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Mechanism of in vivo activation of the MutLgamma-Exo1 complex for meiotic crossover formation
- Authors
- Borde, Valerie
- Description
Summary from the GEO: "Programmed DNA double-strand breaks (DSBs) initiate meiotic recombination and their subsequent repair culminates in crossover (CO) formation. COs result from the asymmetric cleavage of double-Holliday junction (dHJ) intermediates, that requires the MutLγ complex together with a non-catalytic function of Exo1, an activity essential for fertility but at risk of generating unwanted...
- Subject
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DNA Breaks, Double-StrandedMeiosisMutL ProteinsProtein BindingRecombination, Genetic
- Access Rights
- Free to All
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Mechanism of in vivo activation of the MutL-Exo1 complex for meiotic crossover formation
- Authors
- Sanchez, AuroreMu, XiaojingBorde, ValerieKeeney, Scott
- Description
Summary from the GEO: "Programmed DNA double-strand breaks (DSBs) initiate meiotic recombination and their subsequent repair culminates in crossover (CO) formation. COs result from the asymmetric cleavage of double-Holliday junction (dHJ) intermediates, that requires the MutLγ endonuclease and a non-catalytic function of Exo1, an activity essential for fertility but at risk of generating unwanted...
- Subject
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DNA Breaks, Double-StrandedMeiosisMutL ProteinsProtein BindingRecombination, Genetic
- Access Rights
- Free to All
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Crystal Structure of a nanobody-stabilized active state of the kappa-opioid receptor
- Authors
- Che, TaoMajumdar, SusrutaZaidi, Saheem A.Ondachi, Pauline20 more author(s)...
- Description
This deposit in the Research Collaboratory for Structural Bioinformatics Protein Data Base (PDB) includes x-ray diffraction data used for modeling the crystal structure of a nanobody-stabilized active state of the kappa-opioid receptor. The main summary display for this entry includes information on the experimental data, validation, macromolecules, small molecules, version history and funding information....
- Subject
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Protein BindingReceptors, Opioid, kappa
- Access Rights
- Free to All
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5VNG: Crystal structure of Sec23a/Sec24a/Sec22 complexed with a C-terminal II sorting motif
- Authors
- Ma, WenfuGoldberg, Jonathan
- Description
This deposit in the Research Collaboratory for Structural Bioinformatics Protein Data Base (PDB) includes x-ray diffraction data identifying the crystal structure of Crystal structure of Sec23a/Sec24a/Sec22 complexed with a C-terminal II sorting motif. The main summary display for this entry includes information on the experimental method, protein source, macromolecules and small molecules included...
- Subject
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Models, ChemicalModels, MolecularProtein BindingProtein Transport
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5VNE: Crystal structure of Sec23a/Sec24a/Sec22 complexed with Emp24 sorting motif
- Authors
- Ma, WenfuGoldberg, Jonathan
- Description
This deposit in the Research Collaboratory for Structural Bioinformatics Protein Data Base (PDB) includes x-ray diffraction data identifying the crystal structure of Sec23a/Sec24a/Sec22 complexed with Emp24 sorting motif. The main summary display for this entry includes information on the experimental method, protein source, macromolecules and small molecules included in the deposit, and version...
- Subject
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Models, ChemicalModels, MolecularProtein BindingProtein Transport
- Access Rights
- Free to All
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DPP9 activity and not protein binding inhibits the CARD8 inflammasome
- Authors
- Griswold, AndrewBachovchin, Daniel
- Description
Inflammasomes are multiprotein complexes formed in response to pathogens. NLRP1 and CARD8 are related proteins that form inflammasomes, but the pathogen-associated signal(s) and the molecular mechanisms controlling their activation have not been established. Inhibitors of the serine dipeptidyl peptidases DPP8 and DPP9 (DPP8/9) were recently discovered to activate both NLRP1 and CARD8. Interestingly,...
- Subject
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CARD Signaling Adaptor ProteinsDipeptidyl-Peptidases and Tripeptidyl-PeptidasesInflammasomesMass spectrometryProtein BindingProteomics
- Access Rights
- Free to All
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Mutant calreticulin binders analysis
- Authors
- Kentsis, Alex
- Description
Mutant, truncated and wild-type human calreticul was co-purified with binding proteins
- Subject
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CalreticulinLiquid Chromatography-Mass SpectrometryMass spectrometryProtein Binding
- Access Rights
- Free to All
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Mutant PP2A interactome
- Authors
- Kentsis, Alex
- Description
Affinity enrichment of ligand to mutant and wild-type PP2A protein
- Subject
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LigandsLiquid Chromatography-Mass SpectrometryProtein BindingProtein Phosphatase 2
- Access Rights
- Free to All
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Oxidized thioredoxin-1 restrains the NLRP1 inflammasome
- Authors
- Ball, DanielBachovchin, Daniel
- Description
To find cellular protein binding partners of the NLRP1 inflammasome, FLAG-tagged full length NLRP1 (or a GFP-FLAG protein control) was ectopically expressed in HEK 293T cells and affinity purified from cell lysates (Note: the NLRP1-FLAG-containing lysate samples were affinity purified in the presence or absence of excess proline) before proteins were reduced, alkylated, and trypsinized before TMT...
- Subject
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HEK293 CellsInflammasomesLiquid Chromatography-Mass SpectrometryProtein BindingProteome
- Access Rights
- Free to All