cho, Hyunju and Shan, Shu-ou (2018) Substrate relay in an Hsp70‐cochaperone cascade safeguards tail‐anchored membrane protein targeting; EMBO Journal; Vol. 37; No. 16; Art. No. e99264; PMCID PMC6092619; 10.15252/embj.201899264
• Lee, Jae Ho and Chandrasekar, Sowmya, et el. (2018) Sequential activation of human signal recognition particle by the ribosome and signal sequence drives efficient protein targeting; Proceedings of the National Academy of Sciences of the United States of America; Vol. 115; No. 24; E5487-E5496; PMCID PMC6004459; 10.1073/pnas.1802252115
• McAvoy, Camille and Siegel, Alex, et el. (2018) Two Distinct Sites of client protein interaction with the chaperone cpSRP43; Journal of Biological Chemistry; Vol. 293; No. 23; 8861-8873; PMCID PMC5995501; 10.1074/jbc.RA118.002215
• Kobayashi, Kan and Jomaa, Ahmad, et el. (2018) Structure of a prehandover mammalian ribosomal SRP•SRP receptor targeting complex; Science; Vol. 360; No. 6386; 323-327; PMCID PMC6309883; 10.1126/science.aar7924
• Wang, Peng and Liang, Fu-Cheng, et el. (2018) Chloroplast SRP43 acts as a chaperone for glutamyl-tRNA reductase, the rate-limiting enzyme in tetrapyrrole biosynthesis; Proceedings of the National Academy of Sciences of the United States of America; Vol. 115; No. 15; E3588-E3596; PMCID PMC5899456; 10.1073/pnas.1719645115
• Fu, Yu-Hsien Hwang and Huang, William Y. C., et el. (2018) Two-Step Membrane Binding by the Bacterial SRP Receptor Enables Efficient and Accurate Co-Translational Protein Targeting; Biophysical Journal; Vol. 114; No. 3; 209A; 10.1016/j.bpj.2017.11.1170
• Hsieh, Hao Hsuan and Shan, Shu-ou (2018) Co-translational Targeting by Signal Recognition Particle Activates Only after Cytosolic Exposure of Signal Sequence; Biophysical Journal; Vol. 114; No. 3; 69a; 10.1016/j.bpj.2017.11.425
• Shan, Shu-ou and Chio, Un Seng (2018) A Protean Clamp Guides Membrane Targeting of Tail-Anchored Proteins; Biophysical Journal; Vol. 114; No. 3; 553a; 10.1016/j.bpj.2017.11.3022
• McAvoy, Camille and Liang, Fu-Cheng, et el. (2017) Dynamics of Membrane Protein-Chaperone Interaction; Protein Science; Vol. 26; No. S1; 29-30; 10.1002/pro.3349
• Wang, Shuai and Yang, Chien-I, et el. (2017) SecA mediates cotranslational targeting and translocation of an inner membrane protein; Journal of Cell Biology; Vol. 216; No. 11; 3639-3653; PMCID PMC5674894; 10.1083/jcb.201704036
• Chio, Un Seng and Chung, SangYoon, et el. (2017) A protean clamp guides membrane targeting of tail-anchored proteins; Proceedings of the National Academy of Sciences of the United States of America; Vol. 114; No. 41; E8585-E8594; PMCID PMC5642712; 10.1073/pnas.1708731114
• Chio, Un Seng and Cho, Hyunjun, et el. (2017) Mechanisms of Tail-Anchored Membrane Protein Targeting and Insertion; Annual Review of Cell and Developmental Biology; Vol. 33; 417-438; PMCID PMC6343671; 10.1146/annurev-cellbio-100616-060839
• Fu, Yu-Hsien Hwang and Huang, William Y. C., et el. (2017) Two-step membrane binding by the bacterial SRP receptor enable efficient and accurate Co-translational protein targeting; eLife; Vol. 6; Art. No. e25885; PMCID PMC5533587; 10.7554/eLife.25885
• Jomaa, Ahmad and Fu, Yu-Hsien Hwang, et el. (2017) Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome; Nature Communications; Vol. 8; Art. No. 15470; PMCID PMC5454536; 10.1038/ncomms15470
• Chandrasekar, Sowmya and Sweredoski, Michael J., et el. (2017) Co-evolution of two GTPases enables efficient protein targeting in an RNA-less chloroplast Signal Recognition Particle pathway; Journal of Biological Chemistry; Vol. 292; No. 1; 386-396; PMCID PMC5217696; 10.1074/jbc.M116.752931
• Chandrasekar, Sowmya and Shan, Shu-ou (2017) Anionic Phospholipids and the Albino3 Translocase Activate Signal Recognition Particle-Receptor Interaction during Light-harvesting Chlorophyll a/b-binding Protein Targeting; Journal of Biological Chemistry; Vol. 292; No. 1; 397-406; PMCID PMC5217697; 10.1074/jbc.M116.752956
• Rao, Meera and Okreglak, Voytek, et el. (2016) Multiple selection filters ensure accurate tail-anchored membrane protein targeting; eLife; Vol. 5; Art. No. e21301; PMCID PMC5214336; 10.7554/eLife.21301
• Shan, Shu-ou (2016) ATPase and GTPase Tangos Drive Intracellular Protein Transport; Trends in Biochemical Sciences; Vol. 41; No. 12; 1050-1060; PMCID PMC5627767; 10.1016/j.tibs.2016.08.012
• Chen, Yang and Shen, Kuang, et el. (2016) Analyzing Single-Molecule Protein Transportation Experiments via Hierarchical Hidden Markov Models; Journal of the American Statistical Association; Vol. 111; No. 515; 951-966; PMCID PMC5606165; 10.1080/01621459.2016.1140050
• Liu, Wenpeng and Zhou, Mian, et el. (2016) A Selective Small Molecule DNA2 Inhibitor for Sensitization of Human Cancer Cells to Chemotherapy; EBioMedicine; Vol. 6; 73-86; PMCID PMC4856754; 10.1016/j.ebiom.2016.02.043
• Liang, Fu-Cheng and Kroon, Gerard, et el. (2016) Conformational dynamics of a membrane protein chaperone enables spatially regulated substrate capture and release; Proceedings of the National Academy of Sciences of the United States of America; Vol. 113; No. 12; E1615-E1624; PMCID PMC4812700; 10.1073/pnas.1524777113
• Wang, Connie and Wang, Shuai, et el. (2016) Inversion of Signal Sequence Topology during Membrane Integration; Biophysical Journal; Vol. 110; No. 3; 226A-227A; 10.1016/j.bpj.2015.11.1252
• Gristick, Harry B. and Rome, Michael E., et el. (2015) Mechanism of assembly of a substrate-transfer complex during tail-anchored protein targeting; Journal of Biological Chemistry; Vol. 290; No. 50; 30006-30017; PMCID PMC4705998; 10.1074/jbc.M115.677328
• Ariosa, Aileen and Lee, Jae Ho, et el. (2015) Regulation by a chaperone improves substrate selectivity during cotranslational protein targeting; Proceedings of the National Academy of Sciences of the United States of America; Vol. 112; No. 25; E3169-E3178; PMCID PMC4485088; 10.1073/pnas.1422594112
• von Loeffelholz, Ottilie and Jiang, Qiyang, et el. (2015) Ribosome–SRP–FtsY cotranslational targeting complex in the closed state; Proceedings of the National Academy of Sciences of the United States of America; Vol. 112; No. 13; 3943-3948; PMCID PMC4386334; 10.1073/pnas.1424453112
• Fu, Yu-Hsien Hwang and Shan, Shu-ou (2015) Distinct Membrane Association Modes Facilitate Co-Translational Protein Targeting; Biophysical Journal; Vol. 108; No. 2; 253A; 10.1016/j.bpj.2014.11.1401
• Liang, Fu-Cheng and McAvoy, Camille, et el. (2015) Inter-Domain Dynamics of a Novel Chaperone Enables Effective Capture of Membrane Protein Substrates; Biophysical Journal; Vol. 108; No. 2; 53a; 10.1016/j.bpj.2014.11.323
• Rome, Michael E. and Chio, Un Seng, et el. (2014) Differential gradients of interaction affinities drive efficient targeting and recycling in the GET pathway; Proceedings of the National Academy of Sciences of the United States of America; Vol. 111; No. 46; E4929-E4935; PMCID PMC4246279; 10.1073/pnas.1411284111
• Saraogi, Ishu and Shan, Shu-ou (2014) Co-translational protein targeting to the bacterial membrane; Biochimica et Biophysica Acta - Molecular Cell Research; Vol. 1843; No. 8; 1433-1441; PMCID PMC3999308; 10.1016/j.bbamcr.2013.10.013
• Saraogi, Ishu and Akopian, David, et el. (2014) Regulation of cargo recognition, commitment, and unloading drives cotranslational protein targeting; Journal of Cell Biology; Vol. 205; No. 5; 693-706; PMCID PMC4050729; 10.1083/jcb.201311028
• Guo, Huan and Xiong, Yi, et el. (2014) Inefficient Translocation of Preproinsulin Contributes to Pancreatic β Cell Failure and Late-onset Diabetes; Journal of Biological Chemistry; Vol. 289; No. 23; 16290-16302; PMCID PMC4047398; 10.1074/jbc.M114.562355
• Gristick, Harry B. and Rao, Meera, et el. (2014) Crystal structure of ATP-bound Get3–Get4–Get5 complex reveals regulation of Get3 by Get4; Nature Structural & Molecular Biology; Vol. 21; No. 5; 437-442; PMCID PMC4386898; 10.1038/nsmb.2813
• Zhang, Xin and Shan, Shu-ou (2014) Fidelity of Cotranslational Protein Targeting by the Signal Recognition Particle; Annual Review of Biophysics; Vol. 43; 381-408; PMCID PMC4444370; 10.1146/annurev-biophys-051013-022653
• Losn, Oliver and Rome, Michael, et el. (2014) Regulation of mitochondrial fission by MiD51; FASEB Journal; Vol. 28; No. 1; 757.1
• Gristick, Harry and Rao, Meera, et el. (2014) The structure of a tail-anchor membrane protein-binding complex reveals the regulation of Get3 by Get4; FASEB Journal; Vol. 28; No. 1; Art. No. 950.4
• Losón, Oliver C. and Liu, Raymond, et el. (2014) The Mitochondrial Fission Receptor MiD51 Requires ADP as a Cofactor; Structure; Vol. 22; No. 3; 367-377; PMCID PMC4066849; 10.1016/j.str.2014.01.001
• Shen, Kuang and Wang, Yaqiang, et el. (2013) Molecular Mechanism of GTPase Activation at the Signal Recognition Particle (SRP) RNA Distal End; Journal of Biological Chemistry; Vol. 288; No. 51; 36385-36397; PMCID PMC3868752; 10.1074/jbc.M113.513614
• Voigts-Hoffmann, Felix and Schmitz, Nikolaus, et el. (2013) The Structural Basis of FtsY Recruitment and GTPase Activation by SRP RNA; Molecular Cell; Vol. 52; No. 5; 643-654; PMCID PMC3910249; 10.1016/j.molcel.2013.10.005
• Akopian, David and Shen, Kuang, et el. (2013) Signal Recognition Particle: An Essential Protein-Targeting Machine; Annual Review of Biochemistry; Vol. 82; 693-721; PMCID PMC3805129; 10.1146/annurev-biochem-072711-164732
• Nguyen, Thang X. and Jaru-Ampornpan, Peera, et el. (2013) Mechanism of an ATP-independent Protein Disaggregase - I. Structure of a Membrane Protein Aggregate Reveals a Mechanism of Recognition by its Chaperone; Journal of Biological Chemistry; Vol. 288; No. 19; 13420-13430; PMCID PMC3650380; 10.1074/jbc.M113.462812
• Jaru-Ampornpan, Peera and Liang, Fu-Cheng, et el. (2013) Mechanism of an ATP-independent Protein Disaggregase. II. Distinct Molecular Interactions Drive Multiple Steps During Aggregate Disassembly; Journal of Biological Chemistry; Vol. 288; No. 19; 13431-13445; PMCID PMC3650381; 10.1074/jbc.M113.462861
• Rome, Michael E. and Rao, Meera, et el. (2013) Precise timing of ATPase activation drives targeting of tail-anchored proteins; Proceedings of the National Academy of Sciences of the United States of America; Vol. 110; No. 19; 7666-7671; PMCID PMC3651441; 10.1073/pnas.1222054110
• von Loeffelholz, Ottilie and Knoops, Kèvin, et el. (2013) Structural basis of signal sequence surveillance and selection by the SRP–FtsY complex; Nature Structural & Molecular Biology; Vol. 20; No. 5; 604-610; PMCID PMC3874396; 10.1038/nsmb.2546
• Rome, Michael and Shan, Shu-ou (2013) The ATPase Cycle of the Tail-Anchored Protein Chaperone Get3; FASEB Journal; Vol. 27; Art. No. 542.4
• Shan, Shu-ou (2013) GTPase and ATPase tangos during intracellular protein targeting; FASEB Journal; Vol. 27; Art. No. 198.1
• Shen, Kuang and Arslan, Sinan, et el. (2013) Activated GTPase movement on an RNA scaffold drives cotranslational protein targeting; FASEB Journal; Vol. 27; Art. No. 556.3
• Pierce, Nathan W. and Lee, J. Eugene, et el. (2013) Cand1 Promotes Assembly of New SCF Complexes through Dynamic Exchange of F Box Proteins; Cell; Vol. 153; No. 1; 206-215; PMCID PMC3656483; 10.1016/j.cell.2013.02.024
• Akopian, David and Dalal, Kush, et el. (2013) SecYEG activates GTPases to drive the completion of cotranslational protein targeting; Journal of Cell Biology; Vol. 200; No. 4; 397-405; PMCID PMC3575545; 10.1083/jcb.201208045
• Shen, Kuang and Arslan, Sinan, et el. (2013) Activated GTPase Movement on SRP RNA Drives Cotranslational Protein Targeting; Biophysical Journal; Vol. 104; No. 2; 419A; 10.1016/j.bpj.2012.11.2334
• Rao, Meera and Rome, Michael E., et el. (2013) Precise Timing of ATPase Activation Drives Targeting of Tail-Anchored Proteins; Biophysical Journal; Vol. 104; No. 2; 572A; 10.1016/j.bpj.2012.11.3178
• Ariosa, Aileen R. and Duncan, Stacy S., et el. (2013) Fingerloop activates cargo delivery and unloading during cotranslational protein targeting; Molecular Biology of the Cell; Vol. 24; No. 2; 63-73; PMCID PMC3541965; 10.1091/mbc.E12-06-0434
• Shen, Kuang and Arslan, Sinan, et el. (2012) Activated GTPase movement on an RNA scaffold drives co-translational protein targeting; Nature; Vol. 492; No. 7428; 271-275; PMCID PMC3531814; 10.1038/nature11726
• Liu, Ming and Lara-Lemus, Roberto, et el. (2012) Impaired Cleavage of Preproinsulin Signal Peptide Linked to Autosomal-Dominant Diabetes; Diabetes; Vol. 61; No. 4; 828-837; PMCID PMC3314357; 10.2337/db11-0878
• Lu, Zeyu Mike and Chandrasekar, Sowmya, et el. (2012) The cpSRP54-cpFtsY Interaction in the Chloroplast SRP Pathway; FASEB Journal; Vol. 26; Art. No. 973.3
• Zhang, Dawei and Shan, Shu-ou (2012) Translation Elongation Regulates Substrate Selection by the Signal Recognition Particle; Journal of Biological Chemistry; Vol. 287; No. 10; 7652-7660; PMCID PMC3293578; 10.1074/jbc.M111.325001
• Zhang, Dawei and Sweredoski, Michael J., et el. (2012) Novel Proteomic Tools Reveal Essential Roles of SRP and Importance of Proper Membrane Protein Biogenesis; Molecular and Cellular Proteomics; Vol. 11; No. 2; Art. No. M111.011585; PMCID PMC3277757; 10.1074/mcp.M111.011585
• Saraogi, Ishu and Akopian, David, et el. (2011) A tale of two GTPases in cotranslational protein targeting; Protein Science; Vol. 20; No. 11; 1790-1795; PMCID PMC3267943; 10.1002/pro.729
• Saraogi, Ishu and Zhang, Dawei, et el. (2011) Site-Specific Fluorescent Labeling of Nascent Proteins on the Translating Ribosome; Journal of the American Chemical Society; Vol. 133; No. 38; 14936-14939; PMCID PMC3189723; 10.1021/ja206626g
• Nguyen, Thang X. and Chandrasekar, Sowmya, et el. (2011) Concerted Complex Assembly and GTPase Activation in the Chloroplast Signal Recognition Particle; Biochemistry; Vol. 50; No. 33; 7208-7217; PMCID PMC6309729; 10.1021/bi200742a
• Shen, Kuang and Zhang, Xin, et el. (2011) Synergistic actions between the SRP RNA and translating ribosome allow efficient delivery of the correct cargos during cotranslational protein targeting; RNA; Vol. 17; No. 5; 892-902; PMCID PMC3078738; 10.1261/rna.2610411
• Saraogi, Ishu and Shan, Shu-ou (2011) Molecular Mechanism of Co-translational Protein Targeting by the Signal Recognition Particle; Traffic; Vol. 12; No. 5; 535-542; PMCID PMC3077218; 10.1111/j.1600-0854.2011.01171.x
• Zhang, Xin and Lam, Vinh Q., et el. (2011) Direct visualization reveals dynamics of a transient intermediate during protein assembly; Proceedings of the National Academy of Sciences of the United States of America; Vol. 108; No. 16; 6450-6455; PMCID PMC3081034; 10.1073/pnas.1019051108
• Ataide, Sandro F. and Schmitz, Nikolaus, et el. (2011) The Crystal Structure of the Signal Recognition Particle in Complex with Its Receptor; Science; Vol. 331; No. 6019; 881-886; PMCID PMC3758919; 10.1126/science.1196473
• Estrozi, Leandro F. and Boehringer, Daniel, et el. (2011) Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor; Nature Structural & Molecular Biology; Vol. 18; No. 1; 88-90; PMCID PMC3764645; 10.1038/nsmb.1952
• Lam, Vinh Q. and Akopian, David, et el. (2010) Lipid activation of the signal recognition particle receptor provides spatial coordination of protein targeting; Journal of Cell Biology; Vol. 190; No. 4; 623-635; PMCID PMC2928010; 10.1083/jcb.201004129
• Jaru-Ampornpan, Peera and Shen, Kuang, et el. (2010) ATP-independent reversal of a membrane protein aggregate by a chloroplast SRP subunit; Nature Structural & Molecular Biology; Vol. 17; No. 6; 696-703; PMCID PMC2917185; 10.1038/nsmb.1836
• Zhang, Xin and Rashid, Rumana, et el. (2010) Sequential Checkpoints Govern Substrate Selection During Cotranslational Protein Targeting; Science; Vol. 328; No. 5979; 757-760; PMCID PMC3760334; 10.1126/science.1186743
• Shen, Kuang and Shan, Shu-ou (2010) Transient tether between the SRP RNA and SRP receptor ensures efficient cargo delivery during cotranslational protein targeting; Proceedings of the National Academy of Sciences of the United States of America; Vol. 107; No. 17; 7698-7703; PMCID PMC2867919; 10.1073/pnas.1002968107
• Pierce, Nathan W. and Kleiger, Gary, et el. (2009) Detection of sequential polyubiquitylation on a millisecond timescale; Nature; Vol. 462; No. 7273; 615-620; PMCID PMC2791906; 10.1038/nature08595
• Jaru-Ampornpan, Peera and Nguyen, Thang X., et el. (2009) A Distinct Mechanism to Achieve Efficient Signal Recognition Particle (SRP)-SRP Receptor Interaction by the Chloroplast SRP Pathway; Molecular Biology of the Cell; Vol. 20; No. 17; 3965-3973; PMCID PMC2735494; 10.1091/mbc.E08-10-0989
• Shan, Shu-ou and Schmid, Sandra L., et el. (2009) Signal Recognition Particle (SRP) and SRP Receptor: A New Paradigm for Multistate Regulatory GTPases; Biochemistry; Vol. 48; No. 29; 6696-6704; PMCID PMC2883566; 10.1021/bi9006989
• Zhang, Xin and Schaffitzel, Christiane, et el. (2009) Multiple conformational switches in a GTPase complex control co-translational protein targeting; Proceedings of the National Academy of Sciences of the United States of America; Vol. 106; No. 6; 1754-1759; PMCID PMC2644110; 10.1073/pnas.0808573106
• Zhang, Xin and Kung, Simon, et el. (2008) Demonstration of a Multistep Mechanism for Assembly of the SRP·SRP Receptor Complex: Implications for the Catalytic Role of SRP RNA; Journal of Molecular Biology; Vol. 381; No. 3; 581-593; PMCID PMC2630804; 10.1016/j.jmb.2008.05.049
• Chandrasekar, Sowmya and Chartron, Justin, et el. (2008) Structure of the Chloroplast Signal Recognition Particle (SRP) Receptor: Domain Arrangement Modulates SRP–Receptor Interaction; Journal of Molecular Biology; Vol. 375; No. 2; 425-436; 10.1016/j.jmb.2007.09.061
• Shan, Shu-ou and Chandrasekar, Sowmya, et el. (2007) Conformational changes in the GTPase modules of the signal reception particle and its receptor drive initiation of protein translocation; Journal of Cell Biology; Vol. 178; No. 4; 611-620; PMCID PMC2064468; 10.1083/jcb.200702018
• Jaru-Ampornpan, Peera and Chandrasekar, Sowmya, et el. (2007) Efficient Interaction between Two GTPases Allows the Chloroplast SRP Pathway to Bypass the Requirement for an SRP RNA; Molecular Biology of the Cell; Vol. 18; No. 7; 2636-2645; PMCID PMC1924832; 10.1091/mbc.E07-01-0037
• Shan, Shu-ou and Walter, Peter (2005) Molecular Crosstalk between the Nucleotide Specificity Determinant of the SRP GTPase and the SRP Receptor; Biochemistry; Vol. 44; No. 16; 6214-6222; 10.1021/bi0500980
• Shan, Shu-ou and Walter, Peter (2005) Co-translational protein targeting by the signal recognition particle; FEBS Letters; Vol. 579; No. 4; 921-926; 10.1016/j.febslet.2004.11.049
• Chu, Feixia and Shan, Shu-ou, et el. (2004) Unraveling the interface of signal recognition particle and its receptor by using chemical cross-linking and tandem mass spectrometry; Proceedings of the National Academy of Sciences of the United States of America; Vol. 101; No. 47; 16454-16459; PMCID PMC528904; 10.1073/pnas.0407456101
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