ParkinsonFranceV1, PascalFrancis, Curation, bibRecord, 000489

Proteasome inhibitors as therapeutic agents: Current and future strategies

Identifieur interne : 000489 ( PascalFrancis/Curation ); précédent : 000488; suivant : 000490

Proteasome inhibitors as therapeutic agents: Current and future strategies

Auteurs : J. G. Delcros [France] ; M. Baudy Floc'H [France] ; C. Prigent [France] ; Y. Arlot-Bonnemains [France]

Source :

Current medicinal chemistry [ 0929-8673 ] ; 2003.

RBID : Pascal:03-0297215

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.

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C01	`01`		`ENG`	@0 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.
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C03	`20`	`X`	`FRE`	`@0 Pseudopeptide @5 25`
C03	`20`	`X`	`ENG`	`@0 Pseudopeptide @5 25`
C03	`20`	`X`	`SPA`	`@0 Seudopéptido @5 25`
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Pascal:03-0297215

Le document en format XML

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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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<sZ>4 aut.</sZ>
</fA14>
<fA20><s1>479-503</s1>
</fA20>
<fA21><s1>2003</s1>
</fA21>
<fA23 i1="01"><s0>ENG</s0>
</fA23>
<fA43 i1="01"><s1>INIST</s1>
<s2>22999</s2>
<s5>354000111020770030</s5>
</fA43>
<fA44><s0>0000</s0>
<s1>© 2003 INIST-CNRS. All rights reserved.</s1>
</fA44>
<fA45><s0>271 ref.</s0>
</fA45>
<fA47 i1="01" i2="1"><s0>03-0297215</s0>
</fA47>
<fA60><s1>P</s1>
</fA60>
<fA61><s0>A</s0>
</fA61>
<fA64 i1="01" i2="1"><s0>Current medicinal chemistry</s0>
</fA64>
<fA66 i1="01"><s0>NLD</s0>
</fA66>
<fC01 i1="01" l="ENG"><s0>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.</s0>
</fC01>
<fC02 i1="01" i2="X"><s0>002B02R01</s0>
</fC02>
<fC03 i1="01" i2="X" l="FRE"><s0>Article synthèse</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="ENG"><s0>Review</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="SPA"><s0>Artículo síntesis</s0>
<s5>01</s5>
</fC03>
<fC03 i1="02" i2="X" l="FRE"><s0>Recherche développement</s0>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="ENG"><s0>Research and development</s0>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="SPA"><s0>Investigación desarrollo</s0>
<s5>02</s5>
</fC03>
<fC03 i1="03" i2="X" l="FRE"><s0>Relation structure activité</s0>
<s5>03</s5>
</fC03>
<fC03 i1="03" i2="X" l="ENG"><s0>Structure activity relation</s0>
<s5>03</s5>
</fC03>
<fC03 i1="03" i2="X" l="SPA"><s0>Relación estructura actividad</s0>
<s5>03</s5>
</fC03>
<fC03 i1="04" i2="X" l="FRE"><s0>Inhibiteur enzyme</s0>
<s5>04</s5>
</fC03>
<fC03 i1="04" i2="X" l="ENG"><s0>Enzyme inhibitor</s0>
<s5>04</s5>
</fC03>
<fC03 i1="04" i2="X" l="SPA"><s0>Inhibidor enzima</s0>
<s5>04</s5>
</fC03>
<fC03 i1="05" i2="X" l="FRE"><s0>Multicatalytic endopeptidase complex</s0>
<s2>FE</s2>
<s5>05</s5>
</fC03>
<fC03 i1="05" i2="X" l="ENG"><s0>Multicatalytic endopeptidase complex</s0>
<s2>FE</s2>
<s5>05</s5>
</fC03>
<fC03 i1="05" i2="X" l="SPA"><s0>Multicatalytic endopeptidase complex</s0>
<s2>FE</s2>
<s5>05</s5>
</fC03>
<fC03 i1="06" i2="X" l="FRE"><s0>Localisation</s0>
<s5>06</s5>
</fC03>
<fC03 i1="06" i2="X" l="ENG"><s0>Localization</s0>
<s5>06</s5>
</fC03>
<fC03 i1="06" i2="X" l="SPA"><s0>Localización</s0>
<s5>06</s5>
</fC03>
<fC03 i1="07" i2="X" l="FRE"><s0>Intracellulaire</s0>
<s5>07</s5>
</fC03>
<fC03 i1="07" i2="X" l="ENG"><s0>Intracellular</s0>
<s5>07</s5>
</fC03>
<fC03 i1="07" i2="X" l="SPA"><s0>Intracelular</s0>
<s5>07</s5>
</fC03>
<fC03 i1="08" i2="X" l="FRE"><s0>Ubiquitine</s0>
<s5>09</s5>
</fC03>
<fC03 i1="08" i2="X" l="ENG"><s0>Ubiquitin</s0>
<s5>09</s5>
</fC03>
<fC03 i1="08" i2="X" l="SPA"><s0>Ubiquitina</s0>
<s5>09</s5>
</fC03>
<fC03 i1="09" i2="X" l="FRE"><s0>Anticancéreux</s0>
<s5>11</s5>
</fC03>
<fC03 i1="09" i2="X" l="ENG"><s0>Antineoplastic agent</s0>
<s5>11</s5>
</fC03>
<fC03 i1="09" i2="X" l="SPA"><s0>Anticanceroso</s0>
<s5>11</s5>
</fC03>
<fC03 i1="10" i2="X" l="FRE"><s0>Maladie dégénérative</s0>
<s5>13</s5>
</fC03>
<fC03 i1="10" i2="X" l="ENG"><s0>Degenerative disease</s0>
<s5>13</s5>
</fC03>
<fC03 i1="10" i2="X" l="SPA"><s0>Enfermedad degenerativa</s0>
<s5>13</s5>
</fC03>
<fC03 i1="11" i2="X" l="FRE"><s0>Système nerveux central pathologie</s0>
<s5>14</s5>
</fC03>
<fC03 i1="11" i2="X" l="ENG"><s0>Central nervous system disease</s0>
<s5>14</s5>
</fC03>
<fC03 i1="11" i2="X" l="SPA"><s0>Sistema nervosio central patología</s0>
<s5>14</s5>
</fC03>
<fC03 i1="12" i2="X" l="FRE"><s0>Système nerveux pathologie</s0>
<s5>15</s5>
</fC03>
<fC03 i1="12" i2="X" l="ENG"><s0>Nervous system diseases</s0>
<s5>15</s5>
</fC03>
<fC03 i1="12" i2="X" l="SPA"><s0>Sistema nervioso patología</s0>
<s5>15</s5>
</fC03>
<fC03 i1="13" i2="X" l="FRE"><s0>Encéphale pathologie</s0>
<s5>16</s5>
</fC03>
<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>
</inist>
</record>

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	La maladie de Parkinson en France (serveur d'exploration)
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La maladie de Parkinson en France (serveur d'exploration)

Proteasome inhibitors as therapeutic agents: Current and future strategies

Proteasome inhibitors as therapeutic agents: Current and future strategies

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