ArticleProtein & cell2010
Interaction of the α2A domain of integrin with small collagen fragments.
Article in Protein & cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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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.
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Who cites it
16 citing papers in PubMed.
- The effect of specific bioactive collagen peptides on function and muscle remodeling during human resistance training.Acta physiologica (Oxford, England) · 2023Trial
- Therapeutic potential of fish collagen hydrolysates in osteoporosis prevention: a narrative review based on cellular, molecular, and clinical evidence.Osteoporosis international : a journal established as result of cooperation between the European Foundation for Osteoporosis and the National Osteoporosis Foundation of the USA · 2026Review
- Oral Collagen Peptides and Vulvovaginal Radiofrequency Therapy for Genitourinary Syndrome of Menopause: A Pilot Randomized Study.Journal of clinical medicine · 2025Article
- Blood pH Analysis in Combination with Molecular Medical Tools in Relation to COVID-19 Symptoms.Biomedicines · 2023Article
- Assessing a computational pipeline to identify binding motifs to theFrontiers in chemistry · 2023Article
- Paradoxical Duel Role of Collagen in Rheumatoid Arthritis: Cause of Inflammation and Treatment.Bioengineering (Basel, Switzerland) · 2022Review
- Intra-articular MMP-1 in the spinal facet joint induces sustained pain and neuronal dysregulation in the DRG and spinal cord, and alters ligament kinematics under tensile loading.Frontiers in bioengineering and biotechnology · 2022Article
- Efficacy of Chondroprotective Food Supplements Based on Collagen Hydrolysate and Compounds Isolated from Marine Organisms.Marine drugs · 2021Article
- Evidence for Quantum Chemical Effects in Receptor-Ligand Binding Between Integrin and Collagen Fragments - A Computational Investigation With an Impact on Tissue Repair, Neurooncolgy and Glycobiology.Frontiers in molecular biosciences · 2021Article
- Intra-articular collagenase in the spinal facet joint induces pain, DRG neuron dysregulation and increased MMP-1 absent evidence of joint destruction.Scientific reports · 2020Article
- The Sialic Acid-Dependent Nematocyst Discharge Process in Relation to Its Physical-Chemical Properties Is A Role Model for Nanomedical Diagnostic and Therapeutic Tools.Marine drugs · 2019Article
- Significant Amounts of Functional Collagen Peptides Can Be Incorporated in the Diet While Maintaining Indispensable Amino Acid Balance.Nutrients · 2019Article
- Nanomedical Relevance of the Intermolecular Interaction Dynamics-Examples from Lysozymes and Insulins.ACS omega · 2019Article
- Cryptic binding sites become accessible through surface reconstruction of the type I collagen fibril.Scientific reports · 2018Article
- Metabolic Response of Human Osteoarthritic Cartilage to Biochemically Characterized Collagen Hydrolysates.International journal of molecular sciences · 2017Article
- Collagen metabolism of human osteoarthritic articular cartilage as modulated by bovine collagen hydrolysates.PloS one · 2013Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
We here present a detailed study of the ligand-receptor interactions between single and triple-helical strands of collagen and the α2A domain of integrin (α2A), providing valuable new insights into the mechanisms and dynamics of collagen-integrin binding at a sub-molecular level. The occurrence of single and triple-helical strands of the collagen fragments was scrutinized with atom force microscopy (AFM) techniques. Strong interactions of the triple-stranded fragments comparable to those of collagen can only be detected for the 42mer triple-helical collagen-like peptide under study (which contains 42 amino acid residues per strand) by solid phase assays as well as by surface plasmon resonance (SPR) measurements. However, changes in NMR signals during titration and characteristic saturation transfer difference (STD) NMR signals are also detectable when α2A is added to a solution of the 21mer single-stranded collagen fragment. Molecular dynamics (MD) simulations employing different sets of force field parameters were applied to study the interaction between triple-helical or single-stranded collagen fragments with α2A. It is remarkable that even single-stranded collagen fragments can form various complexes with α2A showing significant differences in the complex stability with identical ligands. The results of MD simulations are in agreement with the signal alterations in our NMR experiments, which are indicative of the formation of weak complexes between single-stranded collagen and α2A in solution. These results provide useful information concerning possible interactions of α2A with small collagen fragments that are of relevance to the design of novel therapeutic A-domain inhibitors.
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Registered trials
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