Year |
Citation |
Score |
2022 |
Tsai PL, Cameron CJF, Forni MF, Wasko RR, Naughton BS, Horsley V, Gerstein MB, Schlieker C. Dynamic quality control machinery that operates across compartmental borders mediates the degradation of mammalian nuclear membrane proteins. Cell Reports. 41: 111675. PMID 36417855 DOI: 10.1016/j.celrep.2022.111675 |
0.395 |
|
2022 |
Prophet SM, Rampello AJ, Niescier RF, Gentile JE, Mallik S, Koleske AJ, Schlieker C. Atypical nuclear envelope condensates linked to neurological disorders reveal nucleoporin-directed chaperone activities. Nature Cell Biology. 24: 1630-1641. PMID 36302970 DOI: 10.1038/s41556-022-01001-y |
0.31 |
|
2021 |
Amaya C, Cameron CJ, Devarkar SC, Seager SJ, Gerstein MB, Xiong Y, Schlieker C. Nodal modulator (NOMO) is required to sustain endoplasmic reticulum morphology. The Journal of Biological Chemistry. 100937. PMID 34224731 DOI: 10.1016/j.jbc.2021.100937 |
0.361 |
|
2020 |
Bahmanyar S, Schlieker C. Lipid and protein dynamics that shape nuclear envelope identity. Molecular Biology of the Cell. 31: 1315-1323. PMID 32530796 DOI: 10.1091/Mbc.E18-10-0636 |
0.387 |
|
2020 |
Rampello AJ, Laudermilch E, Vishnoi N, Prophet SM, Shao L, Zhao C, Lusk CP, Schlieker C. Torsin ATPase deficiency leads to defects in nuclear pore biogenesis and sequestration of MLF2. The Journal of Cell Biology. 219. PMID 32342107 DOI: 10.1083/Jcb.201910185 |
0.357 |
|
2020 |
Rampello AJ, Prophet SM, Schlieker C. The Role of Torsin AAA+ Proteins in Preserving Nuclear Envelope Integrity and Safeguarding Against Disease. Biomolecules. 10. PMID 32204310 DOI: 10.3390/biom10030468 |
0.414 |
|
2019 |
Tsai PL, Zhao C, Schlieker C. Methodologies to monitor protein turnover at the inner nuclear membrane. Methods in Enzymology. 619: 47-69. PMID 30910029 DOI: 10.1016/Bs.Mie.2018.12.033 |
0.477 |
|
2017 |
Chase AR, Laudermilch E, Wang J, Shigematsu H, Yokoyama T, Schlieker C. Dynamic functional assembly of the Torsin AAA+ ATPase and its modulation by LAP1. Molecular Biology of the Cell. PMID 28814508 DOI: 10.1091/Mbc.E17-05-0281 |
0.42 |
|
2017 |
Chase AR, Laudermilch E, Schlieker C. Torsin ATPases: Harnessing Dynamic Instability for Function. Frontiers in Molecular Biosciences. 4: 29. PMID 28553638 DOI: 10.3389/Fmolb.2017.00029 |
0.496 |
|
2016 |
Turner EM, Schlieker C. Pelger-Huët anomaly and Greenberg skeletal dysplasia: LBR-associated diseases of cholesterol metabolism. Rare Diseases (Austin, Tex.). 4: e1241363. PMID 27830109 DOI: 10.1080/21675511.2016.1241363 |
0.331 |
|
2016 |
Laudermilch E, Tsai PL, Graham M, Turner E, Zhao C, Schlieker C. Dissecting Torsin/cofactor function at the nuclear envelope: a genetic study. Molecular Biology of the Cell. PMID 27798237 DOI: 10.1091/Mbc.E16-07-0511 |
0.347 |
|
2016 |
Tsai PL, Zhao C, Turner E, Schlieker CD. The Lamin B receptor is essential for cholesterol synthesis and perturbed by disease-causing mutations. Elife. 5. PMID 27336722 DOI: 10.7554/eLife.16011 |
0.332 |
|
2016 |
Zhao C, Brown RS, Tang CA, Hu CA, Schlieker C. Site-specific Proteolysis Mobilizes TorsinA from the Membrane of the Endoplasmic Reticulum in Response to ER Stress and B cell Stimulation. The Journal of Biological Chemistry. PMID 26953341 DOI: 10.1074/Jbc.M115.709337 |
0.393 |
|
2016 |
Laudermilch E, Schlieker C. Torsin ATPases: structural insights and functional perspectives. Current Opinion in Cell Biology. 40: 1-7. PMID 26803745 DOI: 10.1016/J.Ceb.2016.01.001 |
0.376 |
|
2015 |
Rose AE, Brown RS, Schlieker C. Torsins: not your typical AAA+ ATPases. Critical Reviews in Biochemistry and Molecular Biology. 1-18. PMID 26592310 DOI: 10.3109/10409238.2015.1091804 |
0.672 |
|
2015 |
Speltz EB, Brown RS, Hajare HS, Schlieker C, Regan L. A designed repeat protein as an affinity capture reagent. Biochemical Society Transactions. 43: 874-80. PMID 26517897 DOI: 10.1042/Bst20150091 |
0.39 |
|
2015 |
Turner EM, Brown RS, Laudermilch E, Tsai PL, Schlieker C. The Torsin Activator LULL1 Is Required for Efficient Growth of Herpes Simplex Virus 1. Journal of Virology. 89: 8444-52. PMID 26041288 DOI: 10.1128/Jvi.01143-15 |
0.397 |
|
2014 |
Brown RS, Zhao C, Chase AR, Wang J, Schlieker C. The mechanism of Torsin ATPase activation. Proceedings of the National Academy of Sciences of the United States of America. 111: E4822-31. PMID 25352667 DOI: 10.1073/Pnas.1415271111 |
0.445 |
|
2014 |
Rose AE, Zhao C, Turner EM, Steyer AM, Schlieker C. Arresting a Torsin ATPase reshapes the endoplasmic reticulum. The Journal of Biological Chemistry. 289: 552-64. PMID 24275647 DOI: 10.1074/Jbc.M113.515791 |
0.67 |
|
2013 |
Zhao C, Brown RS, Chase AR, Eisele MR, Schlieker C. Regulation of Torsin ATPases by LAP1 and LULL1. Proceedings of the National Academy of Sciences of the United States of America. 110: E1545-54. PMID 23569223 DOI: 10.1073/Pnas.1300676110 |
0.459 |
|
2013 |
Sehrawat S, Koenig PA, Kirak O, Schlieker C, Fankhauser M, Ploegh HL. A catalytically inactive mutant of the deubiquitylase YOD-1 enhances antigen cross-presentation. Blood. 121: 1145-56. PMID 23243279 DOI: 10.1182/Blood-2012-08-447409 |
0.429 |
|
2012 |
Rose A, Schlieker C. Alternative nuclear transport for cellular protein quality control. Trends in Cell Biology. 22: 509-14. PMID 22858153 DOI: 10.1016/J.Tcb.2012.07.003 |
0.685 |
|
2011 |
Ernst R, Claessen JH, Mueller B, Sanyal S, Spooner E, van der Veen AG, Kirak O, Schlieker CD, Weihofen WA, Ploegh HL. Enzymatic blockade of the ubiquitin-proteasome pathway. Plos Biology. 8: e1000605. PMID 21468303 DOI: 10.1371/Journal.Pbio.1000605 |
0.544 |
|
2011 |
Van der Veen AG, Schorpp K, Schlieker C, Buti L, Damon JR, Spooner E, Ploegh HL, Jentsch S. Role of the ubiquitin-like protein Urm1 as a noncanonical lysine-directed protein modifier. Proceedings of the National Academy of Sciences of the United States of America. 108: 1763-70. PMID 21209336 DOI: 10.1073/Pnas.1014402108 |
0.606 |
|
2010 |
Rose A, Schlieker C. DNA repair: Blocking ubiquitin transfer. Nature. 466: 929-30. PMID 20725029 DOI: 10.1038/466929A |
0.672 |
|
2009 |
Ernst R, Mueller B, Ploegh HL, Schlieker C. The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER. Molecular Cell. 36: 28-38. PMID 19818707 DOI: 10.1016/J.Molcel.2009.09.016 |
0.554 |
|
2008 |
Schlieker CD, Van der Veen AG, Damon JR, Spooner E, Ploegh HL. A functional proteomics approach links the ubiquitin-related modifier Urm1 to a tRNA modification pathway. Proceedings of the National Academy of Sciences of the United States of America. 105: 18255-60. PMID 19017811 DOI: 10.1073/Pnas.0808756105 |
0.475 |
|
2007 |
Love KR, Catic A, Schlieker C, Ploegh HL. Mechanisms, biology and inhibitors of deubiquitinating enzymes. Nature Chemical Biology. 3: 697-705. PMID 17948018 DOI: 10.1038/Nchembio.2007.43 |
0.557 |
|
2007 |
Gredmark S, Schlieker C, Quesada V, Spooner E, Ploegh HL. A functional ubiquitin-specific protease embedded in the large tegument protein (ORF64) of murine gammaherpesvirus 68 is active during the course of infection. Journal of Virology. 81: 10300-9. PMID 17634221 DOI: 10.1128/Jvi.01149-07 |
0.581 |
|
2007 |
Schlieker C, Weihofen WA, Frijns E, Kattenhorn LM, Gaudet R, Ploegh HL. Structure of a herpesvirus-encoded cysteine protease reveals a unique class of deubiquitinating enzymes. Molecular Cell. 25: 677-87. PMID 17349955 DOI: 10.1016/J.Molcel.2007.01.033 |
0.531 |
|
2005 |
Schlieker C, Zentgraf H, Dersch P, Mogk A. ClpV, a unique Hsp100/Clp member of pathogenic proteobacteria. Biological Chemistry. 386: 1115-27. PMID 16307477 DOI: 10.1515/Bc.2005.128 |
0.493 |
|
2005 |
Schlieker C, Korbel GA, Kattenhorn LM, Ploegh HL. A deubiquitinating activity is conserved in the large tegument protein of the herpesviridae. Journal of Virology. 79: 15582-5. PMID 16306630 DOI: 10.1128/Jvi.79.24.15582-15585.2005 |
0.549 |
|
2005 |
Weibezahn J, Schlieker C, Tessarz P, Mogk A, Bukau B. Novel insights into the mechanism of chaperone-assisted protein disaggregation. Biological Chemistry. 386: 739-44. PMID 16201868 DOI: 10.1515/Bc.2005.086 |
0.644 |
|
2004 |
Schlieker C, Tews I, Bukau B, Mogk A. Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides. Febs Letters. 578: 351-6. PMID 15589844 DOI: 10.1016/J.Febslet.2004.11.051 |
0.595 |
|
2004 |
Weibezahn J, Tessarz P, Schlieker C, Zahn R, Maglica Z, Lee S, Zentgraf H, Weber-Ban EU, Dougan DA, Tsai FT, Mogk A, Bukau B. Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell. 119: 653-65. PMID 15550247 DOI: 10.1016/J.Cell.2004.11.027 |
0.645 |
|
2004 |
Schlieker C, Weibezahn J, Patzelt H, Tessarz P, Strub C, Zeth K, Erbse A, Schneider-Mergener J, Chin JW, Schultz PG, Bukau B, Mogk A. Substrate recognition by the AAA+ chaperone ClpB. Nature Structural & Molecular Biology. 11: 607-15. PMID 15208691 DOI: 10.1038/Nsmb787 |
0.614 |
|
2004 |
Schlieker C, Mogk A, Bukau B. A PDZ switch for a cellular stress response. Cell. 117: 417-9. PMID 15137934 DOI: 10.1016/S0092-8674(04)00453-2 |
0.605 |
|
2004 |
Mogk A, Dougan D, Weibezahn J, Schlieker C, Turgay K, Bukau B. Broad yet high substrate specificity: the challenge of AAA+ proteins. Journal of Structural Biology. 146: 90-8. PMID 15037240 DOI: 10.1016/J.Jsb.2003.10.009 |
0.647 |
|
2003 |
Strub C, Schlieker C, Bukau B, Mogk A. Poly-L-lysine enhances the protein disaggregation activity of ClpB. Febs Letters. 553: 125-30. PMID 14550559 DOI: 10.1016/S0014-5793(03)00985-2 |
0.608 |
|
2003 |
Weibezahn J, Schlieker C, Bukau B, Mogk A. Characterization of a trap mutant of the AAA+ chaperone ClpB. The Journal of Biological Chemistry. 278: 32608-17. PMID 12805357 DOI: 10.1074/Jbc.M303653200 |
0.649 |
|
2003 |
Mogk A, Schlieker C, Friedrich KL, Schönfeld HJ, Vierling E, Bukau B. Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK. The Journal of Biological Chemistry. 278: 31033-42. PMID 12788951 DOI: 10.1074/Jbc.M303587200 |
0.64 |
|
2003 |
Mogk A, Schlieker C, Strub C, Rist W, Weibezahn J, Bukau B. Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity. The Journal of Biological Chemistry. 278: 17615-24. PMID 12624113 DOI: 10.1074/Jbc.M209686200 |
0.597 |
|
2002 |
Schlieker C, Bukau B, Mogk A. Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: implications for their applicability in biotechnology. Journal of Biotechnology. 96: 13-21. PMID 12142139 DOI: 10.1016/S0168-1656(02)00033-0 |
0.633 |
|
Low-probability matches (unlikely to be authored by this person) |
2019 |
Prophet SM, Schlieker C. An unbiased approach de-livers unexpected insight into torsin biology. The Journal of Clinical Investigation. PMID 31589164 DOI: 10.1172/Jci132442 |
0.287 |
|
2022 |
Prophet SM, Naughton BS, Schlieker C. p97/UBXD1 Generate Ubiquitylated Proteins That Are Sequestered into Nuclear Envelope Herniations in Torsin-Deficient Cells. International Journal of Molecular Sciences. 23. PMID 35563018 DOI: 10.3390/ijms23094627 |
0.287 |
|
2023 |
Kuiper EFE, Prophet SM, Schlieker C. Coordinating nucleoporin condensation and nuclear pore complex assembly. Febs Letters. PMID 37620293 DOI: 10.1002/1873-3468.14725 |
0.237 |
|
2016 |
Tsai P, Zhao C, Turner E, Schlieker C. Author response: The Lamin B receptor is essential for cholesterol synthesis and perturbed by disease-causing mutations Elife. DOI: 10.7554/Elife.16011.022 |
0.233 |
|
1999 |
Stathakis P, Lay AJ, Fitzgerald M, Schlieker C, Matthias LJ, Hogg PJ. Angiostatin formation involves disulfide bond reduction and proteolysis in kringle 5 of plasmin. The Journal of Biological Chemistry. 274: 8910-6. PMID 10085135 DOI: 10.1074/jbc.274.13.8910 |
0.158 |
|
2022 |
Stoewer P, Schlieker C, Schilling A, Metzner C, Maier A, Krauss P. Neural network based successor representations to form cognitive maps of space and language. Scientific Reports. 12: 11233. PMID 35787659 DOI: 10.1038/s41598-022-14916-1 |
0.058 |
|
Hide low-probability matches. |