ArticleThe Journal of biological chemistry2009
Interdomain flexibility in full-length matrix metalloproteinase-1 (MMP-1).
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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
31 citing papers in PubMed, 76 citations in OpenAlex.
- High-Resolution Relaxometry for Fragment Screening.Journal of medicinal chemistry · 2026Article
- Structure of Vibrio collagenase VhaC provides insight into the mechanism of bacterial collagenolysis.Nature communications · 2022Article
- Effects of the Nature of the Metal Ion, Protein and Substrate on the Catalytic Center in Matrix Metalloproteinase-1: Insights from Multilevel MD, QM/MM and QM Studies.Chemphyschem : a European journal of chemical physics and physical chemistry · 2021Article
- Role of HSP90 in Cancer.International journal of molecular sciences · 2021Review
- Allosteric Communications between Domains Modulate the Activity of Matrix Metalloprotease-1.Biophysical journal · 2020Article
- Integrative Approaches in Structural Biology: A More Complete Picture from the Combination of Individual Techniques.Biomolecules · 2019Review
- Matrix metalloproteinase collagenolysis in health and disease.Biochimica et biophysica acta. Molecular cell research · 2017Review
- Regulation of HuR structure and function by dihydrotanshinone-I.Nucleic acids research · 2017Article
- Effects of Mutations on Structure-Function Relationships of Matrix Metalloproteinase-1.International journal of molecular sciences · 2016Article
- Bilayer Membrane Modulation of Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) Structure and Proteolytic Activity.Scientific reports · 2016Article
- Functional dynamics in replication protein A DNA binding and protein recruitment domains.Structure (London, England : 1993) · 2015Article
- Matrix metalloproteinases as breast cancer drivers and therapeutic targets.Frontiers in bioscience (Landmark edition) · 2015Review
- The dynamic duo: combining NMR and small angle scattering in structural biology.Protein science : a publication of the Protein Society · 2014Review
- Simultaneous use of solution NMR and X-ray data in REFMAC5 for joint refinement/detection of structural differences.Acta crystallographica. Section D, Biological crystallography · 2014Article
- The role of collagen charge clusters in the modulation of matrix metalloproteinase activity.The Journal of biological chemistry · 2014Article
- Biophysical studies of matrix metalloproteinase/triple-helix complexes.Advances in protein chemistry and structural biology · 2014Review
- Crystal structure of full-length human collagenase 3 (MMP-13) with peptides in the active site defines exosites in the catalytic domain.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013Article
- Examination of matrix metalloproteinase-1 in solution: a preference for the pre-collagenolysis state.The Journal of biological chemistry · 2013Article
- Interstitial collagen catabolism.The Journal of biological chemistry · 2013Review
- MaxOcc: a web portal for maximum occurrence analysis.Journal of biomolecular NMR · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The presence of extensive reciprocal conformational freedom between the catalytic and the hemopexin-like domains of full-length matrix metalloproteinase-1 (MMP-1) is demonstrated by NMR and small angle x-ray scattering experiments. This finding is discussed in relation to the essentiality of the hemopexin-like domain for the collagenolytic activity of MMP-1. The conformational freedom experienced by the present system, having the shortest linker between the two domains, when compared with similar findings on MMP-12 and MMP-9 having longer and the longest linker within the family, respectively, suggests this type of conformational freedom to be a general property of all MMPs.
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.