N
Noa Reis
Researcher at Technion – Israel Institute of Technology
Publications - 17
Citations - 1212
Noa Reis is an academic researcher from Technion – Israel Institute of Technology. The author has contributed to research in topics: Proteasome & Ubiquitin. The author has an hindex of 13, co-authored 16 publications receiving 1072 citations.
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Journal ArticleDOI
Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome
TL;DR: Comprehensive subunit interaction maps for the 26S proteasome and CSN support the ancestral relationship of these two complexes.
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MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function
TL;DR: The putative catalytic nature of the MPN+ motif makes it a good candidate for a pivotal enzymatic function, possibly a proteasome-associated deubiquitinating activity and a CSN-associated Nedd8/Rub1-removing activity.
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Reversible 26S Proteasome Disassembly upon Mitochondrial Stress
Nurit Livnat-Levanon,Éva Kevei,Oded Kleifeld,Daria Krutauz,Alexandra Segref,Teresa Rinaldi,Zoi Erpapazoglou,Mickael M. Cohen,Noa Reis,Thorsten Hoppe,Michael H. Glickman +10 more
TL;DR: It is shown that acute oxidative stress caused by environmental insults or mitochondrial defects results in rapid disassembly of 26S proteasomes into intact 20S core and 19S regulatory particles, and polyubiquitinated substrates accumulate, mitochondrial networks fragment, and cellular reactive oxygen species (ROS) levels increase.
Journal ArticleDOI
A perturbed ubiquitin landscape distinguishes between ubiquitin in trafficking and in proteolysis
Inbal Ziv,Yulia Matiuhin,Donald S. Kirkpatrick,Zoi Erpapazoglou,Sébastien Léon,Marina Pantazopoulou,Woong Kim,Steven P. Gygi,Rosine Haguenauer-Tsapis,Noa Reis,Michael H. Glickman,Oded Kleifeld +11 more
TL;DR: It is concluded that despite the shared use of the ubiquitin molecule, the two branches of the Ubiquitin machinery—the ubiquit in-proteasome system and the ubiqu itin trafficking system—were unevenly perturbed by expression of K0 Ub.
Journal ArticleDOI
Extraproteasomal Rpn10 Restricts Access of the Polyubiquitin-Binding Protein Dsk2 to Proteasome
Yulia Matiuhin,Donald S. Kirkpatrick,Inbal Ziv,Woong Kim,Arun Dakshinamurthy,Oded Kleifeld,Steven P. Gygi,Noa Reis,Michael H. Glickman +8 more
TL;DR: By restricting Dsk2 access to the proteasome, extraproteasomal Rpn10 was essential for alleviating the cellular stress associated with DSk2, highlighting the importance of polyubiquitin shuttles such as RPN10 and Dsk1 in controlling the ubiquitin landscape.