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Sumit Prakash, Ph.D. - Publications

Affiliations: 
2007 Biochemistry and Molecular Biology Northwestern University, Evanston, IL 
 2016 Chemistry and Chemical Biology University of California, San Francisco, San Francisco, CA 
Area:
Cancer Signaling
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20 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2022 Bashore C, Prakash S, Johnson MC, Conrad RJ, Kekessie IA, Scales SJ, Ishisoko N, Kleinheinz T, Liu PS, Popovych N, Wecksler AT, Zhou L, Tam C, Zilberleyb I, Srinivasan R, et al. Targeted degradation via direct 26S proteasome recruitment. Nature Chemical Biology. 19: 55-63. PMID 36577875 DOI: 10.1038/s41589-022-01218-w  0.39
2021 Cockram PE, Kist M, Prakash S, Chen SH, Wertz IE, Vucic D. Ubiquitination in the regulation of inflammatory cell death and cancer. Cell Death and Differentiation. 28: 591-605. PMID 33432113 DOI: 10.1038/s41418-020-00708-5  0.34
2018 Wertz I, Kategaya L, Lello PD, Rouge L, Pastor R, Clark KR, Drummond J, Kleinheinz T, Lin E, Upton J, Prakash S, Heideker J, McCleland M, Ritorto MS, Alessi DR, et al. Abstract SY23-03: Development and mechanistic characterization of USP7 deubiquitinase inhibitors Cancer Research. 78. DOI: 10.1158/1538-7445.Am2018-Sy23-03  0.486
2017 Kategaya L, Di Lello P, Rougé L, Pastor R, Clark KR, Drummond J, Kleinheinz T, Lin E, Upton JP, Prakash S, Heideker J, McCleland M, Ritorto MS, Alessi DR, Trost M, et al. USP7 small-molecule inhibitors interfere with ubiquitin binding. Nature. PMID 29045385 DOI: 10.1038/Nature24006  0.502
2015 Okrut J, Prakash S, Wu Q, Kelly MJ, Taunton J. Allosteric N-WASP activation by an inter-SH3 domain linker in Nck. Proceedings of the National Academy of Sciences of the United States of America. PMID 26554011 DOI: 10.1073/Pnas.1510876112  0.541
2011 Fishbain S, Prakash S, Herrig A, Elsasser S, Matouschek A. Rad23 escapes degradation because it lacks a proteasome initiation region. Nature Communications. 2: 192. PMID 21304521 DOI: 10.1038/Ncomms1194  0.738
2011 Inobe T, Fishbain S, Prakash S, Matouschek A. Defining the geometry of the two-component proteasome degron. Nature Chemical Biology. 7: 161-7. PMID 21278740 DOI: 10.1038/Nchembio.521  0.751
2010 Inobe T, Prakash S, Fishbain S, Matouschek A. 1P034 1YA0915 Defining the geometry of the two-component proteasome degron(Protein:Structure & Function,Early Research in Biophysics Award Candidate Presentations,Early Research in Biophysics Award,The 48th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 50: S24-S25. DOI: 10.2142/Biophys.50.S24_5  0.609
2009 Koodathingal P, Jaffe NE, Kraut DA, Prakash S, Fishbain S, Herman C, Matouschek A. ATP-dependent proteases differ substantially in their ability to unfold globular proteins. The Journal of Biological Chemistry. 284: 18674-84. PMID 19383601 DOI: 10.1074/Jbc.M900783200  0.692
2009 Prakash S, Inobe T, Hatch AJ, Matouschek A. Substrate selection by the proteasome during degradation of protein complexes. Nature Chemical Biology. 5: 29-36. PMID 19029916 DOI: 10.1038/Nchembio.130  0.772
2009 Inobe T, Fishbain S, Prakash S, Matouschek A. 2TA1-03 Optimal spacing between ubiquitin modification and unstructured initiation site for efficient proteasome-mediated degradation(The 47th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 49: S39. DOI: 10.2142/Biophys.49.S39_2  0.587
2008 Mohammad MM, Prakash S, Matouschek A, Movileanu L. Controlling a single protein in a nanopore through electrostatic traps. Journal of the American Chemical Society. 130: 4081-8. PMID 18321107 DOI: 10.1021/Ja710787A  0.719
2007 Kraut DA, Prakash S, Matouschek A. To degrade or release: ubiquitin-chain remodeling. Trends in Cell Biology. 17: 419-21. PMID 17900906 DOI: 10.1016/J.Tcb.2007.06.008  0.757
2007 Inobe T, Prakash S, Tian L, Matouschek A. 1P041 SELECTING PROTEINS FOR DEGRADATION: THE INITIATION STEP(Proteins-functions, methodology, and protein enigineering,Oral Presentations) Seibutsu Butsuri. 47: S33. DOI: 10.2142/Biophys.47.S33_4  0.733
2004 Prakash S, Matouschek A. Protein unfolding in the cell. Trends in Biochemical Sciences. 29: 593-600. PMID 15501678 DOI: 10.1016/J.Tibs.2004.09.011  0.773
2004 Prakash S, Tian L, Ratliff KS, Lehotzky RE, Matouschek A. An unstructured initiation site is required for efficient proteasome-mediated degradation Nature Structural and Molecular Biology. 11: 830-837. PMID 15311270 DOI: 10.1038/Nsmb814  0.766
2003 Herman C, Prakash S, Lu CZ, Matouschek A, Gross CA. Lack of a robust unfoldase activity confers a unique level of substrate specificity to the universal AAA protease FtsH. Molecular Cell. 11: 659-69. PMID 12667449 DOI: 10.1016/S1097-2765(03)00068-6  0.729
2002 Lee C, Prakash S, Matouschek A. Concurrent translocation of multiple polypeptide chains through the proteasomal degradation channel. The Journal of Biological Chemistry. 277: 34760-5. PMID 12080075 DOI: 10.1074/Jbc.M204750200  0.729
2001 Lee C, Schwartz MP, Prakash S, Iwakura M, Matouschek A. ATP-Dependent Proteases Degrade Their Substrates by Processively Unraveling Them from the Degradation Signal Molecular Cell. 7: 627-637. PMID 11463387 DOI: 10.1016/S1097-2765(01)00209-X  0.759
2001 Lee C, Schwartz MP, Prakash S, Iwakura M, Matouschek A.. ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. Mol Cell.. 7: 627-37.. DOI: https://doi.org/10.1016/S1097-2765(01)00209-X  0.317
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