| Year |
Citation |
Score |
| 2024 |
Li J, Purser N, Liwocha J, Scott DC, Byers HA, Steigenberger B, Hill S, Tripathi-Giesgen I, Hinkle T, Hansen FM, Prabu JR, Radhakrishnan SK, Kirkpatrick DS, Reichermeier KM, Schulman BA, ... Kleiger G, et al. Cullin-RING ligases employ geometrically optimized catalytic partners for substrate targeting. Molecular Cell. PMID 38382526 DOI: 10.1016/j.molcel.2024.01.022 |
0.324 |
|
| 2024 |
Liwocha J, Li J, Purser N, Rattanasopa C, Maiwald S, Krist DT, Scott DC, Steigenberger B, Prabu JR, Schulman BA, Kleiger G. Mechanism of millisecond Lys48-linked poly-ubiquitin chain formation by cullin-RING ligases. Nature Structural & Molecular Biology. PMID 38326650 DOI: 10.1038/s41594-023-01206-1 |
0.331 |
|
| 2023 |
Purser N, Tripathi-Giesgen I, Li J, Scott DC, Horn-Ghetko D, Baek K, Schulman BA, Alpi AF, Kleiger G. Catalysis of non-canonical protein ubiquitylation by the ARIH1 ubiquitin ligase. The Biochemical Journal. PMID 37870100 DOI: 10.1042/BCJ20230373 |
0.406 |
|
| 2023 |
Scott DC, King MT, Baek K, Gee CT, Kalathur R, Li J, Purser N, Nourse A, Chai SC, Vaithiyalingam S, Chen T, Lee RE, Elledge SJ, Kleiger G, Schulman BA. E3 ligase autoinhibition by C-degron mimicry maintains C-degron substrate fidelity. Molecular Cell. PMID 36805027 DOI: 10.1016/j.molcel.2023.01.019 |
0.315 |
|
| 2021 |
Ibarra R, Borror HR, Hart B, Gardner RG, Kleiger G. The San1 Ubiquitin Ligase Avidly Recognizes Misfolded Proteins through Multiple Substrate Binding Sites. Biomolecules. 11. PMID 34827617 DOI: 10.3390/biom11111619 |
0.353 |
|
| 2020 |
Liwocha J, Krist DT, van der Heden van Noort GJ, Hansen FM, Truong VH, Karayel O, Purser N, Houston D, Burton N, Bostock MJ, Sattler M, Mann M, Harrison JS, Kleiger G, Ovaa H, et al. Linkage-specific ubiquitin chain formation depends on a lysine hydrocarbon ruler. Nature Chemical Biology. PMID 33288957 DOI: 10.1038/s41589-020-00696-0 |
0.317 |
|
| 2020 |
Baek K, Krist DT, Prabu JR, Hill S, Klügel M, Neumaier LM, von Gronau S, Kleiger G, Schulman BA. NEDD8 nucleates a multivalent cullin-RING-UBE2D ubiquitin ligation assembly. Nature. PMID 32051583 DOI: 10.1038/S41586-020-2000-Y |
0.483 |
|
| 2019 |
Hill S, Reichermeier K, Scott DC, Samentar L, Coulombe-Huntington J, Izzi L, Tang X, Ibarra R, Bertomeu T, Moradian A, Sweredoski MJ, Caberoy N, Schulman BA, Sicheri F, Tyers M, ... Kleiger G, et al. Robust cullin-RING ligase function is established by a multiplicity of poly-ubiquitylation pathways. Elife. 8. PMID 31868589 DOI: 10.7554/Elife.51163 |
0.368 |
|
| 2019 |
Jones RD, Enam C, Ibarra R, Borror HR, Mostoller KE, Fredrickson EK, Lin J, Chuang E, March Z, Shorter J, Ravid T, Kleiger G, Gardner RG. The extent of Ssa1/Ssa2 Hsp70 chaperone involvement in nuclear protein quality control degradation varies with the substrate. Molecular Biology of the Cell. mbcE18020121. PMID 31825716 DOI: 10.1091/Mbc.E18-02-0121 |
0.412 |
|
| 2017 |
Hill S, Kleiger G. Self-regulating ubiquitin ligases. The Embo Journal. PMID 28087580 DOI: 10.15252/Embj.201696154 |
0.303 |
|
| 2016 |
Kleiger G, Deshaies R. Tag Team Ubiquitin Ligases. Cell. 166: 1080-1. PMID 27565338 DOI: 10.1016/J.Cell.2016.08.014 |
0.337 |
|
| 2016 |
Ibarra R, Sandoval D, Fredrickson EK, Gardner RG, Kleiger G. The San1 ubiquitin ligase functions preferentially with ubiquitin-conjugating enzyme Ubc1 during protein quality control. The Journal of Biological Chemistry. PMID 27405755 DOI: 10.1074/Jbc.M116.737619 |
0.446 |
|
| 2016 |
Hill S, Harrison JS, Lewis SM, Kuhlman B, Kleiger G. Mechanism of Lysine 48 selectivity during poly-ubiquitin chain formation by the Ube2R1/2 ubiquitin-conjugating enzyme. Molecular and Cellular Biology. PMID 27044868 DOI: 10.1128/Mcb.00097-16 |
0.49 |
|
| 2015 |
Sandoval D, Hill S, Ziemba A, Lewis S, Kuhlman B, Kleiger G. Ubiquitin-conjugating enzyme Cdc34 and ubiquitin ligase Skp1-cullin-F-box ligase (SCF) interact through multiple conformations. The Journal of Biological Chemistry. 290: 1106-18. PMID 25425648 DOI: 10.1074/Jbc.M114.615559 |
0.485 |
|
| 2014 |
Kleiger G, Mayor T. Perilous journey: a tour of the ubiquitin–proteasome system Trends in Cell Biology. 24: 352-359. PMID 24457024 DOI: 10.1016/J.Tcb.2013.12.003 |
0.41 |
|
| 2014 |
Huang H, Ceccarelli DF, Orlicky S, St-Cyr DJ, Ziemba A, Garg P, Plamondon S, Auer M, Sidhu S, Marinier A, Kleiger G, Tyers M, Sicheri F. E2 enzyme inhibition by stabilization of a low-affinity interface with ubiquitin. Nature Chemical Biology. 10: 156-163. PMID 24316736 DOI: 10.1038/Nchembio.1412 |
0.446 |
|
| 2013 |
Ziemba A, Hill S, Sandoval D, Webb K, Bennett EJ, Kleiger G. Multimodal mechanism of action for the Cdc34 acidic loop: a case study for why ubiquitin-conjugating enzymes have loops and tails. The Journal of Biological Chemistry. 288: 34882-96. PMID 24129577 DOI: 10.1074/Jbc.M113.509190 |
0.413 |
|
| 2012 |
den Besten W, Verma R, Kleiger G, Oania RS, Deshaies RJ. NEDD8 links cullin-RING ubiquitin ligase function to the p97 pathway. Nature Structural & Molecular Biology. 19: 511-6, S1. PMID 22466964 DOI: 10.1038/Nsmb.2269 |
0.407 |
|
| 2011 |
Saha A, Lewis S, Kleiger G, Kuhlman B, Deshaies RJ. Essential role for ubiquitin-ubiquitin-conjugating enzyme interaction in ubiquitin discharge from Cdc34 to substrate. Molecular Cell. 42: 75-83. PMID 21474069 DOI: 10.1016/J.Molcel.2011.03.016 |
0.405 |
|
| 2010 |
Tyrrell A, Flick K, Kleiger G, Zhang H, Deshaies RJ, Kaiser P. Physiologically relevant and portable tandem ubiquitin-binding domain stabilizes polyubiquitylated proteins. Proceedings of the National Academy of Sciences of the United States of America. 107: 19796-801. PMID 21041680 DOI: 10.1073/Pnas.1010648107 |
0.439 |
|
| 2009 |
Pierce NW, Kleiger G, Shan SO, Deshaies RJ. Detection of sequential polyubiquitylation on a millisecond timescale. Nature. 462: 615-9. PMID 19956254 DOI: 10.1038/Nature08595 |
0.376 |
|
| 2009 |
Kleiger G, Saha A, Lewis S, Kuhlman B, Deshaies RJ. Rapid E2-E3 assembly and disassembly enable processive ubiquitylation of cullin-RING ubiquitin ligase substrates. Cell. 139: 957-68. PMID 19945379 DOI: 10.1016/J.Cell.2009.10.030 |
0.44 |
|
| 2009 |
Kleiger G, Hao B, Mohl DA, Deshaies RJ. The acidic tail of the Cdc34 ubiquitin-conjugating enzyme functions in both binding to and catalysis with ubiquitin ligase SCFCdc4. The Journal of Biological Chemistry. 284: 36012-23. PMID 19875449 DOI: 10.1074/Jbc.M109.058529 |
0.43 |
|
| 2006 |
Petroski MD, Kleiger G, Deshaies RJ. Evaluation of a diffusion-driven mechanism for substrate ubiquitination by the SCF-Cdc34 ubiquitin ligase complex. Molecular Cell. 24: 523-34. PMID 17114057 DOI: 10.1016/J.Molcel.2006.10.010 |
0.371 |
|
| 2004 |
Kleiger G, Panina EM, Mallick P, Eisenberg D. PFIT and PFRIT: bioinformatic algorithms for detecting glycosidase function from structure and sequence. Protein Science : a Publication of the Protein Society. 13: 221-9. PMID 14691237 DOI: 10.1110/Ps.03274104 |
0.565 |
|
| 2003 |
McCarty AS, Kleiger G, Eisenberg D, Smale ST. Selective dimerization of a C2H2 zinc finger subfamily. Molecular Cell. 11: 459-70. PMID 12620233 DOI: 10.1016/S1097-2765(03)00043-1 |
0.499 |
|
| 2002 |
Kleiger G, Eisenberg D. GXXXG and GXXXA motifs stabilize FAD and NAD(P)-binding Rossmann folds through C(alpha)-H... O hydrogen bonds and van der waals interactions. Journal of Molecular Biology. 323: 69-76. PMID 12368099 DOI: 10.1016/S0022-2836(02)00885-9 |
0.558 |
|
| 2002 |
Kleiger G, Grothe R, Mallick P, Eisenberg D. GXXXG and AXXXA: Common α-Helical Interaction Motifs in Proteins, Particularly in Extremophiles† Biochemistry. 41: 5990-5997. PMID 11993993 DOI: 10.1021/Bi0200763 |
0.587 |
|
| 2001 |
Kleiger G, Perry J, Eisenberg D. 3D structure and significance of the GPhiXXG helix packing motif in tetramers of the E1beta subunit of pyruvate dehydrogenase from the archeon Pyrobaculum aerophilum. Biochemistry. 40: 14484-14492. PMID 11724561 DOI: 10.1021/Bi011016K |
0.473 |
|
| 2000 |
Cobb BS, Morales-Alcelay S, Kleiger G, Brown KE, Fisher AG, Smale ST. Targeting of Ikaros to pericentromeric heterochromatin by direct DNA binding. Genes & Development. 14: 2146-60. PMID 10970879 DOI: 10.1101/Gad.816400 |
0.34 |
|
| 2000 |
Kleiger G, Beamer LJ, Grothe R, Mallick P, Eisenberg D. The 1.7 A crystal structure of BPI: a study of how two dissimilar amino acid sequences can adopt the same fold. Journal of Molecular Biology. 299: 1019-34. PMID 10843855 DOI: 10.1006/Jmbi.2000.3805 |
0.564 |
|
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