scholarly article | Q13442814 |
P356 | DOI | 10.1074/JBC.M114.631804 |
P8608 | Fatcat ID | release_r7lnrmmlirfhdkmi3m53nr4i4a |
P932 | PMC publication ID | 4392246 |
P698 | PubMed publication ID | 25713138 |
P50 | author | Toshiya Senda | Q58326815 |
Naoyuki Kuwabara | Q64682251 | ||
P2093 | author name string | Ryuichi Kato | |
Hirofumi Matsumoto | |||
Hiroyuki Kawahara | |||
Naoto Yokota | |||
Ryosuke Minami | |||
P2860 | cites work | A ribosome-associating factor chaperones tail-anchored membrane proteins | Q24293683 |
A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation | Q24305231 | ||
SGTA recognizes a noncanonical ubiquitin-like domain in the Bag6-Ubl4A-Trc35 complex to promote endoplasmic reticulum-associated degradation | Q24306367 | ||
Bag6 complex contains a minimal tail-anchor-targeting module and a mock BAG domain | Q24311324 | ||
USP13 antagonizes gp78 to maintain functionality of a chaperone in ER-associated degradation | Q24320201 | ||
A "housekeeping" gene on the X chromosome encodes a protein similar to ubiquitin | Q24339641 | ||
Scythe regulates apoptosis through modulating ubiquitin-mediated proteolysis of the Xenopus elongation factor XEF1AO. | Q41895930 | ||
Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion | Q44959545 | ||
Prediction of protein secondary structure from circular dichroism using theoretically derived spectra | Q45421787 | ||
Unique proteasome subunit Xrpn10c is a specific receptor for the antiapoptotic ubiquitin-like protein Scythe | Q48109396 | ||
Automated matching of high- and low-resolution structural models | Q56444545 | ||
PRIMUS: a Windows PC-based system for small-angle scattering data analysis | Q57091059 | ||
Determination of domain structure of proteins from X-ray solution scattering | Q24537462 | ||
Reversible inhibition of Hsp70 chaperone function by Scythe and Reaper | Q24545641 | ||
A gene pair from the human major histocompatibility complex encodes large proline-rich proteins with multiple repeated motifs and a single ubiquitin-like domain | Q24558733 | ||
PHENIX: a comprehensive Python-based system for macromolecular structure solution | Q24654617 | ||
BAG4/SODD protein contains a short BAG domain | Q27639158 | ||
Crystal Structure of Get4-Get5 Complex and Its Interactions with Sgt2, Get3, and Ydj1 | Q27659241 | ||
Structural characterization of the Get4/Get5 complex and its interaction with Get3 | Q27662391 | ||
Structures of the Sgt2/SGTA Dimerization Domain with the Get5/UBL4A UBL Domain Reveal an Interaction that Forms a Conserved Dynamic Interface | Q27675050 | ||
Get5 Carboxyl-terminal Domain Is a Novel Dimerization Motif That Tethers an Extended Get4/Get5 Complex | Q27676804 | ||
XDS | Q27860472 | ||
Towards automated crystallographic structure refinement with phenix.refine | Q27860678 | ||
Features and development of Coot | Q27861079 | ||
SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae | Q27931740 | ||
The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome | Q28144546 | ||
Molecular chaperone targeting and regulation by BAG family proteins | Q28190053 | ||
Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling | Q28202126 | ||
Identification of a targeting factor for posttranslational membrane protein insertion into the ER | Q28294726 | ||
BAG-6 is essential for selective elimination of defective proteasomal substrates | Q28505838 | ||
Solution structure of the SGTA dimerisation domain and investigation of its interactions with the ubiquitin-like domains of BAG6 and UBL4A | Q28545114 | ||
SGTA antagonizes BAG6-mediated protein triage | Q28596609 | ||
Development of an automated large-scale protein-crystallization and monitoring system for high-throughput protein-structure analyses. | Q30356430 | ||
BAT3 guides misfolded glycoproteins out of the endoplasmic reticulum | Q34103187 | ||
The association of BAG6 with SGTA and tail-anchored proteins | Q34637885 | ||
Protein targeting and degradation are coupled for elimination of mislocalized proteins | Q35147351 | ||
The complex process of GETting tail-anchored membrane proteins to the ER. | Q35986793 | ||
Structures of Get3, Get4, and Get5 provide new models for TA membrane protein targeting | Q36570230 | ||
A ubiquitin-like domain recruits an oligomeric chaperone to a retrotranslocation complex in endoplasmic reticulum-associated degradation | Q36947746 | ||
The BAG proteins: a ubiquitous family of chaperone regulators | Q37081047 | ||
Tail-anchored membrane protein insertion into the endoplasmic reticulum | Q37140792 | ||
Protein quality control in the ER: balancing the ubiquitin checkbook | Q37953004 | ||
Post-translational translocation into the endoplasmic reticulum | Q38069735 | ||
BAG6/BAT3: emerging roles in quality control for nascent polypeptides | Q38070391 | ||
Bag6/Bat3/Scythe: a novel chaperone activity with diverse regulatory functions in protein biogenesis and degradation. | Q38082449 | ||
BAG-6, a jack of all trades in health and disease | Q38168708 | ||
Sequential interplay between BAG6 and HSP70 upon heat shock | Q39862448 | ||
Bat3 promotes the membrane integration of tail-anchored proteins | Q41113412 | ||
P433 | issue | 15 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 9387-9398 | |
P577 | publication date | 2015-02-20 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | Structure of a BAG6 (Bcl-2-associated athanogene 6)-Ubl4a (ubiquitin-like protein 4a) complex reveals a novel binding interface that functions in tail-anchored protein biogenesis | |
P478 | volume | 290 |
Q40215164 | A conserved island of BAG6/Scythe is related to ubiquitin domains and participates in short hydrophobicity recognition. |
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Q64104486 | Cytoplasmic control of Rab family small GTPases through BAG6 |
Q44897873 | Elimination of a signal sequence-uncleaved form of defective HLA protein through BAG6. |
Q47800028 | Heat Shock Protein A2 (HSPA2): Regulatory Roles in Germ Cell Development and Sperm Function. |
Q100235790 | Insertion of tail-anchored proteins into the endoplasmic reticulum membrane |
Q42011073 | Structural and functional insights into the E3 ligase, RNF126. |
Q55657250 | Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control. |
Q100157385 | Tail-anchored protein:SGTA dimer binds BAG6:GET4:UBL4A and ASNA1:ATP |
Q38775370 | UBQLN4 recognizes mislocalized transmembrane domain proteins and targets these to proteasomal degradation |
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