Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Maurits F. Kleijnen"'
Autor:
David S. Pitcher, Kate de Mattos-Shipley, Konstantinos Tzortzis, Holger W. Auner, Anastasios Karadimitris, Maurits F. Kleijnen
Publikováno v:
EBioMedicine, Vol 2, Iss 7, Pp 642-648 (2015)
The proteasome inhibitor Bortezomib is used to treat multiple myeloma (MM). Bortezomib inhibits protein degradation by inactivating proteasomes' active-sites. MM cells are exquisitely sensitive to Bortezomib – exhibiting a low-nanomolar IC50 – su
Externí odkaz:
https://doaj.org/article/dac0543ad72f41d1be390db0bd98e837
Autor:
David S. Pitcher, Amin Rahemtulla, Irene Roberts, Maurits F. Kleijnen, Ziming Wang, Kate de Mattos-Shipley, Katerina Goudevenou, Ambrosius P. Snijders, Georg Bohn, Konstantinos N. Tzortzis, Anastasios Karadimitris, Helen R. Flynn
Publikováno v:
Europe PubMed Central
We report that subunits of human nuclear proteasomes carry a previously unrecognised, constitutive posttranslational modification. Subunits with this modification are not visualised by SDS-PAGE, which is used in almost all denaturing protein gel elec
Autor:
Katarzyna Parzych, Sandra Loaiza, F. Porsch, Holger W. Auner, Tamara M. Chinn, Hector C. Keun, Eileen Gentleman, Maurits F. Kleijnen, Anastasios Karadimitris, Z. Chen, Gabriel N. Valbuena
Publikováno v:
Parzych, K, Chinn, T M, Chen, Z, Loaiza, S, Porsch, F, Valbuena, G N, Kleijnen, M F, Karadimitris, A, Gentleman, E, Keun, H C & Auner, H W 2015, ' Inadequate fine-tuning of protein synthesis and failure of amino acid homeostasis following inhibition of the ATPase VCP/p97 ', Cell Death & Disease, vol. 6, no. 12, e2031 . https://doi.org/10.1038/cddis.2015.373
Cell Death & Disease
Cell Death & Disease
The cellular mechanisms that control protein degradation may constitute a non-oncogenic cancer cell vulnerability and, therefore, a therapeutic target. Although this proposition is supported by the clinical success of proteasome inhibitors in some ma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2021bfd29b62fc2d27aa9de8f796dc21
http://hdl.handle.net/10044/1/28796
http://hdl.handle.net/10044/1/28796
Publikováno v:
Molecular Biology of the Cell. 14:3868-3875
The ubiquitin-like hPLIC proteins can associate with proteasomes, and hPLIC overexpression can specifically interfere with ubiquitin-mediated proteolysis ( Kleijnen et al., 2000 ). Because the hPLIC proteins can also interact with certain E3 ubiquiti
Autor:
Anna K. Bassil, Binbin Liu, Valentina S. Caputo, Nigel J. Parr, Rab K. Prinjha, BaoChau Le, Trevor D. Chapman, Irene Roberts, Nicola Harker, Jason Witherington, Leanne Cutler, Niam Al-Mahdi, Anastasios Karadimitris, Antonia Rotolo, Nicholas Smithers, Ilaria Marigo, David F. Tough, Amin Rahemtulla, Maurits F. Kleijnen, Katerina Gouvedenou, Aristeidis Chaidos, Peter J. Tummino, Mohammed Suhail Chaudhry, Olena Barbash, Andrea C. Haynes
Publikováno v:
Blood. 123(5)
The bromodomain and extraterminal (BET) protein BRD2-4 inhibitors hold therapeutic promise in preclinical models of hematologic malignancies. However, translation of these data to molecules suitable for clinical development has yet to be accomplished
Autor:
Raymond E. Soccio, Sushant Kumar, Grace Gill, Alan H. Shih, Pengbo Zhou, Maurits F. Kleijnen, Nancy Kedersha, Peter M. Howley
Publikováno v:
Molecular Cell. 6(2):409-419
Although there is a binding site on the proteasome for the polyubiquitin chains attached to degradation substrates by the ubiquitination machinery, it is currently unclear whether in vivo the activities of the ubiquitination machinery and the proteas
Autor:
Maurits F. Kleijnen, Ann B. Hill, Siddhartha Mukherjee, Pero Lučin, Ulrich H. Koszinowski, Ann E. Campbell, Hidde L. Ploegh, Helen E. Farrell, Johannes B. Huppa
Publikováno v:
The EMBO Journal. 16:685-694
Murine cytomegalovirus (MCMV) interferes with antigen presentation by means of retaining major histocompatibility complex (MHC) class I molecules in the endoplasmic reticulum (ER). Here we identify and characterize an MCMV-encoded glycoprotein, gp34,
Autor:
Randall W. King, Daniel Finley, Michael H. Glickman, Jeroen Roelofs, Soyeon Park, Maurits F. Kleijnen, Nathaniel A. Hathaway
Publikováno v:
Nature structuralmolecular biology. 14(12)
The 26S proteasome holoenzyme is formed by the association of a 20S core particle (CP) with a 19S regulatory particle (RP). The CP-RP interaction is labile and subject to regulation in vivo, but the factors controlling this association are poorly und
Ubiquitination is known to regulate early stages of intracellular vesicular transport, without proteasomal involvement. We now show that, in yeast, ubiquitination regulates a late-stage, membrane fusion, with proteasomal involvement. A known proteaso
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e1d8391e9d9820e790e3eb027fee102
https://europepmc.org/articles/PMC1783458/
https://europepmc.org/articles/PMC1783458/
Publikováno v:
Biochemistry. 41(6)
The 26S proteasome is essential for the proteolysis of proteins that have been covalently modified by the attachment of polyubiquitinated chains. Although the 20S core particle performs the degradation, the 19S regulatory cap complex is responsible f