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UnknownHallmarks of Alpha- and Betacoronavirus non-structural protein 7+8 complexes.
Not available
S-EPMC7536876 | biostudies-literature
UnknownHallmarks of Alpha- and Betacoronavirus non-structural protein 7+8 complexes.
Not available
S-EPMC7929516 | biostudies-literature
UnknownA docking model based on mass spectrometric and biochemical data describes phage packaging motor incorporation.
Not available
S-EPMC2938058 | biostudies-literature
ProteomicsGlycan-induced structural dynamics in human norovirus P dimers depend on the virus strain and deamidation status
Noroviruses are non-enveloped (+) single stranded RNA viruses of the Caliciviridae family that cause an estimated 20 % of gastroenteritis cases worldwide . The virus possesses an icosahedral capsid, build by the two structural proteins VP1 and VP2. Noroviruses of genogroup II, especially GII.4, domi...
ORGANISM(S): Norwalk virus Norovirus Hu/GII.4/Saga4/2009/JP Norovirus Hu/GII/JP/2015/GII.P17_GII.17/Kawasaki308 Norovirus Hu/GII.4/MI001/2011/USA 
2021-04-08 | PXD019884 | Pride
Protein dynamics Norovirus Glycan Hdx-ms Interaction Deamidation 
ProteomicsMapping the peptide binding groove of MHC class I
An essential element of adaptive immunity is the selective binding of peptide antigens by major histocompatibility complex (MHC) class I proteins and their presentation to cytotoxic T lymphocytes on the cell surface. Using native mass spectrometry, we here analyze the binding of peptides to an empty...
ORGANISM(S): Homo sapiens (Human) 
2022-05-31 | PXD027725 | Pride
Peptide-binding Hla-a Native ms Human Mhc class i 
ProteomicsDissociation of β2m from MHC Class I triggers formation of noncovalent, transient heavy chain dimers
At the plasma membrane of mammalian cells, major histocompatibility complex class I molecules (MHC-I) present antigenic peptides to cytotoxic T cells. Following the loss of the peptide and the light chain beta-2 microglobulin (beta2m), the resulting free heavy chains (FHCs) can associate into homoty...
ORGANISM(S): Homo sapiens (Human) 
2022-05-11 | PXD033485 | Pride
Hla-a Dimerization Native ms Human Mhc class i 
UnknownStructure and target interaction of a G-quadruplex RNA-aptamer.
Not available
S-EPMC5056769 | biostudies-literature
ProteomicsInteractions of human norovirus capsid P domain with histo-blood group antigens with Hydrogen-Deuterium Exchange Mass Spectrometry
Attachment of human noroviruses to histo blood group antigens (HBGAs) is essential for infection, but how this binding event promotes the infection of host cells is unknown. Here, we employed protein NMR experiments supported by mass spectrometry and crystallography to study HBGA binding to the P ...
ORGANISM(S): Norwalk virus Norovirus Hu/GII/JP/2015/GII.P17_GII.17/Kawasaki308 Norovirus Hu/GII.4/MI001/2011/USA Norovirus Hu/GII-4/Saga4/2006/JP 
2019-03-20 | PXD011914 | Pride
Hdx ms P domain Gii.4 saga Human norovirus Histo-blood group antigens 
ProteomicsNative mass spectrometry of peptide-free and partially loaded MHC class I molecules
A disulfide-stabilized MHC class I molecule (HLA-A*02:01(Y84C/A139C), short dsA2) was characterized by native mass spectrometry. dsA2 was shown to be structurally intact in absence of any peptide whereas its wild type form was not. Furthermore, it was observed that the mutation did not disrupt the b...
ORGANISM(S): Homo sapiens (Human) 
2022-05-11 | PXD016708 | Pride
Peptide-binding Hla-a Native ms Human Mhc class i 
ProteomicsN-terminal VP1 truncation favor T=1 norovirus-like particles
Noroviruses cause immense sporadic gastroenteritis outbreaks worldwide. Upcoming genotypes, which are divided based on VP1 sequence, further enhance this public thread regularly. Self-assembling properties of the human norovirus major capsid protein VP1 are crucial for using virus-like particles (VL...
ORGANISM(S): Norovirus 
2021-01-11 | PXD023182 | Pride
Capsid assembly Norovirus Vp1 truncation 
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