Ragwan E, Kisker F, Morning A, Weiser K, Lago A, Kraut D
Protein Sci. 2024; 33(6):e5034.
PMID: 38801231
PMC: 11129623.
DOI: 10.1002/pro.5034.
Barman P, Chakraborty P, Bhaumik R, Bhaumik S
Biochim Biophys Acta Gene Regul Mech. 2023; 1866(4):194981.
PMID: 37657588
PMC: 10843445.
DOI: 10.1016/j.bbagrm.2023.194981.
Taylor G, Cui H, Leodolter J, Giese C, Weber-Ban E
Commun Biol. 2023; 6(1):301.
PMID: 36944713
PMC: 10030653.
DOI: 10.1038/s42003-023-04658-9.
Oliveira B, de Almeida A, Pirovani C, Barroso J, de C Neto C, Santos N
Ecotoxicology. 2020; 29(3):340-358.
PMID: 32107699
DOI: 10.1007/s10646-020-02178-4.
Uversky V
Intrinsically Disord Proteins. 2017; 1(1):e26782.
PMID: 28516024
PMC: 5424783.
DOI: 10.4161/idp.26782.
Valosin-containing protein (VCP/p97) is capable of unfolding polyubiquitinated proteins through its ATPase domains.
Song C, Wang Q, Song C, Rogers T
Biochem Biophys Res Commun. 2015; 463(3):453-7.
PMID: 26043696
PMC: 4470855.
DOI: 10.1016/j.bbrc.2015.05.111.
Conditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function.
Jakob U, Kriwacki R, Uversky V
Chem Rev. 2014; 114(13):6779-805.
PMID: 24502763
PMC: 4090257.
DOI: 10.1021/cr400459c.
Archaeal proteasomes and sampylation.
Maupin-Furlow J
Subcell Biochem. 2013; 66:297-327.
PMID: 23479445
PMC: 3936409.
DOI: 10.1007/978-94-007-5940-4_11.
Defining the geometry of the two-component proteasome degron.
Inobe T, Fishbain S, Prakash S, Matouschek A
Nat Chem Biol. 2011; 7(3):161-7.
PMID: 21278740
PMC: 3129032.
DOI: 10.1038/nchembio.521.
Distinct regulatory mechanisms of eukaryotic transcriptional activation by SAGA and TFIID.
Bhaumik S
Biochim Biophys Acta. 2010; 1809(2):97-108.
PMID: 20800707
PMC: 3018551.
DOI: 10.1016/j.bbagrm.2010.08.009.
Jostling for position: optimizing linker location in the design of estrogen receptor-targeting PROTACs.
Cyrus K, Wehenkel M, Choi E, Lee H, Swanson H, Kim K
ChemMedChem. 2010; 5(7):979-85.
PMID: 20512796
PMC: 3516907.
DOI: 10.1002/cmdc.201000146.
The 19 s proteasome subcomplex establishes a specific protein interaction network at the promoter for stimulated transcriptional initiation in vivo.
Malik S, Shukla A, Sen P, Bhaumik S
J Biol Chem. 2009; 284(51):35714-24.
PMID: 19843524
PMC: 2791002.
DOI: 10.1074/jbc.M109.035709.
Recognition and processing of ubiquitin-protein conjugates by the proteasome.
Finley D
Annu Rev Biochem. 2009; 78:477-513.
PMID: 19489727
PMC: 3431160.
DOI: 10.1146/annurev.biochem.78.081507.101607.
Architecture and molecular mechanism of PAN, the archaeal proteasome regulatory ATPase.
Medalia N, Beer A, Zwickl P, Mihalache O, Beck M, Medalia O
J Biol Chem. 2009; 284(34):22952-60.
PMID: 19363223
PMC: 2755702.
DOI: 10.1074/jbc.M809643200.
Functional and biochemical characterization of the 20S proteasome in a yeast temperature-sensitive mutant, rpt6-1.
Chouduri A, Tokumoto T, Dohra H, Ushimaru T, Yamada S
BMC Biochem. 2008; 9:20.
PMID: 18644121
PMC: 2515314.
DOI: 10.1186/1471-2091-9-20.
Interplay of PDZ and protease domain of DegP ensures efficient elimination of misfolded proteins.
Krojer T, Pangerl K, Kurt J, Sawa J, Stingl C, Mechtler K
Proc Natl Acad Sci U S A. 2008; 105(22):7702-7.
PMID: 18505836
PMC: 2396557.
DOI: 10.1073/pnas.0803392105.
A comprehensive genetic study of the proteasomal subunit S6 ATPase in German Parkinson's disease patients.
Wahl C, Kautzmann S, Krebiehl G, Strauss K, Woitalla D, Muller T
J Neural Transm (Vienna). 2008; 115(8):1141-8.
PMID: 18446261
DOI: 10.1007/s00702-008-0054-3.
Protein targeting to ATP-dependent proteases.
Inobe T, Matouschek A
Curr Opin Struct Biol. 2008; 18(1):43-51.
PMID: 18276129
PMC: 2346608.
DOI: 10.1016/j.sbi.2007.12.014.
Rooting the tree of life by transition analyses.
Cavalier-Smith T
Biol Direct. 2006; 1:19.
PMID: 16834776
PMC: 1586193.
DOI: 10.1186/1745-6150-1-19.
Ligand binding modulates the mechanical stability of dihydrofolate reductase.
Ainavarapu S, Li L, Badilla C, Fernandez J
Biophys J. 2005; 89(5):3337-44.
PMID: 16100277
PMC: 1366830.
DOI: 10.1529/biophysj.105.062034.