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ProteomicsDisulfide mapping of J-chain by crosslinking MS
Here we show how J-chain (JC) outcompetes the sixth IgM subunit during assembly. We looked at the disulfide re-arrangements in JC and showed that it exists as an unstructured protein with non-native disulfides before its insertion into IgM.
ORGANISM(S): Mus musculus (Mouse) 
2024-12-04 | PXD048614 | Pride
Disulfide J-chain Crosslinking 
UnknownHow J-chain ensures the assembly of immunoglobulin IgM pentamers
Not available
S-SCDT-10_1038-S44318-024-00317-9 | biostudies-other
UnknownSystemically Administered TLR7/8 Agonist and Antigen-Conjugated Nanogels Govern Immune Responses against Tumors.
Not available
S-EPMC8945363 | biostudies-literature
ProteomicsPhosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble
Hsp26 is a small heat shock protein (sHsp) from S. cerevisiae. It is known to be activated by dissociation of the oligomer at heat shock temperatures. We wondered whether phosphorylation regulates its activity at physiological temperatures. In Hsp26, 9 phosphorylation sites which are located in diff...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2021-12-17 | PXD025314 | Pride
Hsp26 Phosphorylation Shsp 
UnknownPeptide-Decorated Degradable Polycarbonate Nanogels for Eliciting Antigen-Specific Immune Responses.
Not available
S-EPMC10607756 | biostudies-literature
ProteomicsThe isoforms of the molecular chaperone Hsp90 from S. cerevisiae differ in structure, function and client range
The molecular chaperone Hsp90 is an important regulator of proteostasis. It has remained unclear why S. cerevisiae possesses two Hsp90 isoforms, the constitutively expressed Hsc82 and the stress-inducible Hsp82. Here, we report distinct differences despite a sequence identity of 97 %. Consistent wit...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2019-08-12 | PXD013955 | Pride
Yeast Hsp90 Hsc90 
ProteomicsThe heat shock response in yeast is modular and maintains protein homeostasis via distinct mechanisms
We globally analyzed the heat stress response (HSR) in yeast on the transcriptomic, tranlatomic and the proteomic level. The cells were stressed at 37 °C, 42 °C and 46 °C and the fractionated proteomes measured on a Fusion and Q-Exactive Plus (both Thermo) mass spectrometer, respectively. With this ...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2019-12-25 | PXD014189 | Pride
Chaperones Phase transition Silac Lfq Heat shock response Proteome 
ProteomicsThe heat shock response relies on orthogonal mechanisms to maintain protein homeostasis in yeast
We globally analyzed the heat stress response (HSR) in yeast on the transcriptomic, tranlatomic and the proteomic level. The cells were stressed at 37 °C, 42 °C and 46 °C and the fractionated proteomes measured on a Fusion mass spectrometer. With this approach we were able to reveal a modular charac...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2020-01-07 | PXD016125 | Pride
Chaperones Heat shock response Proteome Aggregation 
ProteomicsThe permanently chaperone-active small heat shock protein Hsp17 from C. elegans exhibits topological separation of its N-terminal regions
Small Heat shock proteins (sHsps) are a family of molecular chaperones that bind non-native proteins in an ATP-independent manner. C. elegans encodes 16 different sHsps, among them Hsp17, which is evolutionarily distinct from other sHsps in the nematode. The structure and mechanism of Hsp17 and how ...
ORGANISM(S): Caenorhabditis elegans 
2022-12-08 | PXD028080 | Pride
Hsp-17 Cehsp17 Shsps C. elegans Chaperone Hsp17 Small heat shock protein 
ProteomicsThe permanently chaperone-active small heat shock protein Hsp17 from C. elegans exhibits topological separation of its N-terminal regions
Small Heat shock proteins (sHsps) are a family of molecular chaperones that bind non-native proteins in an ATP-independent manner. C. elegans encodes 16 different sHsps, among them Hsp17, which is evolutionarily distinct from other sHsps in the nematode. The structure and mechanism of Hsp17 and how ...
ORGANISM(S): Caenorhabditis elegans 
2022-12-08 | PXD038019 | Pride
Molecular chaperone Protein structure Protein aggregation Small heat shock protein 
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