| Year |
Citation |
Score |
| 2024 |
Cho H, Liu Y, Chung S, Chandrasekar S, Weiss S, Shan SO. Dynamic stability of Sgt2 enables selective and privileged client handover in a chaperone triad. Nature Communications. 15: 134. PMID 38167697 DOI: 10.1038/s41467-023-44260-5 |
0.494 |
|
| 2023 |
Gupta A, Lentzsch AM, Siegel A, Yu Z, Chio US, Cheng Y, Shan SO. Dodecamer assembly of a metazoan AAA chaperone couples substrate extraction to refolding. Science Advances. 9: eadf5336. PMID 37163603 DOI: 10.1126/sciadv.adf5336 |
0.811 |
|
| 2023 |
Shan SO. Role of Hsp70 in Post-Translational Protein Targeting: Tail-Anchored Membrane Proteins and Beyond. International Journal of Molecular Sciences. 24. PMID 36674686 DOI: 10.3390/ijms24021170 |
0.502 |
|
| 2022 |
Yang CI, Zhu Z, Jones JJ, Lomenick B, Chou TF, Shan SO. System-wide analyses reveal essential roles of N-terminal protein modification in bacterial membrane integrity. Iscience. 25: 104756. PMID 35942092 DOI: 10.1016/j.isci.2022.104756 |
0.829 |
|
| 2022 |
Zhu Z, Wang S, Shan SO. Ribosome profiling reveals multiple roles of SecA in cotranslational protein export. Nature Communications. 13: 3393. PMID 35697696 DOI: 10.1038/s41467-022-31061-5 |
0.847 |
|
| 2022 |
Yang CI, Kim J, Shan SO. Ribosome-nascent Chain Interaction Regulates N-terminal Protein Modification. Journal of Molecular Biology. 434: 167535. PMID 35278477 DOI: 10.1016/j.jmb.2022.167535 |
0.461 |
|
| 2022 |
Jomaa A, Gamerdinger M, Hsieh HH, Wallisch A, Chandrasekaran V, Ulusoy Z, Scaiola A, Hegde RS, Shan SO, Ban N, Deuerling E. Mechanism of signal sequence handover from NAC to SRP on ribosomes during ER-protein targeting. Science (New York, N.Y.). 375: 839-844. PMID 35201867 DOI: 10.1126/science.abl6459 |
0.429 |
|
| 2021 |
Hsieh HH, Shan SO. Fidelity of Cotranslational Protein Targeting to the Endoplasmic Reticulum. International Journal of Molecular Sciences. 23. PMID 35008707 DOI: 10.3390/ijms23010281 |
0.516 |
|
| 2021 |
Chio US, Liu Y, Chung S, Shim WJ, Chandrasekar S, Weiss S, Shan SO. Subunit cooperation in the Get1/2 receptor promotes tail-anchored membrane protein insertion. The Journal of Cell Biology. 220. PMID 34614151 DOI: 10.1083/jcb.202103079 |
0.834 |
|
| 2021 |
Ji S, Siegel A, Shan SO, Grimm B, Wang P. Chloroplast SRP43 autonomously protects chlorophyll biosynthesis proteins against heat shock. Nature Plants. PMID 34475529 DOI: 10.1038/s41477-021-00994-y |
0.393 |
|
| 2021 |
Jomaa A, Eitzinger S, Zhu Z, Chandrasekar S, Kobayashi K, Shan SO, Ban N. Molecular mechanism of cargo recognition and handover by the mammalian signal recognition particle. Cell Reports. 36: 109350. PMID 34260909 DOI: 10.1016/j.celrep.2021.109350 |
0.849 |
|
| 2021 |
Lee JH, Jomaa A, Chung S, Hwang Fu YH, Qian R, Sun X, Hsieh HH, Chandrasekar S, Bi X, Mattei S, Boehringer D, Weiss S, Ban N, Shan SO. Receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER. Science Advances. 7. PMID 34020957 DOI: 10.1126/sciadv.abg0942 |
0.444 |
|
| 2021 |
Cho H, Shim WJ, Liu Y, Shan SO. J-domain proteins promote client relay from Hsp70 during tail-anchored membrane protein targeting. The Journal of Biological Chemistry. 100546. PMID 33741343 DOI: 10.1016/j.jbc.2021.100546 |
0.421 |
|
| 2020 |
Hsieh HH, Lee JH, Chandrasekar S, Shan SO. A ribosome-associated chaperone enables substrate triage in a cotranslational protein targeting complex. Nature Communications. 11: 5840. PMID 33203865 DOI: 10.1038/s41467-020-19548-5 |
0.548 |
|
| 2020 |
Siegel A, McAvoy CZ, Lam V, Liang FC, Kroon G, Miaou E, Griffin P, Wright PE, Shan SO. A disorder-to-order transition activates an ATP-Independent Membrane Protein Chaperone. Journal of Molecular Biology. PMID 33188783 DOI: 10.1016/j.jmb.2020.11.007 |
0.412 |
|
| 2020 |
Shan S, Wang S, Yang C, Hsieh H. Nascent Protein Selection and Triage at the Ribosome Exit Site The Faseb Journal. 34: 1-1. DOI: 10.1096/Fasebj.2020.34.S1.00156 |
0.489 |
|
| 2019 |
Yang CI, Hsieh HH, Shan SO. Timing and specificity of cotranslational nascent protein modification in bacteria. Proceedings of the National Academy of Sciences of the United States of America. PMID 31666319 DOI: 10.1096/Fasebj.2020.34.S1.04322 |
0.438 |
|
| 2019 |
Shan SO. Guiding Tail-anchored Membrane Proteins to the ER In a Chaperone Cascade. The Journal of Biological Chemistry. PMID 31575659 DOI: 10.1074/Jbc.Rev119.006197 |
0.588 |
|
| 2019 |
Wang S, Jomaa A, Jaskolowski M, Yang CI, Ban N, Shan SO. The molecular mechanism of cotranslational membrane protein recognition and targeting by SecA. Nature Structural & Molecular Biology. PMID 31570874 DOI: 10.1038/S41594-019-0297-8 |
0.667 |
|
| 2019 |
Hwang Fu YH, Chandrasekar S, Lee JH, Shan SO. A molecular recognition feature mediates ribosome-induced SRP-receptor assembly during protein targeting. The Journal of Cell Biology. PMID 31537711 DOI: 10.1083/Jcb.201901001 |
0.568 |
|
| 2019 |
Chio US, Chung S, Weiss S, Shan SO. A Chaperone Lid Ensures Efficient and Privileged Client Transfer during Tail-Anchored Protein Targeting. Cell Reports. 26: 37-44.e7. PMID 30605684 DOI: 10.1016/J.Celrep.2018.12.035 |
0.836 |
|
| 2018 |
Cho H, Chio US, Shan SO. In vitro Assays for Targeting and Insertion of Tail-Anchored Proteins Into the ER Membrane. Current Protocols in Cell Biology. e63. PMID 30253068 DOI: 10.1002/Cpcb.63 |
0.846 |
|
| 2018 |
Cho H, Shan SO. Substrate relay in an Hsp70-cochaperone cascade safeguards tail-anchored membrane protein targeting. The Embo Journal. PMID 29973361 DOI: 10.15252/Embj.201899264 |
0.571 |
|
| 2018 |
Lee JH, Chandrasekar S, Chung S, Hwang Fu YH, Liu D, Weiss S, Shan SO. 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. PMID 29848629 DOI: 10.1073/Pnas.1802252115 |
0.538 |
|
| 2018 |
McAvoy C, Siegel A, Piszkiewicz S, Miaou E, Yu M, Nguyen T, Moradian A, Sweredoski MJ, Hess S, Shan SO. Two Distinct Sites of client protein interaction with the chaperone cpSRP43. The Journal of Biological Chemistry. PMID 29669809 DOI: 10.1074/Jbc.Ra118.002215 |
0.709 |
|
| 2018 |
Wang P, Liang FC, Wittmann D, Siegel A, Shan SO, Grimm B. 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. PMID 29581280 DOI: 10.1073/Pnas.1719645115 |
0.544 |
|
| 2018 |
Kobayashi K, Jomaa A, Lee JH, Chandrasekar S, Boehringer D, Shan SO, Ban N. Structure of a prehandover mammalian ribosomal SRP•SRP receptor targeting complex. Science (New York, N.Y.). PMID 29567807 DOI: 10.1126/Science.Aar7924 |
0.56 |
|
| 2018 |
Hsieh HH, Shan S. Co-translational Targeting by Signal Recognition Particle Activates Only after Cytosolic Exposure of Signal Sequence Biophysical Journal. 114. DOI: 10.1016/J.Bpj.2017.11.425 |
0.54 |
|
| 2017 |
Chio US, Cho H, Shan SO. Mechanisms of Tail-Anchored Membrane Protein Targeting and Insertion. Annual Review of Cell and Developmental Biology. 33: 417-438. PMID 28992441 DOI: 10.1146/Annurev-Cellbio-100616-060839 |
0.842 |
|
| 2017 |
Chio US, Chung S, Weiss S, Shan SO. A protean clamp guides membrane targeting of tail-anchored proteins. Proceedings of the National Academy of Sciences of the United States of America. PMID 28973888 DOI: 10.1073/pnas.1708731114 |
0.846 |
|
| 2017 |
Wang S, Yang CI, Shan SO. SecA mediates cotranslational targeting and translocation of an inner membrane protein. The Journal of Cell Biology. PMID 28928132 DOI: 10.1083/Jcb.201704036 |
0.65 |
|
| 2017 |
Hwang Fu YH, Huang WYC, Shen K, Groves JT, Miller T, Shan SO. Two-step membrane binding by the bacterial SRP receptor enable efficient and accurate Co-translational protein targeting. Elife. 6. PMID 28753124 DOI: 10.1016/J.Bpj.2017.11.1170 |
0.689 |
|
| 2017 |
Jomaa A, Fu YH, Boehringer D, Leibundgut M, Shan SO, Ban N. Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome. Nature Communications. 8: 15470. PMID 28524878 DOI: 10.1038/Ncomms15470 |
0.822 |
|
| 2017 |
Fu YH, Huang WYC, Shen K, Groves JT, Miller T, Shan S. Author response: Two-step membrane binding by the bacterial SRP receptor enable efficient and accurate Co-translational protein targeting Elife. DOI: 10.7554/Elife.25885.026 |
0.816 |
|
| 2016 |
Chen Y, Shen K, Shan SO, Kou SC. Analyzing Single-Molecule Protein Transportation Experiments via Hierarchical Hidden Markov Models. Journal of the American Statistical Association. 111: 951-966. PMID 28943680 DOI: 10.1080/01621459.2016.1140050 |
0.601 |
|
| 2016 |
Rao M, Okreglak V, Chio US, Cho H, Walter P, Shan SO. Multiple selection filters ensure accurate tail-anchored membrane protein targeting. Elife. 5. PMID 27925580 DOI: 10.7554/Elife.21301 |
0.844 |
|
| 2016 |
Chandrasekar S, Shan SO. Anionic phospholipids and the Albino3 translocase activate SRP-receptor interaction during LHCP targeting. The Journal of Biological Chemistry. PMID 27895124 DOI: 10.1074/Jbc.M116.752956 |
0.604 |
|
| 2016 |
Chandrasekar S, Sweredoski MJ, Sohn CH, Hess S, Shan SO. Co-evolution of two GTPases enables efficient protein targeting in an RNA-less chloroplast Signal Recognition Particle pathway. The Journal of Biological Chemistry. PMID 27895118 DOI: 10.1074/Jbc.M116.752931 |
0.406 |
|
| 2016 |
Shan SO. ATPase and GTPase Tangos Drive Intracellular Protein Transport. Trends in Biochemical Sciences. PMID 27658684 DOI: 10.1016/J.Tibs.2016.08.012 |
0.506 |
|
| 2016 |
Liang FC, Kroon G, McAvoy CZ, Chi C, Wright PE, Shan SO. 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. PMID 26951662 DOI: 10.1073/Pnas.1524777113 |
0.556 |
|
| 2016 |
Rao M, Okreglak V, Chio US, Cho H, Walter P, Shan S. Author response: Multiple selection filters ensure accurate tail-anchored membrane protein targeting Elife. DOI: 10.7554/Elife.21301.015 |
0.809 |
|
| 2016 |
Wang C, Wang S, Niesen M, Shan S, Miller TF. Inversion of Signal Sequence Topology during Membrane Integration Biophysical Journal. 110: 226a-227a. DOI: 10.1016/J.Bpj.2015.11.1252 |
0.476 |
|
| 2015 |
Gristick HB, Rome ME, Chartron JW, Rao M, Hess S, Shan SO, Clemons WM. Mechanism of assembly of a substrate-transfer complex during tail-anchored protein targeting. The Journal of Biological Chemistry. PMID 26451041 DOI: 10.1074/Jbc.M115.677328 |
0.844 |
|
| 2015 |
Ariosa A, Lee JH, Wang S, Saraogi I, Shan SO. Regulation by a chaperone improves substrate selectivity during cotranslational protein targeting. Proceedings of the National Academy of Sciences of the United States of America. 112: E3169-78. PMID 26056263 DOI: 10.1073/Pnas.1422594112 |
0.852 |
|
| 2015 |
von Loeffelholz O, Jiang Q, Ariosa A, Karuppasamy M, Huard K, Berger I, Shan SO, Schaffitzel C. Ribosome-SRP-FtsY cotranslational targeting complex in the closed state. Proceedings of the National Academy of Sciences of the United States of America. 112: 3943-8. PMID 25775537 DOI: 10.1073/Pnas.1424453112 |
0.847 |
|
| 2015 |
Liang F, McAvoy C, Piszkiewicz S, Kroon GJ, Yamout M, Wright P, Shan S. Inter-Domain Dynamics of a Novel Chaperone Enables Effective Capture of Membrane Protein Substrates Biophysical Journal. 108: 53a. DOI: 10.1016/J.Bpj.2014.11.323 |
0.556 |
|
| 2015 |
Fu YH, Shan S. Distinct Membrane Association Modes Facilitate Co-Translational Protein Targeting Biophysical Journal. 108. DOI: 10.1016/J.Bpj.2014.11.1401 |
0.534 |
|
| 2014 |
Rome ME, Chio US, Rao M, Gristick H, Shan SO. 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. 111: E4929-35. PMID 25368153 DOI: 10.1073/Pnas.1411284111 |
0.834 |
|
| 2014 |
Saraogi I, Akopian D, Shan SO. Regulation of cargo recognition, commitment, and unloading drives cotranslational protein targeting. The Journal of Cell Biology. 205: 693-706. PMID 24914238 DOI: 10.1083/Jcb.201311028 |
0.865 |
|
| 2014 |
Zhang X, Shan SO. Fidelity of cotranslational protein targeting by the signal recognition particle. Annual Review of Biophysics. 43: 381-408. PMID 24895856 DOI: 10.1146/Annurev-Biophys-051013-022653 |
0.637 |
|
| 2014 |
Gristick HB, Rao M, Chartron JW, Rome ME, Shan SO, Clemons WM. Crystal structure of ATP-bound Get3-Get4-Get5 complex reveals regulation of Get3 by Get4. Nature Structural & Molecular Biology. 21: 437-42. PMID 24727835 DOI: 10.1038/Nsmb.2813 |
0.845 |
|
| 2014 |
Saraogi I, Shan SO. Co-translational protein targeting to the bacterial membrane. Biochimica Et Biophysica Acta. 1843: 1433-41. PMID 24513458 DOI: 10.1016/J.Bbamcr.2013.10.013 |
0.828 |
|
| 2014 |
Losón OC, Liu R, Rome ME, Meng S, Kaiser JT, Shan SO, Chan DC. The mitochondrial fission receptor MiD51 requires ADP as a cofactor. Structure (London, England : 1993). 22: 367-77. PMID 24508339 DOI: 10.1016/J.Str.2014.01.001 |
0.793 |
|
| 2013 |
Voigts-Hoffmann F, Schmitz N, Shen K, Shan SO, Ataide SF, Ban N. The structural basis of FtsY recruitment and GTPase activation by SRP RNA. Molecular Cell. 52: 643-54. PMID 24211265 DOI: 10.1016/J.Molcel.2013.10.005 |
0.669 |
|
| 2013 |
Shen K, Wang Y, Hwang Fu YH, Zhang Q, Feigon J, Shan SO. Molecular mechanism of GTPase activation at the signal recognition particle (SRP) RNA distal end. The Journal of Biological Chemistry. 288: 36385-97. PMID 24151069 DOI: 10.1074/Jbc.M113.513614 |
0.6 |
|
| 2013 |
Rome ME, Rao M, Clemons WM, Shan SO. Precise timing of ATPase activation drives targeting of tail-anchored proteins Proceedings of the National Academy of Sciences of the United States of America. 110: 7666-7671. PMID 23610396 DOI: 10.1073/Pnas.1222054110 |
0.841 |
|
| 2013 |
von Loeffelholz O, Knoops K, Ariosa A, Zhang X, Karuppasamy M, Huard K, Schoehn G, Berger I, Shan SO, Schaffitzel C. Structural basis of signal sequence surveillance and selection by the SRP-FtsY complex. Nature Structural & Molecular Biology. 20: 604-10. PMID 23563142 DOI: 10.1038/Nsmb.2546 |
0.845 |
|
| 2013 |
Nguyen TX, Jaru-Ampornpan P, Lam VQ, Cao P, Piszkiewicz S, Hess S, Shan SO. Mechanism of an ATP-independent protein disaggregase: I. structure of a membrane protein aggregate reveals a mechanism of recognition by its chaperone. The Journal of Biological Chemistry. 288: 13420-30. PMID 23525109 DOI: 10.1074/Jbc.M113.462812 |
0.808 |
|
| 2013 |
Jaru-Ampornpan P, Liang FC, Nisthal A, Nguyen TX, Wang P, Shen K, Mayo SL, Shan SO. Mechanism of an ATP-independent protein disaggregase: II. distinct molecular interactions drive multiple steps during aggregate disassembly. The Journal of Biological Chemistry. 288: 13431-45. PMID 23519468 DOI: 10.1074/Jbc.M113.462861 |
0.835 |
|
| 2013 |
Pierce NW, Lee JE, Liu X, Sweredoski MJ, Graham RL, Larimore EA, Rome M, Zheng N, Clurman BE, Hess S, Shan SO, Deshaies RJ. Cand1 promotes assembly of new SCF complexes through dynamic exchange of F box proteins. Cell. 153: 206-15. PMID 23453757 DOI: 10.1016/J.Cell.2013.02.024 |
0.819 |
|
| 2013 |
Akopian D, Shen K, Zhang X, Shan SO. Signal recognition particle: an essential protein-targeting machine. Annual Review of Biochemistry. 82: 693-721. PMID 23414305 DOI: 10.1146/Annurev-Biochem-072711-164732 |
0.802 |
|
| 2013 |
Akopian D, Dalal K, Shen K, Duong F, Shan SO. SecYEG activates GTPases to drive the completion of cotranslational protein targeting. The Journal of Cell Biology. 200: 397-405. PMID 23401005 DOI: 10.1083/Jcb.201208045 |
0.801 |
|
| 2013 |
Ariosa AR, Duncan SS, Saraogi I, Lu X, Brown A, Phillips GJ, Shan SO. Fingerloop activates cargo delivery and unloading during cotranslational protein targeting. Molecular Biology of the Cell. 24: 63-73. PMID 23135999 DOI: 10.1091/Mbc.E12-06-0434 |
0.853 |
|
| 2013 |
Shen K, Arslan S, Akopian D, Ha T, Shan S. Activated GTPase Movement on SRP RNA Drives Cotranslational Protein Targeting Biophysical Journal. 104: 419a. DOI: 10.1016/J.Bpj.2012.11.2334 |
0.775 |
|
| 2012 |
Shen K, Arslan S, Akopian D, Ha T, Shan SO. Activated GTPase movement on an RNA scaffold drives co-translational protein targeting. Nature. 492: 271-5. PMID 23235881 DOI: 10.1038/Nature11726 |
0.782 |
|
| 2012 |
Zhang D, Shan SO. Translation elongation regulates substrate selection by the signal recognition particle. The Journal of Biological Chemistry. 287: 7652-60. PMID 22228766 DOI: 10.1074/Jbc.M111.325001 |
0.612 |
|
| 2012 |
Zhang D, Sweredoski MJ, Graham RL, Hess S, Shan SO. Novel proteomic tools reveal essential roles of SRP and importance of proper membrane protein biogenesis. Molecular & Cellular Proteomics : McP. 11: M111.011585. PMID 22030350 DOI: 10.1074/Mcp.M111.011585 |
0.553 |
|
| 2011 |
Saraogi I, Akopian D, Shan SO. A tale of two GTPases in cotranslational protein targeting. Protein Science : a Publication of the Protein Society. 20: 1790-5. PMID 21898651 DOI: 10.1002/Pro.729 |
0.818 |
|
| 2011 |
Saraogi I, Zhang D, Chandrasekaran S, Shan SO. Site-specific fluorescent labeling of nascent proteins on the translating ribosome. Journal of the American Chemical Society. 133: 14936-9. PMID 21870811 DOI: 10.1021/Ja206626G |
0.769 |
|
| 2011 |
Nguyen TX, Chandrasekar S, Neher S, Walter P, Shan SO. Concerted complex assembly and GTPase activation in the chloroplast signal recognition particle. Biochemistry. 50: 7208-17. PMID 21780778 DOI: 10.1021/Bi200742A |
0.768 |
|
| 2011 |
Zhang X, Lam VQ, Mou Y, Kimura T, Chung J, Chandrasekar S, Winkler JR, Mayo SL, Shan SO. Direct visualization reveals dynamics of a transient intermediate during protein assembly. Proceedings of the National Academy of Sciences of the United States of America. 108: 6450-5. PMID 21464281 DOI: 10.1073/Pnas.1019051108 |
0.471 |
|
| 2011 |
Shen K, Zhang X, Shan SO. Synergistic actions between the SRP RNA and translating ribosome allow efficient delivery of the correct cargos during cotranslational protein targeting. Rna (New York, N.Y.). 17: 892-902. PMID 21460239 DOI: 10.1261/Rna.2610411 |
0.683 |
|
| 2011 |
Ataide SF, Schmitz N, Shen K, Ke A, Shan SO, Doudna JA, Ban N. The crystal structure of the signal recognition particle in complex with its receptor. Science (New York, N.Y.). 331: 881-6. PMID 21330537 DOI: 10.1126/Science.1196473 |
0.691 |
|
| 2011 |
Saraogi I, Shan SO. Molecular mechanism of co-translational protein targeting by the signal recognition particle. Traffic (Copenhagen, Denmark). 12: 535-42. PMID 21291501 DOI: 10.1111/J.1600-0854.2011.01171.X |
0.81 |
|
| 2011 |
Estrozi LF, Boehringer D, Shan SO, Ban N, Schaffitzel C. Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor. Nature Structural & Molecular Biology. 18: 88-90. PMID 21151118 DOI: 10.1038/Nsmb.1952 |
0.466 |
|
| 2010 |
Lam VQ, Akopian D, Rome M, Henningsen D, Shan SO. Lipid activation of the signal recognition particle receptor provides spatial coordination of protein targeting. The Journal of Cell Biology. 190: 623-35. PMID 20733058 DOI: 10.1083/Jcb.201004129 |
0.862 |
|
| 2010 |
Zhang X, Rashid R, Wang K, Shan SO. Sequential checkpoints govern substrate selection during cotranslational protein targeting. Science (New York, N.Y.). 328: 757-60. PMID 20448185 DOI: 10.1126/Science.1186743 |
0.627 |
|
| 2010 |
Jaru-Ampornpan P, Shen K, Lam VQ, Ali M, Doniach S, Jia TZ, Shan SO. ATP-independent reversal of a membrane protein aggregate by a chloroplast SRP subunit. Nature Structural & Molecular Biology. 17: 696-702. PMID 20424608 DOI: 10.1038/Nsmb.1836 |
0.863 |
|
| 2010 |
Shen K, Shan SO. 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. 107: 7698-703. PMID 20385832 DOI: 10.1073/Pnas.1002968107 |
0.665 |
|
| 2009 |
Jaru-Ampornpan P, Nguyen TX, Shan SO. A distinct mechanism to achieve efficient signal recognition particle (SRP)-SRP receptor interaction by the chloroplast srp pathway. Molecular Biology of the Cell. 20: 3965-73. PMID 19587121 DOI: 10.1091/Mbc.E08-10-0989 |
0.815 |
|
| 2009 |
Shan SO, Schmid SL, Zhang X. Signal recognition particle (SRP) and SRP receptor: a new paradigm for multistate regulatory GTPases. Biochemistry. 48: 6696-704. PMID 19469550 DOI: 10.1021/Bi9006989 |
0.459 |
|
| 2009 |
Zhang X, Schaffitzel C, Ban N, Shan SO. 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. 106: 1754-9. PMID 19174514 DOI: 10.1073/Pnas.0808573106 |
0.641 |
|
| 2008 |
Zhang X, Kung S, Shan SO. Demonstration of a multistep mechanism for assembly of the SRP x SRP receptor complex: implications for the catalytic role of SRP RNA. Journal of Molecular Biology. 381: 581-93. PMID 18617187 DOI: 10.1016/J.Jmb.2008.05.049 |
0.495 |
|
| 2008 |
Chandrasekar S, Chartron J, Jaru-Ampornpan P, Shan SO. Structure of the chloroplast signal recognition particle (SRP) receptor: domain arrangement modulates SRP-receptor interaction. Journal of Molecular Biology. 375: 425-36. PMID 18035371 DOI: 10.1016/J.Jmb.2007.09.061 |
0.768 |
|
| 2007 |
Shan SO, Chandrasekar S, Walter P. Conformational changes in the GTPase modules of the signal reception particle and its receptor drive initiation of protein translocation. The Journal of Cell Biology. 178: 611-20. PMID 17682051 DOI: 10.1083/Jcb.200702018 |
0.694 |
|
| 2007 |
Jaru-Ampornpan P, Chandrasekar S, Shan SO. Efficient interaction between two GTPases allows the chloroplast SRP pathway to bypass the requirement for an SRP RNA. Molecular Biology of the Cell. 18: 2636-45. PMID 17475780 DOI: 10.1091/Mbc.E07-01-0037 |
0.776 |
|
| 2005 |
Shan SO, Walter P. Molecular crosstalk between the nucleotide specificity determinant of the SRP GTPase and the SRP receptor. Biochemistry. 44: 6214-22. PMID 15835909 DOI: 10.1021/Bi0500980 |
0.647 |
|
| 2005 |
Shan SO, Walter P. Co-translational protein targeting by the signal recognition particle. Febs Letters. 579: 921-6. PMID 15680975 DOI: 10.1016/J.Febslet.2004.11.049 |
0.684 |
|
| 2004 |
Chu F, Shan SO, Moustakas DT, Alber F, Egea PF, Stroud RM, Walter P, Burlingame AL. 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. 101: 16454-9. PMID 15546976 DOI: 10.1073/Pnas.0407456101 |
0.791 |
|
| 2004 |
Shan SO, Stroud RM, Walter P. Mechanism of association and reciprocal activation of two GTPases. Plos Biology. 2: e320. PMID 15383838 DOI: 10.1371/Journal.Pbio.0020320 |
0.64 |
|
| 2004 |
Egea PF, Shan SO, Napetschnig J, Savage DF, Walter P, Stroud RM. Substrate twinning activates the signal recognition particle and its receptor. Nature. 427: 215-21. PMID 14724630 DOI: 10.1038/Nature02250 |
0.832 |
|
| 2003 |
Shan SO, Walter P. Induced nucleotide specificity in a GTPase. Proceedings of the National Academy of Sciences of the United States of America. 100: 4480-5. PMID 12663860 DOI: 10.1073/Pnas.0737693100 |
0.649 |
|
| 2002 |
Shan SO, Herschlag D. Dissection of a metal-ion-mediated conformational change in Tetrahymena ribozyme catalysis. Rna (New York, N.Y.). 8: 861-72. PMID 12166641 DOI: 10.1017/S1355838202020216 |
0.524 |
|
| 2001 |
Peluso P, Shan SO, Nock S, Herschlag D, Walter P. Role of SRP RNA in the GTPase cycles of Ffh and FtsY. Biochemistry. 40: 15224-33. PMID 11735405 DOI: 10.1021/Bi011639Y |
0.801 |
|
| 2001 |
Shan S, Kravchuk AV, Piccirilli JA, Herschlag D. Defining the catalytic metal ion interactions in the Tetrahymena ribozyme reaction. Biochemistry. 40: 5161-71. PMID 11318638 DOI: 10.1021/Bi002887H |
0.518 |
|
| 2000 |
Shan SO, Herschlag D. An unconventional origin of metal-ion rescue and inhibition in the Tetrahymena group I ribozyme reaction. Rna (New York, N.Y.). 6: 795-813. PMID 10864040 DOI: 10.1017/S1355838200000649 |
0.503 |
|
| 2000 |
Yoshida A, Shan So, Herschlag D, Piccirilli JA. The role of the cleavage site 2'-hydroxyl in the Tetrahymena group I ribozyme reaction. Chemistry & Biology. 7: 85-96. PMID 10662698 DOI: 10.1016/S1074-5521(00)00074-0 |
0.487 |
|
| 1999 |
Shan So, Yoshida A, Sun S, Piccirilli JA, Herschlag D. Three metal ions at the active site of the Tetrahymena group I ribozyme. Proceedings of the National Academy of Sciences of the United States of America. 96: 12299-304. PMID 10535916 DOI: 10.1073/Pnas.96.22.12299 |
0.482 |
|
| 1999 |
Shan SO, Herschlag D. Hydrogen bonding in enzymatic catalysis: analysis of energetic contributions. Methods in Enzymology. 308: 246-76. PMID 10507008 DOI: 10.1016/S0076-6879(99)08013-1 |
0.497 |
|
| 1999 |
Shan SO, Narlikar GJ, Herschlag D. Protonated 2'-aminoguanosine as a probe of the electrostatic environment of the active site of the Tetrahymena group I ribozyme. Biochemistry. 38: 10976-88. PMID 10460152 DOI: 10.1021/Bi9903897 |
0.692 |
|
| 1999 |
Shan SO, Herschlag D. Probing the role of metal ions in RNA catalysis: kinetic and thermodynamic characterization of a metal ion interaction with the 2'-moiety of the guanosine nucleophile in the Tetrahymena group I ribozyme. Biochemistry. 38: 10958-75. PMID 10460151 DOI: 10.1021/Bi990388E |
0.509 |
|
| 1997 |
Herschlag D, Narlikar QJ, Peracchi A, Shan S. Biological catalysis: Lessons from the comparison of RNA and protein enzymes Faseb Journal. 11: A852. |
0.517 |
|
| 1996 |
Shan SO, Herschlag D. The change in hydrogen bond strength accompanying charge rearrangement: implications for enzymatic catalysis. Proceedings of the National Academy of Sciences of the United States of America. 93: 14474-9. PMID 8962076 DOI: 10.1073/Pnas.93.25.14474 |
0.474 |
|
| 1996 |
Shan SO, Loh S, Herschlag D. The energetics of hydrogen bonds in model systems: implications for enzymatic catalysis. Science (New York, N.Y.). 272: 97-101. PMID 8600542 DOI: 10.1126/Science.272.5258.97 |
0.459 |
|
| 1996 |
Shan S, Herschlag D. Energetic effects of multiple hydrogen bonds. Implications for enzymatic catalysis Journal of the American Chemical Society. 118: 5515-5518. DOI: 10.1021/Ja954205X |
0.481 |
|
| Show low-probability matches. |
