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Flexible regions in the molecular architecture of Human fibrin clots structurally resolved by XL-MS and integrative structural modeling

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Thrombin Flux and Wall Shear Rate Regulate Fibrin Fiber Deposition State during Polymerization under Flow

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Atomic Structural Models of Fibrin Oligomers

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Computer modeling of fibrin polymerization kinetics correlated with electron microscope and turbidity observations: clot structure and assembly are kinetically controlled

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Fibrinogen and Fibrin

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Chapter 7 Fibrinogen, fibrin and factor XIII

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51. Thrombin cleavage enhances exposure of a heparin binding domain in the N-terminus of the fibrin B chain

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Order out of complexity – protein structures that interact with heparin

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Cross-ID: Analysis and Visualization of Complex XL–MS-Driven Protein Interaction Networks

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Conversion of Fibrinogen to Fibrin: Mechanism of Exposure of tPA- and Plasminogen-Binding Sites

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2.8 Å Crystal Structures of Recombinant Fibrinogen Fragment D with and without Two Peptide Ligands: GHRP Binding to the “b” Site Disrupts Its Nearby Calcium-binding Site

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Binding of Synthetic B Knobs to Fibrinogen Changes the Character of Fibrin and Inhibits Its Ability To Activate Tissue Plasminogen Activator and Its Destruction by Plasmin

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On the Mechanism of αC Polymer Formation in Fibrin

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NMR Solution Structure, Stability, and Interaction of the Recombinant Bovine Fibrinogen αC-Domain Fragment

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Crystal Structure of Human Fibrinogen

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Crystal Structure of Fragment Double-D from Human Fibrin with Two Different Bound Ligands,

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Analysis of Aα251 Fibrinogen: The αC Domain Has a Role in Polymerization, Albeit More Subtle Than Anticipated from the Analogous Proteolytic Fragment X

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High-Resolution Visualization of Fibrinogen Molecules and Fibrin Fibers with Atomic Force Microscopy

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Global quantification of mammalian gene expression control

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Hereditary renal amyloidosis associated with a mutant fibrinogen α–chain

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The I-TASSER Suite: protein structure and function prediction

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Template-based protein structure modeling using the RaptorX web server

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Efficient and robust proteome-wide approaches for cross-linking mass spectrometry

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Limb proportions show developmental plasticity in response to embryo movement

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Does albumin play a role in fibrinolysis by its inhibition of plasminogen activation?

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Anticoagulant Albumin Fragments That Bind to Fibrinogen/Fibrin: Possible Implications

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Human endothelial cells synthesize and express an Arg-Gly-Asp-directed adhesion receptor involved in attachment to fibrinogen and von Willebrand factor.

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Fibroblasts Spread on Immobilized Fibrin Monomer by Mobilizing a β1-class Integrin, Together with a Vitronectin Receptor αvβ3 on Their Surface

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Fibrinogen Is a Ligand for Integrin α5β1 on Endothelial Cells

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The Molecular Weights, Mass Distribution, Chain Composition, and Structure of Soluble Fibrin Degradation Products Released from a Fibrin Clot Perfused with Plasmin

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Mass spectrometry–based molecular mapping of native FXIIIa cross-links in insoluble fibrin clots

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UniRef clusters: a comprehensive and scalable alternative for improving sequence similarity searches

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DisVis: quantifying and visualizing accessible interaction space of distance-restrained biomolecular complexes

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HHalign-Kbest: exploring sub-optimal alignments for remote homology comparative modeling

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Accounting for pairwise distance restraints in FFT-based protein–protein docking

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Protein structure prediction and analysis using the Robetta server

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ANNOVAR: functional annotation of genetic variants from high-throughput sequencing data

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ThreaDomEx: a unified platform for predicting continuous and discontinuous protein domains by multiple-threading and segment assembly

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CADD: predicting the deleteriousness of variants throughout the human genome

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Toward an understanding of fibrin branching structure

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Statistical potential for assessment and prediction of protein structures

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Molecular mechanisms of fibrinolysis

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Fibrinogen and fibrin structure and functions

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Evidence that fibrinogen γ′ directly interferes with protofibril growth: implications for fibrin structure and clot stiffness

inferredcites →https://doi.org/10.1111/j.1749-6632.2001.tb03491.xopenalex-snapshot

The Structure and Biological Features of Fibrinogen and Fibrin

inferredcites →https://doi.org/10.1111/j.1749-6632.2001.tb03517.xopenalex-snapshot

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Heparin-Binding Domains in Vascular Biology

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Synergistic inhibition of platelet aggregation by fibrinogen-related peptides.

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Molecular basis for fibrinogen Dusart (A alpha 554 Arg-->Cys) and its association with abnormal fibrin polymerization and thrombophilia.

inferredcites →https://doi.org/10.1182/blood-2005-05-2039openalex-snapshot

Polymerization of fibrin: specificity, strength, and stability of knob-hole interactions studied at the single-molecule level

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Polymerization of fibrin: direct observation and quantification of individual B:b knob-hole interactions

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Functional analysis of fibrin γ-chain cross-linking by activated factor XIII: determination of a cross-linking pattern that maximizes clot stiffness

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High prevalence of dysfibrinogenemia among patients with chronic thromboembolic pulmonary hypertension

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Visualization and identification of the structures formed during early stages of fibrin polymerization

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Mechanisms of fibrin polymerization and clinical implications

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VLITL is a major cross-β-sheet signal for fibrinogen Aα-chain frameshift variants

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Evidence for a second type of fibril branch point in fibrin polymer networks, the trimolecular junction

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Thrombin cleavage enhances exposure of a heparin binding domain in the N-terminus of the fibrin beta chain

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The impaired polymerization of fibrinogen Longmont (Bβ166Arg→Cys) is not improved by removal of disulfide-linked dimers from a mixture of dimers and cysteine-linked monomers

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Improved model quality assessment using ProQ2

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CPORT: A Consensus Interface Predictor and Its Performance in Prediction-Driven Docking with HADDOCK

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Identification of Fibrin Clot-Bound Plasma Proteins

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Capturing protein communities by structural proteomics in a thermophilic eukaryote

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Diagnosis, Pathogenesis, Treatment, and Prognosis of Hereditary Fibrinogen Aα-Chain Amyloidosis

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CRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRIN WITH TWO DIFFERENT BOUND LIGANDS

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Mechanobiology of Platelets: Techniques to Study the Role of Fluid Flow and Platelet Retraction Forces at the Micro- and Nano-Scale

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Hereditary Fibrinogen Aα-Chain Amyloidosis in Asia: Clinical and Molecular Characteristics

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1038/s41467-020-14608-2openalex-snapshot

A synthetic peptide library for benchmarking crosslinking-mass spectrometry search engines for proteins and protein complexes

inferred← citeshttps://doi.org/10.1073/pnas.1911785117openalex-snapshot

Missing regions within the molecular architecture of human fibrin clots structurally resolved by XL-MS and integrative structural modeling

inferred← citeshttps://doi.org/10.1101/821447openalex-snapshot

A synthetic peptide library for benchmarking crosslinking mass spectrometry search engines

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