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English
The proteasome: a novel target for cancer chemotherapy
scientific article (publication date: April 2002)
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scholarly article
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review article
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Europe PubMed Central
title
The proteasome: a novel target for cancer chemotherapy
(English)
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main subject
chemotherapy
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author name string
J B Almond
series ordinal
1
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G M Cohen
series ordinal
2
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language of work or name
English
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publication date
April 2002
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published in
Leukemia
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volume
16
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page(s)
433-43
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issue
4
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cites work
The ubiquitin-proteasome proteolytic pathway
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Crossref
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7 January 2021
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Subcellular localization of proteasomes and their regulatory complexes in mammalian cells.
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Self-compartmentalizing proteases.
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7 January 2021
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The proteasome: paradigm of a self-compartmentalizing protease
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7 January 2021
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The ubiquitin system
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7 January 2021
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The ubiquitin system
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Proteasome inhibitors as anti-cancer agents.
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reference URL
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7 January 2021
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Roles of ubiquitin-mediated proteolysis in cell cycle control
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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How proteolysis drives the cell cycle
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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The role of the ubiquitin-proteasome pathway in apoptosis
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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The ubiquitin-proteasome pathway in cancer
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7 January 2021
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Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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Protein complexes activate distinct caspase cascades in death receptor and stress-induced apoptosis
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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Apaf-1 oligomerizes into biologically active approximately 700-kDa and inactive approximately 1.4-MDa apoptosome complexes
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reference URL
https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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inferred from DOI database lookup
Caspases: the executioners of apoptosis
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Mammalian caspases: structure, activation, substrates, and functions during apoptosis
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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Caspase structure, proteolytic substrates, and function during apoptotic cell death
1 reference
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7 January 2021
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Ubiquitin-mediated degradation of the proapoptotic active form of bid. A functional consequence on apoptosis induction
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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Bax degradation by the ubiquitin/proteasome-dependent pathway: involvement in tumor survival and progression
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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Proteasomes modulate balance among proapoptotic and antiapoptotic Bcl-2 family members and compromise functioning of the electron transport chain in leukemic cells
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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Proteasome inhibitors: valuable new tools for cell biologists
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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inferred from DOI database lookup
Proteasome inhibition: a new strategy in cancer treatment
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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Mechanistic studies on the inactivation of the proteasome by lactacystin: a central role for clasto-lactacystin beta-lactone
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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inferred from DOI database lookup
Lactacystin, proteasome function, and cell fate
1 reference
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reference URL
https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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Potent and selective inhibitors of the proteasome: dipeptidyl boronic acids
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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Activation of the cell death program by inhibition of proteasome function
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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Proteasome inhibitor-induced apoptosis of B-chronic lymphocytic leukaemia cells involves cytochrome c release and caspase activation, accompanied by formation of an approximately 700 kDa Apaf-1 containing apoptosome complex
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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The proteasome inhibitor lactacystin induces apoptosis and sensitizes chemo- and radioresistant human chronic lymphocytic leukaemia lymphocytes to TNF-alpha-initiated apoptosis
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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inferred from DOI database lookup
Increased sensitivity of CLL-derived lymphocytes to apoptotic death activation by the proteasome-specific inhibitor lactacystin
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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inferred from DOI database lookup
Ubiquitin-proteasome system and increased sensitivity of B-CLL lymphocytes to apoptotic death activation
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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inferred from DOI database lookup
Inhibition of etoposide-induced apoptosis with peptide aldehyde inhibitors of proteasome
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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inferred from DOI database lookup
Proteasomes play an essential role in thymocyte apoptosis
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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Involvement of the proteasome in the programmed cell death of NGF-deprived sympathetic neurons.
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7 January 2021
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Prevention of etoposide-induced apoptosis by proteasome inhibitors in a human leukemic cell line but not in fresh acute leukemia blasts. A differential role of NF-kappab activation
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
based on heuristic
inferred from DOI database lookup
Proteasome inhibitors activate stress kinases and induce Hsp72. Diverse effects on apoptosis
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
based on heuristic
inferred from DOI database lookup
p53 mutations in human cancers
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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Apoptotic death sensor: an organelle's alter ego?
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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Surfing the p53 network
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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inferred from DOI database lookup
p53-dependent induction of apoptosis by proteasome inhibitors
1 reference
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reference URL
https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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inferred from DOI database lookup
Novel dipeptidyl proteasome inhibitors overcome Bcl-2 protective function and selectively accumulate the cyclin-dependent kinase inhibitor p27 and induce apoptosis in transformed, but not normal, human fibroblasts
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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Prostate carcinoma cell death resulting from inhibition of proteasome activity is independent of functional Bcl-2 and p53
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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Inhibition of proteasome function induces programmed cell death in proliferating endothelial cells
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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p27kip1: a multifunctional cyclin-dependent kinase inhibitor with prognostic significance in human cancers
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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inferred from DOI database lookup
Diverse functions of JNK signaling and c-Jun in stress response and apoptosis
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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inferred from DOI database lookup
Translocation of SAPK/JNK to mitochondria and interaction with Bcl-x(L) in response to DNA damage
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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inferred from DOI database lookup
Requirement of JNK for stress-induced activation of the cytochrome c-mediated death pathway
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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inferred from DOI database lookup
Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-kappaB control
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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inferred from DOI database lookup
ch-IAP1, a member of the inhibitor-of-apoptosis protein family, is a mediator of the antiapoptotic activity of the v-Rel oncoprotein
1 reference
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reference URL
https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
based on heuristic
inferred from DOI database lookup
NF-kappaB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
based on heuristic
inferred from DOI database lookup
The prosurvival Bcl-2 homolog Bfl-1/A1 is a direct transcriptional target of NF-kappaB that blocks TNFalpha-induced apoptosis
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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inferred from DOI database lookup
Rel-dependent induction of A1 transcription is required to protect B cells from antigen receptor ligation-induced apoptosis
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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The proteasome is involved in angiogenesis
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
based on heuristic
inferred from DOI database lookup
Proteasome inhibitors as potential novel anticancer agents
1 reference
stated in
Crossref
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
based on heuristic
inferred from DOI database lookup
Resistance to diverse drugs and ultraviolet light conferred by overexpression of a novel human 26 S proteasome subunit
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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inferred from DOI database lookup
Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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inferred from DOI database lookup
Caspase activation involves the formation of the aposome, a large (approximately 700 kDa) caspase-activating complex
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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inferred from DOI database lookup
Recruitment, activation and retention of caspases-9 and -3 by Apaf-1 apoptosome and associated XIAP complexes
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
based on heuristic
inferred from DOI database lookup
An inhibitor of HIV-1 protease modulates proteasome activity, antigen presentation, and T cell responses
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
based on heuristic
inferred from DOI database lookup
Apaf-1 and caspase-9 in p53-dependent apoptosis and tumor inhibition.
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
based on heuristic
inferred from DOI database lookup
Eponemycin analogues: syntheses and use as probes of angiogenesis.
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
based on heuristic
inferred from DOI database lookup
Lactacystin, a specific inhibitor of the proteasome, induces apoptosis in human monoblast U937 cells
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Apoptosis induction resulting from proteasome inhibition
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Inhibition of Proteasome Function Prevents Thymocyte Apoptosis: Involvement of Ornithine Decarboxylase
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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Inhibition versus induction of apoptosis by proteasome inhibitors depends on concentration
1 reference
stated in
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reference URL
https://api.crossref.org/works/10.1038%2FSJ.LEU.2402417
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7 January 2021
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Identifiers
DOI
10.1038/SJ.LEU.2402417
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3200128
Dimensions Publication ID
1044065576
0 references
OpenCitations bibliographic resource ID
3200128
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3200128
PubMed ID
11960320
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3200128
ResearchGate publication ID
11407704
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Springer Nature article ID
10.1038/sj.leu.2402417
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