ArticleBiochemistry2007
NMR solution structure, stability, and interaction of the recombinant bovine fibrinogen alphaC-domain fragment.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
24 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Recommendations for nomenclature on fibrinogen and fibrin.Journal of thrombosis and haemostasis : JTH · 2009Guideline
- Fibrin as a Versatile Fibrous Biopolymer.Sub-cellular biochemistry · 2026Review
- Hyperelasticity of blood clots: Bridging the gap between microscopic and continuum scales.Journal of the mechanics and physics of solids · 2024Article
- Article
- The Story of the Fibrin(ogen) αC-Domains: Evolution of Our View on Their Structure and Interactions.Thrombosis and haemostasis · 2022Review
- Fibrin(ogen) as a Therapeutic Target: Opportunities and Challenges.International journal of molecular sciences · 2021Review
- Fibrinogen αC-regions are not directly involved in fibrin polymerization as evidenced by a "Double-Detroit" recombinant fibrinogen mutant and knobs-mimic peptides.Journal of thrombosis and haemostasis : JTH · 2020Article
- Missing regions within the molecular architecture of human fibrin clots structurally resolved by XL-MS and integrative structural modeling.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Oxidation-induced destabilization of the fibrinogen αC-domain dimer investigated by molecular dynamics simulations.Proteins · 2019Article
- Atomic Structural Models of Fibrin Oligomers.Structure (London, England : 1993) · 2018Article
- Biophysical Mechanisms Mediating Fibrin Fiber Lysis.BioMed research international · 2017Review
- Fibrin-based biomaterials: modulation of macroscopic properties through rational design at the molecular level.Acta biomaterialia · 2014Review
- Structural effects of methionine oxidation on isolated subdomains of human fibrin D and αC regions.PloS one · 2014Article
- Structural insights into fibrinogen dynamics using amide hydrogen/deuterium exchange mass spectrometry.Biochemistry · 2013Article
- Hydrodynamic characterization of recombinant human fibrinogen species.Thrombosis research · 2013Article
- On the mechanism of αC polymer formation in fibrin.Biochemistry · 2012Article
- Structure, stability, and interaction of fibrin αC-domain polymers.Biochemistry · 2011Article
- Molecular mechanisms affecting fibrin structure and stability.Arteriosclerosis, thrombosis, and vascular biology · 2011Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
According to the existing hypothesis, in fibrinogen, the COOH-terminal portions of two Aalpha chains are folded into compact alphaC-domains that interact intramolecularly with each other and with the central region of the molecule; in fibrin, the alphaC-domains switch to an intermolecular interaction resulting in alphaC-polymers. In agreement, our recent NMR study identified within the bovine fibrinogen Aalpha374-538 alphaC-domain fragment an ordered compact structure including a beta-hairpin restricted at the base by a 423-453 disulfide linkage. To establish the complete structure of the alphaC-domain and to further test the hypothesis, we expressed a shorter alphaC-fragment, Aalpha406-483, and performed detailed analysis of its structure, stability, and interactions. NMR experiments on the Aalpha406-483 fragment identified a second loose beta-hairpin formed by residues 459-476, yielding a structure consisting of an intrinsically unstable mixed parallel/antiparallel beta-sheet. Size-exclusion chromatography and sedimentation velocity experiments revealed that the Aalpha406-483 fragment forms soluble oligomers whose fraction increases with an increase in concentration. This was confirmed by sedimentation equilibrium analysis, which also revealed that the addition of each monomer to an assembling alphaC-oligomer substantially increases its stabilizing free energy. In agreement, unfolding experiments monitored by CD established that oligomerization of Aalpha406-483 results in increased thermal stability. Altogether, these experiments establish the complete NMR solution structure of the Aalpha406-483 alphaC-domain fragment, provide direct evidence for the intra- and intermolecular interactions between the alphaC-domains, and confirm that these interactions are thermodynamically driven.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.