nu Search Results


athymic nude rats  (Inotiv)
96
Inotiv athymic nude rats
Athymic Nude Rats, supplied by Inotiv, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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atpγs  (Jena Bioscience)
94
Jena Bioscience atpγs
a, Domain structure of p97, highlighting the D395G mutation located in the D1 domain. b, Schematic representation of preparation of ubiquitinated Ub₄-mEOS3.2 for the p97 substrate unfolding assay (top). Green Ub₄-mEOS3.2 was polyubiquitinated using E1, E2-25K, and ubiquitin, and subsequently photoconverted to its red form under UV illumination, as previously described . <t>The</t> <t>purified</t> substrate was then used in unfolding assays in the presence of the Ufd1-Npl4 complex. Compared with p97 WT (grey), p97 D395G (blue) exhibits reduced substrate unfolding activity (bottom). All measurements were performed with at least three technical replicates. c, NMR characterization of p97 D395G using the ND1L construct, comprising the NTD, D1 domain and linker. Key probes for NTD conformation and bound nucleotide are indicated in the schematic above. <t>ATPγS</t> induces an NTD ‘up’ conformation, similar to p97 WT . In the presence of ADP and the ATP reg , predominantly ‘down’ with a minor ‘up’ conformation is observed, in contrast to p97 WT . For comparison, spectra of the prototypical MSP-1-associated mutant p97 R95G in presence of ADP are shown, which display signals at an averaged position between NTD ‘up’ and ‘down’ conformation, indicating fast conformational exchange on the NMR time scale. This establishes that p97 D395G displays distinct molecular defects from MSP-1-type mutants. d, Cryo-EM reconstructions of p97 D395G under different conditions (ATPγS, ATP reg , and ADP). The N-terminal domain (NTD) is colored grey, and the D1 and D2 ATPase domains are shown in blue. Schematic representations on the left indicate the corresponding nucleotide-bound states. e, Backbone RMSD of a p97 D395G protomer relative to p97 WT in different nucleotide states, calculated without the NTD. p97 D395G structures in ATPγS (PDB: 28VN), ADP (PDB: 28VL), and ADP.P i (PDB: 28XW) states were aligned using the main chain atoms of the D1 and D2 domains to the published p97 WT models in the ATPγS (PDB: 5FTN), ADP (PDB: 5FTK), and ADP.P i (PDB: 8OOI) states, respectively. The inset shows a magnified view of the α 5 helix in the D2 domain of p97 D395G in ADP.P i state.
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dna pk  (Tocris)
91
Tocris dna pk
a, Domain structure of p97, highlighting the D395G mutation located in the D1 domain. b, Schematic representation of preparation of ubiquitinated Ub₄-mEOS3.2 for the p97 substrate unfolding assay (top). Green Ub₄-mEOS3.2 was polyubiquitinated using E1, E2-25K, and ubiquitin, and subsequently photoconverted to its red form under UV illumination, as previously described . <t>The</t> <t>purified</t> substrate was then used in unfolding assays in the presence of the Ufd1-Npl4 complex. Compared with p97 WT (grey), p97 D395G (blue) exhibits reduced substrate unfolding activity (bottom). All measurements were performed with at least three technical replicates. c, NMR characterization of p97 D395G using the ND1L construct, comprising the NTD, D1 domain and linker. Key probes for NTD conformation and bound nucleotide are indicated in the schematic above. <t>ATPγS</t> induces an NTD ‘up’ conformation, similar to p97 WT . In the presence of ADP and the ATP reg , predominantly ‘down’ with a minor ‘up’ conformation is observed, in contrast to p97 WT . For comparison, spectra of the prototypical MSP-1-associated mutant p97 R95G in presence of ADP are shown, which display signals at an averaged position between NTD ‘up’ and ‘down’ conformation, indicating fast conformational exchange on the NMR time scale. This establishes that p97 D395G displays distinct molecular defects from MSP-1-type mutants. d, Cryo-EM reconstructions of p97 D395G under different conditions (ATPγS, ATP reg , and ADP). The N-terminal domain (NTD) is colored grey, and the D1 and D2 ATPase domains are shown in blue. Schematic representations on the left indicate the corresponding nucleotide-bound states. e, Backbone RMSD of a p97 D395G protomer relative to p97 WT in different nucleotide states, calculated without the NTD. p97 D395G structures in ATPγS (PDB: 28VN), ADP (PDB: 28VL), and ADP.P i (PDB: 28XW) states were aligned using the main chain atoms of the D1 and D2 domains to the published p97 WT models in the ATPγS (PDB: 5FTN), ADP (PDB: 5FTK), and ADP.P i (PDB: 8OOI) states, respectively. The inset shows a magnified view of the α 5 helix in the D2 domain of p97 D395G in ADP.P i state.
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dna pkcs inhibitors  (Tocris)
95
Tocris dna pkcs inhibitors
a, Domain structure of p97, highlighting the D395G mutation located in the D1 domain. b, Schematic representation of preparation of ubiquitinated Ub₄-mEOS3.2 for the p97 substrate unfolding assay (top). Green Ub₄-mEOS3.2 was polyubiquitinated using E1, E2-25K, and ubiquitin, and subsequently photoconverted to its red form under UV illumination, as previously described . <t>The</t> <t>purified</t> substrate was then used in unfolding assays in the presence of the Ufd1-Npl4 complex. Compared with p97 WT (grey), p97 D395G (blue) exhibits reduced substrate unfolding activity (bottom). All measurements were performed with at least three technical replicates. c, NMR characterization of p97 D395G using the ND1L construct, comprising the NTD, D1 domain and linker. Key probes for NTD conformation and bound nucleotide are indicated in the schematic above. <t>ATPγS</t> induces an NTD ‘up’ conformation, similar to p97 WT . In the presence of ADP and the ATP reg , predominantly ‘down’ with a minor ‘up’ conformation is observed, in contrast to p97 WT . For comparison, spectra of the prototypical MSP-1-associated mutant p97 R95G in presence of ADP are shown, which display signals at an averaged position between NTD ‘up’ and ‘down’ conformation, indicating fast conformational exchange on the NMR time scale. This establishes that p97 D395G displays distinct molecular defects from MSP-1-type mutants. d, Cryo-EM reconstructions of p97 D395G under different conditions (ATPγS, ATP reg , and ADP). The N-terminal domain (NTD) is colored grey, and the D1 and D2 ATPase domains are shown in blue. Schematic representations on the left indicate the corresponding nucleotide-bound states. e, Backbone RMSD of a p97 D395G protomer relative to p97 WT in different nucleotide states, calculated without the NTD. p97 D395G structures in ATPγS (PDB: 28VN), ADP (PDB: 28VL), and ADP.P i (PDB: 28XW) states were aligned using the main chain atoms of the D1 and D2 domains to the published p97 WT models in the ATPγS (PDB: 5FTN), ADP (PDB: 5FTK), and ADP.P i (PDB: 8OOI) states, respectively. The inset shows a magnified view of the α 5 helix in the D2 domain of p97 D395G in ADP.P i state.
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nu9056  (Tocris)
93
Tocris nu9056
a, Domain structure of p97, highlighting the D395G mutation located in the D1 domain. b, Schematic representation of preparation of ubiquitinated Ub₄-mEOS3.2 for the p97 substrate unfolding assay (top). Green Ub₄-mEOS3.2 was polyubiquitinated using E1, E2-25K, and ubiquitin, and subsequently photoconverted to its red form under UV illumination, as previously described . <t>The</t> <t>purified</t> substrate was then used in unfolding assays in the presence of the Ufd1-Npl4 complex. Compared with p97 WT (grey), p97 D395G (blue) exhibits reduced substrate unfolding activity (bottom). All measurements were performed with at least three technical replicates. c, NMR characterization of p97 D395G using the ND1L construct, comprising the NTD, D1 domain and linker. Key probes for NTD conformation and bound nucleotide are indicated in the schematic above. <t>ATPγS</t> induces an NTD ‘up’ conformation, similar to p97 WT . In the presence of ADP and the ATP reg , predominantly ‘down’ with a minor ‘up’ conformation is observed, in contrast to p97 WT . For comparison, spectra of the prototypical MSP-1-associated mutant p97 R95G in presence of ADP are shown, which display signals at an averaged position between NTD ‘up’ and ‘down’ conformation, indicating fast conformational exchange on the NMR time scale. This establishes that p97 D395G displays distinct molecular defects from MSP-1-type mutants. d, Cryo-EM reconstructions of p97 D395G under different conditions (ATPγS, ATP reg , and ADP). The N-terminal domain (NTD) is colored grey, and the D1 and D2 ATPase domains are shown in blue. Schematic representations on the left indicate the corresponding nucleotide-bound states. e, Backbone RMSD of a p97 D395G protomer relative to p97 WT in different nucleotide states, calculated without the NTD. p97 D395G structures in ATPγS (PDB: 28VN), ADP (PDB: 28VL), and ADP.P i (PDB: 28XW) states were aligned using the main chain atoms of the D1 and D2 domains to the published p97 WT models in the ATPγS (PDB: 5FTN), ADP (PDB: 5FTK), and ADP.P i (PDB: 8OOI) states, respectively. The inset shows a magnified view of the α 5 helix in the D2 domain of p97 D395G in ADP.P i state.
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nu 7441  (Tocris)
95
Tocris nu 7441
a, Domain structure of p97, highlighting the D395G mutation located in the D1 domain. b, Schematic representation of preparation of ubiquitinated Ub₄-mEOS3.2 for the p97 substrate unfolding assay (top). Green Ub₄-mEOS3.2 was polyubiquitinated using E1, E2-25K, and ubiquitin, and subsequently photoconverted to its red form under UV illumination, as previously described . <t>The</t> <t>purified</t> substrate was then used in unfolding assays in the presence of the Ufd1-Npl4 complex. Compared with p97 WT (grey), p97 D395G (blue) exhibits reduced substrate unfolding activity (bottom). All measurements were performed with at least three technical replicates. c, NMR characterization of p97 D395G using the ND1L construct, comprising the NTD, D1 domain and linker. Key probes for NTD conformation and bound nucleotide are indicated in the schematic above. <t>ATPγS</t> induces an NTD ‘up’ conformation, similar to p97 WT . In the presence of ADP and the ATP reg , predominantly ‘down’ with a minor ‘up’ conformation is observed, in contrast to p97 WT . For comparison, spectra of the prototypical MSP-1-associated mutant p97 R95G in presence of ADP are shown, which display signals at an averaged position between NTD ‘up’ and ‘down’ conformation, indicating fast conformational exchange on the NMR time scale. This establishes that p97 D395G displays distinct molecular defects from MSP-1-type mutants. d, Cryo-EM reconstructions of p97 D395G under different conditions (ATPγS, ATP reg , and ADP). The N-terminal domain (NTD) is colored grey, and the D1 and D2 ATPase domains are shown in blue. Schematic representations on the left indicate the corresponding nucleotide-bound states. e, Backbone RMSD of a p97 D395G protomer relative to p97 WT in different nucleotide states, calculated without the NTD. p97 D395G structures in ATPγS (PDB: 28VN), ADP (PDB: 28VL), and ADP.P i (PDB: 28XW) states were aligned using the main chain atoms of the D1 and D2 domains to the published p97 WT models in the ATPγS (PDB: 5FTN), ADP (PDB: 5FTK), and ADP.P i (PDB: 8OOI) states, respectively. The inset shows a magnified view of the α 5 helix in the D2 domain of p97 D395G in ADP.P i state.
Nu 7441, supplied by Tocris, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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biotin 16 dctp  (Jena Bioscience)
94
Jena Bioscience biotin 16 dctp
a, Domain structure of p97, highlighting the D395G mutation located in the D1 domain. b, Schematic representation of preparation of ubiquitinated Ub₄-mEOS3.2 for the p97 substrate unfolding assay (top). Green Ub₄-mEOS3.2 was polyubiquitinated using E1, E2-25K, and ubiquitin, and subsequently photoconverted to its red form under UV illumination, as previously described . <t>The</t> <t>purified</t> substrate was then used in unfolding assays in the presence of the Ufd1-Npl4 complex. Compared with p97 WT (grey), p97 D395G (blue) exhibits reduced substrate unfolding activity (bottom). All measurements were performed with at least three technical replicates. c, NMR characterization of p97 D395G using the ND1L construct, comprising the NTD, D1 domain and linker. Key probes for NTD conformation and bound nucleotide are indicated in the schematic above. <t>ATPγS</t> induces an NTD ‘up’ conformation, similar to p97 WT . In the presence of ADP and the ATP reg , predominantly ‘down’ with a minor ‘up’ conformation is observed, in contrast to p97 WT . For comparison, spectra of the prototypical MSP-1-associated mutant p97 R95G in presence of ADP are shown, which display signals at an averaged position between NTD ‘up’ and ‘down’ conformation, indicating fast conformational exchange on the NMR time scale. This establishes that p97 D395G displays distinct molecular defects from MSP-1-type mutants. d, Cryo-EM reconstructions of p97 D395G under different conditions (ATPγS, ATP reg , and ADP). The N-terminal domain (NTD) is colored grey, and the D1 and D2 ATPase domains are shown in blue. Schematic representations on the left indicate the corresponding nucleotide-bound states. e, Backbone RMSD of a p97 D395G protomer relative to p97 WT in different nucleotide states, calculated without the NTD. p97 D395G structures in ATPγS (PDB: 28VN), ADP (PDB: 28VL), and ADP.P i (PDB: 28XW) states were aligned using the main chain atoms of the D1 and D2 domains to the published p97 WT models in the ATPγS (PDB: 5FTN), ADP (PDB: 5FTK), and ADP.P i (PDB: 8OOI) states, respectively. The inset shows a magnified view of the α 5 helix in the D2 domain of p97 D395G in ADP.P i state.
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nu 1610 cy5  (Jena Bioscience)
94
Jena Bioscience nu 1610 cy5
a, Domain structure of p97, highlighting the D395G mutation located in the D1 domain. b, Schematic representation of preparation of ubiquitinated Ub₄-mEOS3.2 for the p97 substrate unfolding assay (top). Green Ub₄-mEOS3.2 was polyubiquitinated using E1, E2-25K, and ubiquitin, and subsequently photoconverted to its red form under UV illumination, as previously described . <t>The</t> <t>purified</t> substrate was then used in unfolding assays in the presence of the Ufd1-Npl4 complex. Compared with p97 WT (grey), p97 D395G (blue) exhibits reduced substrate unfolding activity (bottom). All measurements were performed with at least three technical replicates. c, NMR characterization of p97 D395G using the ND1L construct, comprising the NTD, D1 domain and linker. Key probes for NTD conformation and bound nucleotide are indicated in the schematic above. <t>ATPγS</t> induces an NTD ‘up’ conformation, similar to p97 WT . In the presence of ADP and the ATP reg , predominantly ‘down’ with a minor ‘up’ conformation is observed, in contrast to p97 WT . For comparison, spectra of the prototypical MSP-1-associated mutant p97 R95G in presence of ADP are shown, which display signals at an averaged position between NTD ‘up’ and ‘down’ conformation, indicating fast conformational exchange on the NMR time scale. This establishes that p97 D395G displays distinct molecular defects from MSP-1-type mutants. d, Cryo-EM reconstructions of p97 D395G under different conditions (ATPγS, ATP reg , and ADP). The N-terminal domain (NTD) is colored grey, and the D1 and D2 ATPase domains are shown in blue. Schematic representations on the left indicate the corresponding nucleotide-bound states. e, Backbone RMSD of a p97 D395G protomer relative to p97 WT in different nucleotide states, calculated without the NTD. p97 D395G structures in ATPγS (PDB: 28VN), ADP (PDB: 28VL), and ADP.P i (PDB: 28XW) states were aligned using the main chain atoms of the D1 and D2 domains to the published p97 WT models in the ATPγS (PDB: 5FTN), ADP (PDB: 5FTK), and ADP.P i (PDB: 8OOI) states, respectively. The inset shows a magnified view of the α 5 helix in the D2 domain of p97 D395G in ADP.P i state.
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biological safety cabinet  (NuAire)
94
NuAire biological safety cabinet
a, Domain structure of p97, highlighting the D395G mutation located in the D1 domain. b, Schematic representation of preparation of ubiquitinated Ub₄-mEOS3.2 for the p97 substrate unfolding assay (top). Green Ub₄-mEOS3.2 was polyubiquitinated using E1, E2-25K, and ubiquitin, and subsequently photoconverted to its red form under UV illumination, as previously described . <t>The</t> <t>purified</t> substrate was then used in unfolding assays in the presence of the Ufd1-Npl4 complex. Compared with p97 WT (grey), p97 D395G (blue) exhibits reduced substrate unfolding activity (bottom). All measurements were performed with at least three technical replicates. c, NMR characterization of p97 D395G using the ND1L construct, comprising the NTD, D1 domain and linker. Key probes for NTD conformation and bound nucleotide are indicated in the schematic above. <t>ATPγS</t> induces an NTD ‘up’ conformation, similar to p97 WT . In the presence of ADP and the ATP reg , predominantly ‘down’ with a minor ‘up’ conformation is observed, in contrast to p97 WT . For comparison, spectra of the prototypical MSP-1-associated mutant p97 R95G in presence of ADP are shown, which display signals at an averaged position between NTD ‘up’ and ‘down’ conformation, indicating fast conformational exchange on the NMR time scale. This establishes that p97 D395G displays distinct molecular defects from MSP-1-type mutants. d, Cryo-EM reconstructions of p97 D395G under different conditions (ATPγS, ATP reg , and ADP). The N-terminal domain (NTD) is colored grey, and the D1 and D2 ATPase domains are shown in blue. Schematic representations on the left indicate the corresponding nucleotide-bound states. e, Backbone RMSD of a p97 D395G protomer relative to p97 WT in different nucleotide states, calculated without the NTD. p97 D395G structures in ATPγS (PDB: 28VN), ADP (PDB: 28VL), and ADP.P i (PDB: 28XW) states were aligned using the main chain atoms of the D1 and D2 domains to the published p97 WT models in the ATPγS (PDB: 5FTN), ADP (PDB: 5FTK), and ADP.P i (PDB: 8OOI) states, respectively. The inset shows a magnified view of the α 5 helix in the D2 domain of p97 D395G in ADP.P i state.
Biological Safety Cabinet, supplied by NuAire, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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dtg digoxigenin 11 utp  (Jena Bioscience)
92
Jena Bioscience dtg digoxigenin 11 utp
a, Domain structure of p97, highlighting the D395G mutation located in the D1 domain. b, Schematic representation of preparation of ubiquitinated Ub₄-mEOS3.2 for the p97 substrate unfolding assay (top). Green Ub₄-mEOS3.2 was polyubiquitinated using E1, E2-25K, and ubiquitin, and subsequently photoconverted to its red form under UV illumination, as previously described . <t>The</t> <t>purified</t> substrate was then used in unfolding assays in the presence of the Ufd1-Npl4 complex. Compared with p97 WT (grey), p97 D395G (blue) exhibits reduced substrate unfolding activity (bottom). All measurements were performed with at least three technical replicates. c, NMR characterization of p97 D395G using the ND1L construct, comprising the NTD, D1 domain and linker. Key probes for NTD conformation and bound nucleotide are indicated in the schematic above. <t>ATPγS</t> induces an NTD ‘up’ conformation, similar to p97 WT . In the presence of ADP and the ATP reg , predominantly ‘down’ with a minor ‘up’ conformation is observed, in contrast to p97 WT . For comparison, spectra of the prototypical MSP-1-associated mutant p97 R95G in presence of ADP are shown, which display signals at an averaged position between NTD ‘up’ and ‘down’ conformation, indicating fast conformational exchange on the NMR time scale. This establishes that p97 D395G displays distinct molecular defects from MSP-1-type mutants. d, Cryo-EM reconstructions of p97 D395G under different conditions (ATPγS, ATP reg , and ADP). The N-terminal domain (NTD) is colored grey, and the D1 and D2 ATPase domains are shown in blue. Schematic representations on the left indicate the corresponding nucleotide-bound states. e, Backbone RMSD of a p97 D395G protomer relative to p97 WT in different nucleotide states, calculated without the NTD. p97 D395G structures in ATPγS (PDB: 28VN), ADP (PDB: 28VL), and ADP.P i (PDB: 28XW) states were aligned using the main chain atoms of the D1 and D2 domains to the published p97 WT models in the ATPγS (PDB: 5FTN), ADP (PDB: 5FTK), and ADP.P i (PDB: 8OOI) states, respectively. The inset shows a magnified view of the α 5 helix in the D2 domain of p97 D395G in ADP.P i state.
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sodium salt  (Jena Bioscience)
92
Jena Bioscience sodium salt
a, Domain structure of p97, highlighting the D395G mutation located in the D1 domain. b, Schematic representation of preparation of ubiquitinated Ub₄-mEOS3.2 for the p97 substrate unfolding assay (top). Green Ub₄-mEOS3.2 was polyubiquitinated using E1, E2-25K, and ubiquitin, and subsequently photoconverted to its red form under UV illumination, as previously described . <t>The</t> <t>purified</t> substrate was then used in unfolding assays in the presence of the Ufd1-Npl4 complex. Compared with p97 WT (grey), p97 D395G (blue) exhibits reduced substrate unfolding activity (bottom). All measurements were performed with at least three technical replicates. c, NMR characterization of p97 D395G using the ND1L construct, comprising the NTD, D1 domain and linker. Key probes for NTD conformation and bound nucleotide are indicated in the schematic above. <t>ATPγS</t> induces an NTD ‘up’ conformation, similar to p97 WT . In the presence of ADP and the ATP reg , predominantly ‘down’ with a minor ‘up’ conformation is observed, in contrast to p97 WT . For comparison, spectra of the prototypical MSP-1-associated mutant p97 R95G in presence of ADP are shown, which display signals at an averaged position between NTD ‘up’ and ‘down’ conformation, indicating fast conformational exchange on the NMR time scale. This establishes that p97 D395G displays distinct molecular defects from MSP-1-type mutants. d, Cryo-EM reconstructions of p97 D395G under different conditions (ATPγS, ATP reg , and ADP). The N-terminal domain (NTD) is colored grey, and the D1 and D2 ATPase domains are shown in blue. Schematic representations on the left indicate the corresponding nucleotide-bound states. e, Backbone RMSD of a p97 D395G protomer relative to p97 WT in different nucleotide states, calculated without the NTD. p97 D395G structures in ATPγS (PDB: 28VN), ADP (PDB: 28VL), and ADP.P i (PDB: 28XW) states were aligned using the main chain atoms of the D1 and D2 domains to the published p97 WT models in the ATPγS (PDB: 5FTN), ADP (PDB: 5FTK), and ADP.P i (PDB: 8OOI) states, respectively. The inset shows a magnified view of the α 5 helix in the D2 domain of p97 D395G in ADP.P i state.
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Image Search Results


a, Domain structure of p97, highlighting the D395G mutation located in the D1 domain. b, Schematic representation of preparation of ubiquitinated Ub₄-mEOS3.2 for the p97 substrate unfolding assay (top). Green Ub₄-mEOS3.2 was polyubiquitinated using E1, E2-25K, and ubiquitin, and subsequently photoconverted to its red form under UV illumination, as previously described . The purified substrate was then used in unfolding assays in the presence of the Ufd1-Npl4 complex. Compared with p97 WT (grey), p97 D395G (blue) exhibits reduced substrate unfolding activity (bottom). All measurements were performed with at least three technical replicates. c, NMR characterization of p97 D395G using the ND1L construct, comprising the NTD, D1 domain and linker. Key probes for NTD conformation and bound nucleotide are indicated in the schematic above. ATPγS induces an NTD ‘up’ conformation, similar to p97 WT . In the presence of ADP and the ATP reg , predominantly ‘down’ with a minor ‘up’ conformation is observed, in contrast to p97 WT . For comparison, spectra of the prototypical MSP-1-associated mutant p97 R95G in presence of ADP are shown, which display signals at an averaged position between NTD ‘up’ and ‘down’ conformation, indicating fast conformational exchange on the NMR time scale. This establishes that p97 D395G displays distinct molecular defects from MSP-1-type mutants. d, Cryo-EM reconstructions of p97 D395G under different conditions (ATPγS, ATP reg , and ADP). The N-terminal domain (NTD) is colored grey, and the D1 and D2 ATPase domains are shown in blue. Schematic representations on the left indicate the corresponding nucleotide-bound states. e, Backbone RMSD of a p97 D395G protomer relative to p97 WT in different nucleotide states, calculated without the NTD. p97 D395G structures in ATPγS (PDB: 28VN), ADP (PDB: 28VL), and ADP.P i (PDB: 28XW) states were aligned using the main chain atoms of the D1 and D2 domains to the published p97 WT models in the ATPγS (PDB: 5FTN), ADP (PDB: 5FTK), and ADP.P i (PDB: 8OOI) states, respectively. The inset shows a magnified view of the α 5 helix in the D2 domain of p97 D395G in ADP.P i state.

Journal: bioRxiv

Article Title: The vacuolar tauopathy-associated mutation D395G confers redox sensitivity to p97/VCP

doi: 10.64898/2026.04.16.718620

Figure Lengend Snippet: a, Domain structure of p97, highlighting the D395G mutation located in the D1 domain. b, Schematic representation of preparation of ubiquitinated Ub₄-mEOS3.2 for the p97 substrate unfolding assay (top). Green Ub₄-mEOS3.2 was polyubiquitinated using E1, E2-25K, and ubiquitin, and subsequently photoconverted to its red form under UV illumination, as previously described . The purified substrate was then used in unfolding assays in the presence of the Ufd1-Npl4 complex. Compared with p97 WT (grey), p97 D395G (blue) exhibits reduced substrate unfolding activity (bottom). All measurements were performed with at least three technical replicates. c, NMR characterization of p97 D395G using the ND1L construct, comprising the NTD, D1 domain and linker. Key probes for NTD conformation and bound nucleotide are indicated in the schematic above. ATPγS induces an NTD ‘up’ conformation, similar to p97 WT . In the presence of ADP and the ATP reg , predominantly ‘down’ with a minor ‘up’ conformation is observed, in contrast to p97 WT . For comparison, spectra of the prototypical MSP-1-associated mutant p97 R95G in presence of ADP are shown, which display signals at an averaged position between NTD ‘up’ and ‘down’ conformation, indicating fast conformational exchange on the NMR time scale. This establishes that p97 D395G displays distinct molecular defects from MSP-1-type mutants. d, Cryo-EM reconstructions of p97 D395G under different conditions (ATPγS, ATP reg , and ADP). The N-terminal domain (NTD) is colored grey, and the D1 and D2 ATPase domains are shown in blue. Schematic representations on the left indicate the corresponding nucleotide-bound states. e, Backbone RMSD of a p97 D395G protomer relative to p97 WT in different nucleotide states, calculated without the NTD. p97 D395G structures in ATPγS (PDB: 28VN), ADP (PDB: 28VL), and ADP.P i (PDB: 28XW) states were aligned using the main chain atoms of the D1 and D2 domains to the published p97 WT models in the ATPγS (PDB: 5FTN), ADP (PDB: 5FTK), and ADP.P i (PDB: 8OOI) states, respectively. The inset shows a magnified view of the α 5 helix in the D2 domain of p97 D395G in ADP.P i state.

Article Snippet: For ADP and ATPγS-bound datasets of p97 D395G , purified p97 D395G was incubated in presence of ADP (#A2754 Sigma) and ATPγS (#NU-406 Jena Bioscience) for 15 minutes at room temperature.

Techniques: Mutagenesis, Ubiquitin Proteomics, Purification, Activity Assay, Construct, Comparison, Cryo-EM Sample Prep