Proteasome inhibitors as therapeutic agents: Current and future strategies
Identifieur interne : 000F45 ( PascalFrancis/Corpus ); précédent : 000F44; suivant : 000F46Proteasome inhibitors as therapeutic agents: Current and future strategies
Auteurs : J. G. Delcros ; M. Baudy Floc'H ; C. Prigent ; Y. Arlot-BonnemainsSource :
- Current medicinal chemistry [ 0929-8673 ] ; 2003.
Descripteurs français
- Pascal (Inist)
- Article synthèse, Recherche développement, Relation structure activité, Inhibiteur enzyme, Multicatalytic endopeptidase complex, Localisation, Intracellulaire, Ubiquitine, Anticancéreux, Maladie dégénérative, Système nerveux central pathologie, Système nerveux pathologie, Encéphale pathologie, Démence Alzheimer, Parkinson maladie, Chorée Huntington, Cachexie, Muscle strié pathologie, Produit synthétique, Pseudopeptide, Peptide cyclique, Composé non peptide, Composé peptidomimétique, Hydrazide organique, Carbazate organique, Aldéhyde.
English descriptors
- KwdEn :
- Aldehyde, Alzheimer disease, Antineoplastic agent, Cachexia, Central nervous system disease, Cerebral disorder, Cyclic peptides, Degenerative disease, Enzyme inhibitor, Huntington disease, Intracellular, Localization, Multicatalytic endopeptidase complex, Nervous system diseases, Non peptide compound, Organic carbazate, Organic hydrazide, Parkinson disease, Peptidomimetic compound, Pseudopeptide, Research and development, Review, Striated muscle disease, Structure activity relation, Synthetic product, Ubiquitin.
Abstract
In cells, protein degradation is a key pathway for the destruction of abnormal or damaged proteins as well as for the elimination of proteins whose presence is no longer required. Among the various cell proteases, the proteasome, a multicatalytic macromolecular complex, is specifically required for the degradation of ubiquitinated proteins. In normal cells, the proteasome ensures the elimination of numerous proteins that play critical roles in cell functions throughout the cell cycle. Defects in the activity of this proteolytic machinery can lead to the disorders of cell function that is believed to be the root cause of certain diseases. Indeed, many proteins involved in the control of cell cycle transitions are readily destroyed by the proteasome once their tasks have been accomplished. Moreover, because proteasome inhibitors can provoke cell death, it has been suggested that proteasomes must be continually degrading certain apoptotic factors. For these reasons, proteasome inhibition has become a new and potentially significant strategy for the drug development in cancer treatment. The proteasome possesses three major peptidase activities that can individually be targeted by drugs. Different classes of proteasome inhibitors are reviewed here. In addition, we present new pseudopeptides with the enriched nitrogen backbones bearing a side chain and a modified C-terminal position that inhibit proteasome activity.
Notice en format standard (ISO 2709)
Pour connaître la documentation sur le format Inist Standard.
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Format Inist (serveur)
NO : | PASCAL 03-0297215 INIST |
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ET : | Proteasome inhibitors as therapeutic agents: Current and future strategies |
AU : | DELCROS (J. G.); BAUDY FLOC'H (M.); PRIGENT (C.); ARLOT-BONNEMAINS (Y.) |
AF : | Groupe de Recherche en Thérapeutique Anticancéreuse, Faculté de Médecine, Université Rennes 1, 2 avenue du Professeur Léon Bernard, CS34317/35043 Rennes/France (1 aut.); Laboratoire de Synthèse et Electrosynthése Organiques (SESO), UMR CNRS 6510, Institut de Chimie, Université Rennes 1, 263 Avenue du Général Leclerc, CS74205/35042 Rennes/France (2 aut.); Groupe Cycle Cellulaire, CNRS UMR 6061 Génétique et Développement, IFR 97 Génomique Fonctionnelle et Santé, Faculté de Médecine, Université Rennes 1, 2 av du Pr Léon Bernard, CS 34317/35043 Rennes/France (3 aut., 4 aut.) |
DT : | Publication en série; Niveau analytique |
SO : | Current medicinal chemistry; ISSN 0929-8673; Pays-Bas; Da. 2003; Vol. 10; No. 6; Pp. 479-503; Bibl. 271 ref. |
LA : | Anglais |
EA : | In cells, protein degradation is a key pathway for the destruction of abnormal or damaged proteins as well as for the elimination of proteins whose presence is no longer required. Among the various cell proteases, the proteasome, a multicatalytic macromolecular complex, is specifically required for the degradation of ubiquitinated proteins. In normal cells, the proteasome ensures the elimination of numerous proteins that play critical roles in cell functions throughout the cell cycle. Defects in the activity of this proteolytic machinery can lead to the disorders of cell function that is believed to be the root cause of certain diseases. Indeed, many proteins involved in the control of cell cycle transitions are readily destroyed by the proteasome once their tasks have been accomplished. Moreover, because proteasome inhibitors can provoke cell death, it has been suggested that proteasomes must be continually degrading certain apoptotic factors. For these reasons, proteasome inhibition has become a new and potentially significant strategy for the drug development in cancer treatment. The proteasome possesses three major peptidase activities that can individually be targeted by drugs. Different classes of proteasome inhibitors are reviewed here. In addition, we present new pseudopeptides with the enriched nitrogen backbones bearing a side chain and a modified C-terminal position that inhibit proteasome activity. |
CC : | 002B02R01 |
FD : | Article synthèse; Recherche développement; Relation structure activité; Inhibiteur enzyme; Multicatalytic endopeptidase complex; Localisation; Intracellulaire; Ubiquitine; Anticancéreux; Maladie dégénérative; Système nerveux central pathologie; Système nerveux pathologie; Encéphale pathologie; Démence Alzheimer; Parkinson maladie; Chorée Huntington; Cachexie; Muscle strié pathologie; Produit synthétique; Pseudopeptide; Peptide cyclique; Composé non peptide; Composé peptidomimétique; Hydrazide organique; Carbazate organique; Aldéhyde |
FG : | Peptidases; Hydrolases; Enzyme |
ED : | Review; Research and development; Structure activity relation; Enzyme inhibitor; Multicatalytic endopeptidase complex; Localization; Intracellular; Ubiquitin; Antineoplastic agent; Degenerative disease; Central nervous system disease; Nervous system diseases; Cerebral disorder; Alzheimer disease; Parkinson disease; Huntington disease; Cachexia; Striated muscle disease; Synthetic product; Pseudopeptide; Cyclic peptides; Non peptide compound; Peptidomimetic compound; Organic hydrazide; Organic carbazate; Aldehyde |
EG : | Peptidases; Hydrolases; Enzyme |
SD : | Artículo síntesis; Investigación desarrollo; Relación estructura actividad; Inhibidor enzima; Multicatalytic endopeptidase complex; Localización; Intracelular; Ubiquitina; Anticanceroso; Enfermedad degenerativa; Sistema nervosio central patología; Sistema nervioso patología; Encéfalo patología; Demencia Alzheimer; Parkinson enfermedad; Corea Huntington; Caquexia; Músculo estriado patología; Producto sintético; Seudopéptido; Péptido cíclico; Compuesto no péptido; Compuesto peptidomimético; Hidrácida orgánica; Carbazato orgánico; Aldehído |
LO : | INIST-22999.354000111020770030 |
ID : | 03-0297215 |
Links to Exploration step
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<front><div type="abstract" xml:lang="en">In cells, protein degradation is a key pathway for the destruction of abnormal or damaged proteins as well as for the elimination of proteins whose presence is no longer required. Among the various cell proteases, the proteasome, a multicatalytic macromolecular complex, is specifically required for the degradation of ubiquitinated proteins. In normal cells, the proteasome ensures the elimination of numerous proteins that play critical roles in cell functions throughout the cell cycle. Defects in the activity of this proteolytic machinery can lead to the disorders of cell function that is believed to be the root cause of certain diseases. Indeed, many proteins involved in the control of cell cycle transitions are readily destroyed by the proteasome once their tasks have been accomplished. Moreover, because proteasome inhibitors can provoke cell death, it has been suggested that proteasomes must be continually degrading certain apoptotic factors. For these reasons, proteasome inhibition has become a new and potentially significant strategy for the drug development in cancer treatment. The proteasome possesses three major peptidase activities that can individually be targeted by drugs. Different classes of proteasome inhibitors are reviewed here. In addition, we present new pseudopeptides with the enriched nitrogen backbones bearing a side chain and a modified C-terminal position that inhibit proteasome activity.</div>
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<s5>16</s5>
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<fC03 i1="13" i2="X" l="ENG"><s0>Cerebral disorder</s0>
<s5>16</s5>
</fC03>
<fC03 i1="13" i2="X" l="SPA"><s0>Encéfalo patología</s0>
<s5>16</s5>
</fC03>
<fC03 i1="14" i2="X" l="FRE"><s0>Démence Alzheimer</s0>
<s5>18</s5>
</fC03>
<fC03 i1="14" i2="X" l="ENG"><s0>Alzheimer disease</s0>
<s5>18</s5>
</fC03>
<fC03 i1="14" i2="X" l="SPA"><s0>Demencia Alzheimer</s0>
<s5>18</s5>
</fC03>
<fC03 i1="15" i2="X" l="FRE"><s0>Parkinson maladie</s0>
<s5>19</s5>
</fC03>
<fC03 i1="15" i2="X" l="ENG"><s0>Parkinson disease</s0>
<s5>19</s5>
</fC03>
<fC03 i1="15" i2="X" l="SPA"><s0>Parkinson enfermedad</s0>
<s5>19</s5>
</fC03>
<fC03 i1="16" i2="X" l="FRE"><s0>Chorée Huntington</s0>
<s5>20</s5>
</fC03>
<fC03 i1="16" i2="X" l="ENG"><s0>Huntington disease</s0>
<s5>20</s5>
</fC03>
<fC03 i1="16" i2="X" l="SPA"><s0>Corea Huntington</s0>
<s5>20</s5>
</fC03>
<fC03 i1="17" i2="X" l="FRE"><s0>Cachexie</s0>
<s5>22</s5>
</fC03>
<fC03 i1="17" i2="X" l="ENG"><s0>Cachexia</s0>
<s5>22</s5>
</fC03>
<fC03 i1="17" i2="X" l="SPA"><s0>Caquexia</s0>
<s5>22</s5>
</fC03>
<fC03 i1="18" i2="X" l="FRE"><s0>Muscle strié pathologie</s0>
<s5>23</s5>
</fC03>
<fC03 i1="18" i2="X" l="ENG"><s0>Striated muscle disease</s0>
<s5>23</s5>
</fC03>
<fC03 i1="18" i2="X" l="SPA"><s0>Músculo estriado patología</s0>
<s5>23</s5>
</fC03>
<fC03 i1="19" i2="X" l="FRE"><s0>Produit synthétique</s0>
<s5>24</s5>
</fC03>
<fC03 i1="19" i2="X" l="ENG"><s0>Synthetic product</s0>
<s5>24</s5>
</fC03>
<fC03 i1="19" i2="X" l="SPA"><s0>Producto sintético</s0>
<s5>24</s5>
</fC03>
<fC03 i1="20" i2="X" l="FRE"><s0>Pseudopeptide</s0>
<s5>25</s5>
</fC03>
<fC03 i1="20" i2="X" l="ENG"><s0>Pseudopeptide</s0>
<s5>25</s5>
</fC03>
<fC03 i1="20" i2="X" l="SPA"><s0>Seudopéptido</s0>
<s5>25</s5>
</fC03>
<fC03 i1="21" i2="X" l="FRE"><s0>Peptide cyclique</s0>
<s5>26</s5>
</fC03>
<fC03 i1="21" i2="X" l="ENG"><s0>Cyclic peptides</s0>
<s5>26</s5>
</fC03>
<fC03 i1="21" i2="X" l="SPA"><s0>Péptido cíclico</s0>
<s5>26</s5>
</fC03>
<fC03 i1="22" i2="X" l="FRE"><s0>Composé non peptide</s0>
<s5>27</s5>
</fC03>
<fC03 i1="22" i2="X" l="ENG"><s0>Non peptide compound</s0>
<s5>27</s5>
</fC03>
<fC03 i1="22" i2="X" l="SPA"><s0>Compuesto no péptido</s0>
<s5>27</s5>
</fC03>
<fC03 i1="23" i2="X" l="FRE"><s0>Composé peptidomimétique</s0>
<s5>28</s5>
</fC03>
<fC03 i1="23" i2="X" l="ENG"><s0>Peptidomimetic compound</s0>
<s5>28</s5>
</fC03>
<fC03 i1="23" i2="X" l="SPA"><s0>Compuesto peptidomimético</s0>
<s5>28</s5>
</fC03>
<fC03 i1="24" i2="X" l="FRE"><s0>Hydrazide organique</s0>
<s5>29</s5>
</fC03>
<fC03 i1="24" i2="X" l="ENG"><s0>Organic hydrazide</s0>
<s5>29</s5>
</fC03>
<fC03 i1="24" i2="X" l="SPA"><s0>Hidrácida orgánica</s0>
<s5>29</s5>
</fC03>
<fC03 i1="25" i2="X" l="FRE"><s0>Carbazate organique</s0>
<s5>30</s5>
</fC03>
<fC03 i1="25" i2="X" l="ENG"><s0>Organic carbazate</s0>
<s5>30</s5>
</fC03>
<fC03 i1="25" i2="X" l="SPA"><s0>Carbazato orgánico</s0>
<s5>30</s5>
</fC03>
<fC03 i1="26" i2="X" l="FRE"><s0>Aldéhyde</s0>
<s5>32</s5>
</fC03>
<fC03 i1="26" i2="X" l="ENG"><s0>Aldehyde</s0>
<s5>32</s5>
</fC03>
<fC03 i1="26" i2="X" l="SPA"><s0>Aldehído</s0>
<s5>32</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE"><s0>Peptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Peptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Peptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="FRE"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="ENG"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="SPA"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="03" i2="X" l="FRE"><s0>Enzyme</s0>
</fC07>
<fC07 i1="03" i2="X" l="ENG"><s0>Enzyme</s0>
</fC07>
<fC07 i1="03" i2="X" l="SPA"><s0>Enzima</s0>
</fC07>
<fN21><s1>195</s1>
</fN21>
<fN82><s1>PSI</s1>
</fN82>
</pA>
</standard>
<server><NO>PASCAL 03-0297215 INIST</NO>
<ET>Proteasome inhibitors as therapeutic agents: Current and future strategies</ET>
<AU>DELCROS (J. G.); BAUDY FLOC'H (M.); PRIGENT (C.); ARLOT-BONNEMAINS (Y.)</AU>
<AF>Groupe de Recherche en Thérapeutique Anticancéreuse, Faculté de Médecine, Université Rennes 1, 2 avenue du Professeur Léon Bernard, CS34317/35043 Rennes/France (1 aut.); Laboratoire de Synthèse et Electrosynthése Organiques (SESO), UMR CNRS 6510, Institut de Chimie, Université Rennes 1, 263 Avenue du Général Leclerc, CS74205/35042 Rennes/France (2 aut.); Groupe Cycle Cellulaire, CNRS UMR 6061 Génétique et Développement, IFR 97 Génomique Fonctionnelle et Santé, Faculté de Médecine, Université Rennes 1, 2 av du Pr Léon Bernard, CS 34317/35043 Rennes/France (3 aut., 4 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Current medicinal chemistry; ISSN 0929-8673; Pays-Bas; Da. 2003; Vol. 10; No. 6; Pp. 479-503; Bibl. 271 ref.</SO>
<LA>Anglais</LA>
<EA>In cells, protein degradation is a key pathway for the destruction of abnormal or damaged proteins as well as for the elimination of proteins whose presence is no longer required. Among the various cell proteases, the proteasome, a multicatalytic macromolecular complex, is specifically required for the degradation of ubiquitinated proteins. In normal cells, the proteasome ensures the elimination of numerous proteins that play critical roles in cell functions throughout the cell cycle. Defects in the activity of this proteolytic machinery can lead to the disorders of cell function that is believed to be the root cause of certain diseases. Indeed, many proteins involved in the control of cell cycle transitions are readily destroyed by the proteasome once their tasks have been accomplished. Moreover, because proteasome inhibitors can provoke cell death, it has been suggested that proteasomes must be continually degrading certain apoptotic factors. For these reasons, proteasome inhibition has become a new and potentially significant strategy for the drug development in cancer treatment. The proteasome possesses three major peptidase activities that can individually be targeted by drugs. Different classes of proteasome inhibitors are reviewed here. In addition, we present new pseudopeptides with the enriched nitrogen backbones bearing a side chain and a modified C-terminal position that inhibit proteasome activity.</EA>
<CC>002B02R01</CC>
<FD>Article synthèse; Recherche développement; Relation structure activité; Inhibiteur enzyme; Multicatalytic endopeptidase complex; Localisation; Intracellulaire; Ubiquitine; Anticancéreux; Maladie dégénérative; Système nerveux central pathologie; Système nerveux pathologie; Encéphale pathologie; Démence Alzheimer; Parkinson maladie; Chorée Huntington; Cachexie; Muscle strié pathologie; Produit synthétique; Pseudopeptide; Peptide cyclique; Composé non peptide; Composé peptidomimétique; Hydrazide organique; Carbazate organique; Aldéhyde</FD>
<FG>Peptidases; Hydrolases; Enzyme</FG>
<ED>Review; Research and development; Structure activity relation; Enzyme inhibitor; Multicatalytic endopeptidase complex; Localization; Intracellular; Ubiquitin; Antineoplastic agent; Degenerative disease; Central nervous system disease; Nervous system diseases; Cerebral disorder; Alzheimer disease; Parkinson disease; Huntington disease; Cachexia; Striated muscle disease; Synthetic product; Pseudopeptide; Cyclic peptides; Non peptide compound; Peptidomimetic compound; Organic hydrazide; Organic carbazate; Aldehyde</ED>
<EG>Peptidases; Hydrolases; Enzyme</EG>
<SD>Artículo síntesis; Investigación desarrollo; Relación estructura actividad; Inhibidor enzima; Multicatalytic endopeptidase complex; Localización; Intracelular; Ubiquitina; Anticanceroso; Enfermedad degenerativa; Sistema nervosio central patología; Sistema nervioso patología; Encéfalo patología; Demencia Alzheimer; Parkinson enfermedad; Corea Huntington; Caquexia; Músculo estriado patología; Producto sintético; Seudopéptido; Péptido cíclico; Compuesto no péptido; Compuesto peptidomimético; Hidrácida orgánica; Carbazato orgánico; Aldehído</SD>
<LO>INIST-22999.354000111020770030</LO>
<ID>03-0297215</ID>
</server>
</inist>
</record>
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