![Entry pathways of the pseudotype VSVs. Huh7 cells were pretreated with... | Download Scientific Diagram Entry pathways of the pseudotype VSVs. Huh7 cells were pretreated with... | Download Scientific Diagram](https://www.researchgate.net/profile/Ruey-Yi-Chang/publication/51722294/figure/fig3/AS:203192123039749@1425456185181/Silencing-Hdj2-using-siRNA-decreases-JEV-NS5-production-HEK293-cells-were-transfected_Q320.jpg)
Entry pathways of the pseudotype VSVs. Huh7 cells were pretreated with... | Download Scientific Diagram
![BAG‐1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release | The EMBO Journal BAG‐1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release | The EMBO Journal](https://www.embopress.org/cms/asset/6efc3d90-eb6e-41b6-9f1b-1330202facd1/embj7591377-fig-0006-m.jpg)
BAG‐1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release | The EMBO Journal
![Endoplasmic Reticulum Protein Quality Control Is Determined by Cooperative Interactions between Hsp/c70 Protein and the CHIP E3 Ligase* - Journal of Biological Chemistry Endoplasmic Reticulum Protein Quality Control Is Determined by Cooperative Interactions between Hsp/c70 Protein and the CHIP E3 Ligase* - Journal of Biological Chemistry](https://els-jbs-prod-cdn.jbs.elsevierhealth.com/cms/asset/815fb185-c4e9-41f5-ae32-04c44c9e98e3/gr1.jpg)
Endoplasmic Reticulum Protein Quality Control Is Determined by Cooperative Interactions between Hsp/c70 Protein and the CHIP E3 Ligase* - Journal of Biological Chemistry
Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1. - Abstract - Europe PMC
The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. - Abstract - Europe PMC
![PDF) Bimston DN, Song J, Winchester D, Takayama S, Reed JC, Morimoto RI.. BAG-1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release. EMBO J 17: 6871-6878 PDF) Bimston DN, Song J, Winchester D, Takayama S, Reed JC, Morimoto RI.. BAG-1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release. EMBO J 17: 6871-6878](https://www.researchgate.net/profile/Richard-Morimoto/publication/13443229/figure/fig2/AS:282024494551072@1444251287864/BAG-1-prevents-ATP-dependent-substrate-release-125-IRCMLA-28-m-M-was-incubated_Q320.jpg)
PDF) Bimston DN, Song J, Winchester D, Takayama S, Reed JC, Morimoto RI.. BAG-1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release. EMBO J 17: 6871-6878
The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. - Abstract - Europe PMC
![The C-terminal GGAP motif of Hsp70 mediates substrate recognition and stress response in yeast - Journal of Biological Chemistry The C-terminal GGAP motif of Hsp70 mediates substrate recognition and stress response in yeast - Journal of Biological Chemistry](https://els-jbs-prod-cdn.jbs.elsevierhealth.com/cms/attachment/63da5ec8-9268-445f-9be9-b8d94024a8f6/gr1_lrg.jpg)
The C-terminal GGAP motif of Hsp70 mediates substrate recognition and stress response in yeast - Journal of Biological Chemistry
The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. - Abstract - Europe PMC
![Human SH-SY5Y cell lines stably expressing Lamp2a display increased CMA... | Download Scientific Diagram Human SH-SY5Y cell lines stably expressing Lamp2a display increased CMA... | Download Scientific Diagram](https://www.researchgate.net/profile/Maria-Xilouri/publication/237148277/figure/fig3/AS:667856882642946@1536240897097/Human-SH-SY5Y-cell-lines-stably-expressing-Lamp2a-display-increased-CMA-activity-which_Q640.jpg)
Human SH-SY5Y cell lines stably expressing Lamp2a display increased CMA... | Download Scientific Diagram
![PDF) A general approach for the synthesis of 5-substituted-4-amino-pyrrolidin-2-ones and 5-substituted-4-amino-3-pyrrolin-2-ones | Sergio Pinheiro - Academia.edu PDF) A general approach for the synthesis of 5-substituted-4-amino-pyrrolidin-2-ones and 5-substituted-4-amino-3-pyrrolin-2-ones | Sergio Pinheiro - Academia.edu](https://0.academia-photos.com/attachment_thumbnails/44097398/mini_magick20190215-15345-1cid4e1.png?1550223514)
PDF) A general approach for the synthesis of 5-substituted-4-amino-pyrrolidin-2-ones and 5-substituted-4-amino-3-pyrrolin-2-ones | Sergio Pinheiro - Academia.edu
![PDF) Bimston DN, Song J, Winchester D, Takayama S, Reed JC, Morimoto RI.. BAG-1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release. EMBO J 17: 6871-6878 PDF) Bimston DN, Song J, Winchester D, Takayama S, Reed JC, Morimoto RI.. BAG-1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release. EMBO J 17: 6871-6878](https://www.researchgate.net/profile/Richard-Morimoto/publication/13443229/figure/fig4/AS:282024498745350@1444251288163/Effects-of-Hdj-1-or-BAG-1-on-Hsp70-ATPase-activity-A-Time-dependence-of-g-32_Q320.jpg)
PDF) Bimston DN, Song J, Winchester D, Takayama S, Reed JC, Morimoto RI.. BAG-1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release. EMBO J 17: 6871-6878
![BAG‐1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release | The EMBO Journal BAG‐1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release | The EMBO Journal](https://www.embopress.org/cms/asset/fc254a2e-7a98-48b5-bf5f-0fef50e35b3f/embj7591377-fig-0004-m.jpg)
BAG‐1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release | The EMBO Journal
The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. - Abstract - Europe PMC
The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. - Abstract - Europe PMC
![PDF) Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1 PDF) Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1](https://i1.rgstatic.net/publication/15423781_Identification_of_a_regulatory_motif_in_Hsp70_that_affects_ATPase_activity_substrate_binding_and_interaction_with_HDJ-1/links/0c9605289412ebd82c000000/largepreview.png)