IndraLab

Statements


COPS6 affects COPS5
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COPS6 binds COPS5.
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"Molecular dynamics simulation studies further suggest that heterodimerization of CSN5 with CSN6 facilitates inhibitor binding by stabilizing an open ins-1 loop conformation [ 58 ]."

No evidence text available

No evidence text available

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"CSN5 and CSN6, which have an MPN (Mpr1 and Pad1 N-terminal) domain, form a dimer and are embedded at the core of the helical bundle."

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"The structure reaffirms the conserved activation mechanism of the deneddylation machinery, including conformational clamping of CRL2 by CSN2/CSN4, release of the catalytic CSN5/CSN6 heterodimer, and s[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"The above suggests that the MPN dimer (CSN5CSN6 dimer) could be highly conserved."

No evidence text available

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"Structurally, CSN6 and CSN5 form a heterodimer through MPN domain and the dimer is topologically knotted to engage in Cullin deneddylation xref ."

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"MD simulations studies and binding energy analysis revealed that the selective binding of the inhibitors can be only explained by the consideration of larger heterodimeric complexes of Rpn11 (Rpn8-Rpn11) and CSN5 (CSN5-CSN6)."

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"In the crystal structure of CSN5-CSN6 heterodimer, initial Ins-1 loop (98–109) conformation blocks the distal ubiquitin binding site which we also observed in cryo-EM structure of Rpn11."
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"CSN5 alone is inactive due to an auto-inhibited conformation of its catalytic domain, and the association of CSN5 with the CSN6 MPN (Mpr1/Pad1 N-terminal) domain activates its isopeptidase activity xref ."

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"The association of CSN5 and CSN6 MPN (for Mpr1/Pad1 N-terminal) domains activates its isopeptidase activity."

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"Here we report that CSN6 N-terminal domain containing its MPN domain can form a stable heterodimer with CSN5 catalytic domain in vitro ."
CSN3 binds COPS5 and COPS6. 3 / 3
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"Our data also demonstrate that CSNAP binds to CSN3, CSN5 and CSN6, possibly linking the MPN and PCI substructures."

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"We show that CSNAP binds CSN3, CSN5 and CSN6 and its incorporation into the CSN complex is mediated through the C-terminal region involving conserved aromatic residues."

sparser
"CSNAP interacts with CSN3, CSN5, and CSN6."
COPS6 binds COPS5 and MPN domain. 2 / 2
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"Structurally, CSN6 and CSN5 form a heterodimer through MPN domain, and the dimer is topologically knotted to engage in Cullin deneddylation."

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"Structurally, CSN6 and CSN5 form a heterodimer through MPN domain and the dimer is topologically knotted to engage in Cullin deneddylation 55."
COPS6 binds COPS5 and CRL. 1 / 1
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sparser
"Conformational changes of CSN2, CSN4 and CSN7 provide an induced fit mechanism that propagates the binding of neddylated CRL to the CSN5CSN6 dimer and activates CSN5 [ xref ]."
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"We previously reported that Drosophila Trc8 genetically and physically interacts with Csn5 and Csn6, but not Rpn8 or Rpn11 ( xref )."
Rpn11 binds RPN8, COPS6, and COPS5. 1 / 1
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"Considering the Rpn8-Rpn11 and CSN5-CSN6 heterodimers, we found that residues in the distal ubiquitin site are responsible for selectivity and must be taken into consideration for the design of selective inhibitors of CSN5 and Rpn11 in future studies."
COPS5 binds COPS6 and MPN domains. 1 / 1
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"Having shown that the N-terminal MPN domains of CSN5 and CSN6 heterodimerize, we went on to evaluate the effect of CSN6 DeltaC on CSN5 DeltaC 's affinity for Nedd8 and its isopeptidase activity on substrates ranging from protein to a physiological complex."
COPS6 binds COPS5 and CSN5i-3. 1 / 1
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sparser
"Binding of capzimin and CSN5i-3 to monomeric CSN5 and CSN5-CSN6 heterodimer."
COPS6 binds COPS5 and CUL1. 1 / 1
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"We found that both CSN6 and CSN5 associated with Cullin-1 and that CSN6 and CSN5 competed with each other for Cullin-1 binding in a dose-dependent manner ( xref )."
COPS6 activates COPS5.
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COPS6 activates COPS5. 2 / 3
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"Previous study has shown that over-expression of CSN6 increases its competition with CSN5 in terms of cullin binding, and thereby inhibits accessibility of cullin to CSN5 for deneddylation, which stab[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"To gain additional insights into the molecular mechanism of CSN5 activation by CSN6, the crystal structure of the MPN − core fragment was determined by molecular replacement at 1.76 Å resolution, using the human Rpn8 ΔC orthologue as the search model (PDB code 2O95; xref )."
COPS6 inhibits COPS5.
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COPS6 inhibits COPS5. 2 / 2
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"Previous study has shown that over-expression of CSN6 increases its competition with CSN5 in terms of cullin binding, and thereby inhibits accessibility of cullin to CSN5 for deneddylation, which stab[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Notably, the MPN domain of CSN6 inhibited the association of CSN5 with Cullin-1, while the C-terminal domain had less impact (XREF_FIG)."
COPS2 affects COPS3, COPS4, COPS5, COPS6, COPS7A, COPS8, and GPS1
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"Inferred from SIGNOR complex SIGNOR-C489"

No evidence text available

No evidence text available
MPN domain affects COPS6
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COPS6 binds COPS5 and MPN domain. 2 / 2
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"Structurally, CSN6 and CSN5 form a heterodimer through MPN domain, and the dimer is topologically knotted to engage in Cullin deneddylation."

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"Structurally, CSN6 and CSN5 form a heterodimer through MPN domain and the dimer is topologically knotted to engage in Cullin deneddylation 55."
Rpn11 affects RPN8
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Rpn11 binds RPN8, COPS6, and COPS5. 1 / 1
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"Considering the Rpn8-Rpn11 and CSN5-CSN6 heterodimers, we found that residues in the distal ubiquitin site are responsible for selectivity and must be taken into consideration for the design of selective inhibitors of CSN5 and Rpn11 in future studies."
RNF139 affects COPS6
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sparser
"We previously reported that Drosophila Trc8 genetically and physically interacts with Csn5 and Csn6, but not Rpn8 or Rpn11 ( xref )."
MPN domains affects COPS6
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COPS5 binds COPS6 and MPN domains. 1 / 1
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"Having shown that the N-terminal MPN domains of CSN5 and CSN6 heterodimerize, we went on to evaluate the effect of CSN6 DeltaC on CSN5 DeltaC 's affinity for Nedd8 and its isopeptidase activity on substrates ranging from protein to a physiological complex."
CUL1 affects COPS6
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COPS6 binds COPS5 and CUL1. 1 / 1
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"We found that both CSN6 and CSN5 associated with Cullin-1 and that CSN6 and CSN5 competed with each other for Cullin-1 binding in a dose-dependent manner ( xref )."
CSN5i-3 affects COPS6
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COPS6 binds COPS5 and CSN5i-3. 1 / 1
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"Binding of capzimin and CSN5i-3 to monomeric CSN5 and CSN5-CSN6 heterodimer."
CRL affects COPS6
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COPS6 binds COPS5 and CRL. 1 / 1
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"Conformational changes of CSN2, CSN4 and CSN7 provide an induced fit mechanism that propagates the binding of neddylated CRL to the CSN5CSN6 dimer and activates CSN5 [ xref ]."
COPS6 affects rpn11
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Rpn11 binds RPN8, COPS6, and COPS5. 1 / 1
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sparser
"Considering the Rpn8-Rpn11 and CSN5-CSN6 heterodimers, we found that residues in the distal ubiquitin site are responsible for selectivity and must be taken into consideration for the design of selective inhibitors of CSN5 and Rpn11 in future studies."
COPS6 affects RNF139
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sparser
"We previously reported that Drosophila Trc8 genetically and physically interacts with Csn5 and Csn6, but not Rpn8 or Rpn11 ( xref )."
COPS6 affects MPN domains
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COPS5 binds COPS6 and MPN domains. 1 / 1
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"Having shown that the N-terminal MPN domains of CSN5 and CSN6 heterodimerize, we went on to evaluate the effect of CSN6 DeltaC on CSN5 DeltaC 's affinity for Nedd8 and its isopeptidase activity on substrates ranging from protein to a physiological complex."
COPS6 affects CUL1
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COPS6 binds COPS5 and CUL1. 1 / 1
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sparser
"We found that both CSN6 and CSN5 associated with Cullin-1 and that CSN6 and CSN5 competed with each other for Cullin-1 binding in a dose-dependent manner ( xref )."
COPS6 affects CSN5i-3
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COPS6 binds COPS5 and CSN5i-3. 1 / 1
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"Binding of capzimin and CSN5i-3 to monomeric CSN5 and CSN5-CSN6 heterodimer."
COPS6 affects CRL
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COPS6 binds COPS5 and CRL. 1 / 1
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"Conformational changes of CSN2, CSN4 and CSN7 provide an induced fit mechanism that propagates the binding of neddylated CRL to the CSN5CSN6 dimer and activates CSN5 [ xref ]."
COPS5 affects rpn11
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Rpn11 binds RPN8, COPS6, and COPS5. 1 / 1
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sparser
"Considering the Rpn8-Rpn11 and CSN5-CSN6 heterodimers, we found that residues in the distal ubiquitin site are responsible for selectivity and must be taken into consideration for the design of selective inhibitors of CSN5 and Rpn11 in future studies."
COPS5 affects RNF139
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sparser
"We previously reported that Drosophila Trc8 genetically and physically interacts with Csn5 and Csn6, but not Rpn8 or Rpn11 ( xref )."
COPS5 affects MPN domains
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COPS5 binds COPS6 and MPN domains. 1 / 1
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"Having shown that the N-terminal MPN domains of CSN5 and CSN6 heterodimerize, we went on to evaluate the effect of CSN6 DeltaC on CSN5 DeltaC 's affinity for Nedd8 and its isopeptidase activity on substrates ranging from protein to a physiological complex."
COPS5 affects CUL1
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COPS6 binds COPS5 and CUL1. 1 / 1
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sparser
"We found that both CSN6 and CSN5 associated with Cullin-1 and that CSN6 and CSN5 competed with each other for Cullin-1 binding in a dose-dependent manner ( xref )."
COPS5 affects CSN5i-3
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COPS6 binds COPS5 and CSN5i-3. 1 / 1
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sparser
"Binding of capzimin and CSN5i-3 to monomeric CSN5 and CSN5-CSN6 heterodimer."
COPS5 affects CRL
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COPS6 binds COPS5 and CRL. 1 / 1
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sparser
"Conformational changes of CSN2, CSN4 and CSN7 provide an induced fit mechanism that propagates the binding of neddylated CRL to the CSN5CSN6 dimer and activates CSN5 [ xref ]."
COPS5 affects COPS6, RPN8, and rpn11
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Rpn11 binds RPN8, COPS6, and COPS5. 1 / 1
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sparser
"Considering the Rpn8-Rpn11 and CSN5-CSN6 heterodimers, we found that residues in the distal ubiquitin site are responsible for selectivity and must be taken into consideration for the design of selective inhibitors of CSN5 and Rpn11 in future studies."
COPS5 affects COPS6, and RNF139
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sparser
"We previously reported that Drosophila Trc8 genetically and physically interacts with Csn5 and Csn6, but not Rpn8 or Rpn11 ( xref )."
COPS5 affects COPS6, and MPN domains
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COPS5 binds COPS6 and MPN domains. 1 / 1
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"Having shown that the N-terminal MPN domains of CSN5 and CSN6 heterodimerize, we went on to evaluate the effect of CSN6 DeltaC on CSN5 DeltaC 's affinity for Nedd8 and its isopeptidase activity on substrates ranging from protein to a physiological complex."
COPS5 affects COPS6, and CUL1
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COPS6 binds COPS5 and CUL1. 1 / 1
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sparser
"We found that both CSN6 and CSN5 associated with Cullin-1 and that CSN6 and CSN5 competed with each other for Cullin-1 binding in a dose-dependent manner ( xref )."
COPS5 affects COPS6, and CSN5i-3
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COPS6 binds COPS5 and CSN5i-3. 1 / 1
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sparser
"Binding of capzimin and CSN5i-3 to monomeric CSN5 and CSN5-CSN6 heterodimer."
COPS5 affects COPS6, and CRL
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COPS6 binds COPS5 and CRL. 1 / 1
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sparser
"Conformational changes of CSN2, CSN4 and CSN7 provide an induced fit mechanism that propagates the binding of neddylated CRL to the CSN5CSN6 dimer and activates CSN5 [ xref ]."
COPS2 affects COPS3, COPS4, COPS5, COPS6, COPS7B, COPS8, and GPS1
1 |

"Inferred from SIGNOR complex SIGNOR-C487"
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No evidence text available
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No evidence text available

No evidence text available

No evidence text available