ArticleBiochemistry2013
Structural insights into fibrinogen dynamics using amide hydrogen/deuterium exchange mass spectrometry.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- The Rho guanine-nucleotide exchange factor P-Rex2 exhibits structural and regulatory features distinct from the related RhoGEF P-Rex1.The Journal of biological chemistry · 2026Article
- P-Rex2 exhibits unique structural features and regulatory mechanisms distinct from the closely related RhoGEF P-Rex1.bioRxiv : the preprint server for biology · 2026Article
- Fibrin as a Versatile Fibrous Biopolymer.Sub-cellular biochemistry · 2026Review
- Antioxidant evolution of fibrinogen: a crucial role of methionines.Biophysical reviews · 2025Review
- Deconstructing fibrin(ogen) structure.Journal of thrombosis and haemostasis : JTH · 2025Review
- A novel gain-of-function phosphorylation site modulates PTPN22 inhibition of TCR signaling.The Journal of biological chemistry · 2024Article
- Systematic mapping of the conformational landscape and dynamism of soluble fibrinogen.Journal of thrombosis and haemostasis : JTH · 2023Article
- Fundamentals of HDX-MS.Essays in biochemistry · 2023Review
- Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition.Nature communications · 2022Article
- Erythrocyte Fraction in Thrombi Is Increased with Serum Iron by Influencing Fibrin Networks via Oxidative Stress.Oxidative medicine and cellular longevity · 2021Article
- Fibrinogen and Fibrin.Sub-cellular biochemistry · 2021Review
- A substitution in cGMP-dependent protein kinase 1 associated with aortic disease induces an active conformation in the absence of cGMP.The Journal of biological chemistry · 2020Article
- CMT disease severity correlates with mutation-induced open conformation of histidyl-tRNA synthetase, not aminoacylation loss, in patient cells.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Optimized Fragmentation for Quantitative Analysis of Fucosylated N-Glycoproteins by LC-MS-MRM.Analytical chemistry · 2019Article
- A Site of Vulnerability on the Influenza Virus Hemagglutinin Head Domain Trimer Interface.Cell · 2019Article
- Small-molecule allosteric inhibitors of BAX.Nature chemical biology · 2019Article
- Bidirectional modulation of HIF-2 activity through chemical ligands.Nature chemical biology · 2019Article
- Fibrinogen and the prediction of residual obstruction manifested after pulmonary embolism treatment.The European respiratory journal · 2018Observational
- Article
- The quaternary architecture of RARβ-RXRα heterodimer facilitates domain-domain signal transmission.Nature communications · 2017Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
We determined the amide hydrogen/deuterium exchange profile of native human fibrinogen under physiologic conditions. After optimization of the quench and proteolysis conditions, more than 1,200 peptides were identified by mass spectrometry, spanning more than 90% of the constituent Aα, Bβ, and γ chain amino acid sequences. The compact central and distal globular regions of fibrinogen were well protected from deuterium exchange, with the exception of the unfolded amino-terminal segments of the Aα and Bβ chains extending from the central region, and the short γ chain "tail" extending from each distal globular region. The triple-helical coiled-coil regions, which bridge the central region to each distal region, were also well protected with the exception of a moderately fast-exchanging area in the middle of each coiled-coil adjacent to the γ chain carbohydrate attachment site. These dynamic regions appear to provide flexibility to the fibrinogen molecule. The γ chain "out loop" contained within each coiled-coil also exchanged rapidly. The αC domain (Aα 392-610) exchanged rapidly, with the exception of a short segment sandwiched between a conserved disulfide linkage in the N-terminal αC subdomain. This latter finding is consistent with a mostly disordered structure for the αC domain in native fibrinogen. Analysis of the dysfibrinogen Bβ 235 Pro/Leu, which exhibits abnormal fibrin structure, revealed enhanced deuterium exchange surrounding the Pro/Leu substitution site as well as in the vicinity of the high affinity calcium binding site and the A knob polymerization pocket within the γC domain. The implication of these changes with respect to fibrin structure is discussed.
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