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ProteomicsMice with fibrinogen-induced arthritis (FIA)
This SuperSeries is composed of the following subset Series: GSE18023: Mice with FIA develop anti-native and anti-in vitro citrullinated fibrinogen antibodies GSE18024: FIA plasma induces arthritis in naïve mice GSE18025: Fibrinogen-reactive T cells transfer disease to naïve mice Refer to individu...
ORGANISM(S): Mus musculus 
2010-05-05 | E-GEOD-18073 | biostudies-arrayexpress
ProteomicsMice with FIA develop anti-native and anti-in vitro citrullinated fibrinogen antibodies
Synovial antigen arrays were probed with 1:150 dilutions of plasma derived from SJL mice immunized with fibrinogen emulsified in CFA or with CFA alone. Autoantibody binding was detected with a Cy3-conjugated goat-anti-mouse IgG/M secondary antibody. SAM was applied to identify antigens with statis...
ORGANISM(S): Mus musculus 
2010-05-05 | E-GEOD-18023 | biostudies-arrayexpress
ProteomicsFibrinogen-reactive T cells transfer disease to naïve mice
Splenocytes harvested from mice with FIA were cultured in vitro and stimulated with 0.01 mg/ml fibrinogen for 3 days. Enriched T cells were transferred into 6-week-old naïve SJL mice, which developed visible signs of arthritis within 2 weeks. Synovial array profiling of plasma from the arthritic ...
ORGANISM(S): Mus musculus 
2010-05-05 | E-GEOD-18025 | biostudies-arrayexpress
TranscriptomicsFibrinogen promotes autoimmunity and demyelination via chemokine release and antigen presentation [Mm]
Determination of the mechanism by which fibrinogen, a central blood coagulation protein drives immunological responses targeted to the CNS. Results identify the factors involved in the regulation and provide mechanistic basis. We subjected fibrinogen-injected corpus callosum to microarray to determi...
ORGANISM(S): Mus musculus 
2015-09-16 | E-GEOD-71082 | biostudies-arrayexpress
TranscriptomicsFibrinogen-induced differentiation of WT adult neural stem cells into astrocytes
Examination of gene expression during adult neural stem cell differentiation after 3 and 12 hours after fibrinogen treatment compared to control.
ORGANISM(S): Mus musculus 
2016-03-09 | E-MTAB-3013 | biostudies-arrayexpress
ProteomicsOxidized fibrinogen HPLC-MS/MS
Fibrinogen is highly susceptible to oxidation compared to other plasma proteins. Fibrinogen oxidation damages its structure and affects the protein function. Fibrinogen was isolated from citrated human plasma by the modified cold ethanol precipitation technique. Oxidation of fibrinogen by ozone: a s...
ORGANISM(S): Homo sapiens (Human) 
2019-04-04 | PXD012046 | Pride
Oxidation Hplc-ms/ms Fibrinogen Oxidative post-translational modifications 
ProteomicsFIA plasma induces arthritis in naïve mice
Plasma collected from mice with FIA were pooled, and 0.3 ml was injected intravenously into 6-week-old naïve SJL mice on days 0 and 2. Synovial antigen array profiling of plasma from the arthritic recipient mice demonstrated autoreactive B-cell responses against peptides representing native fibrino...
ORGANISM(S): Mus musculus 
2010-05-05 | E-GEOD-18024 | biostudies-arrayexpress
ProteomicsRegulation of hepatic inclusions and fibrinogen biogenesis by SEL1L-HRD1 ERAD
Impaired secretion of an essential blood coagulation factor fibrinogen leads to hepatic fibrinogen storage disease (HFSD), characterized by the presence of fibrinogen-positive inclusion bodies and hypofibrinogenemia. However, the molecular mechanisms underlying the biogenesis of fibrinogen in the en...
ORGANISM(S): Mus musculus (Mouse) 
2024-09-11 | PXD047658 | Pride
Hepatocytes Sel1l-hrd1 erad Fibrinogen Inclusion bodies 
ProteomicsFibrinogen function achieved through multiple covalent states
Disulfide bonds link pairs of cysteine amino acids and their formation is assumed to be complete in the mature, functional protein. We tested this assumption by quantifying the redox state of disulfide bonds in the thrombosis protein, fibrinogen. There is an extraordinary disulfide lability in fibri...
ORGANISM(S): Homo sapiens (Human) 
2020-11-09 | PXD018564 | Pride
Redox state Fibrinogen Cysteines Alpha2 macroglobulin 
ProteomicsMultiple disulfide-bonded states confer conformational diversity in fibrinogen
Disulfide bonds constrain the polypeptide backbone and reduce conformational variability in proteins. The blood clotting protein fibrinogen is constitutively produced as multiple partially disulfide-bonded states, suggesting that individual fibrinogen molecules have a variety of conformational forms...
ORGANISM(S): Homo sapiens (Human) 
2026-04-13 | PXD076459 | Pride
Human Fibrinogen Disulfide bonds 
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