We are analyzing https://link.springer.com/article/10.1186/gb-2011-12-11-233.

Title:
Tissue inhibitors of metalloproteinases | Genome Biology
Description:
Orchestration of the growth and remodeling of tissues and responses of cells to their extracellular environment is mediated by metalloproteinases of the Metzincin clan. This group of proteins comprises several families of endopeptidases in which a zinc atom is liganded at the catalytic site to three histidine residues and an invariant methionine residue. Tissue inhibitors of metalloproteinases (TIMPs) are endogenous protein regulators of the matrix metalloproteinase (MMPs) family, and also of families such as the disintegrin metalloproteinases (ADAM and ADAMTS). TIMPs therefore have a pivotal role in determining the influence of the extracellular matrix, of cell adhesion molecules, and of many cytokines, chemokines and growth factors on cell phenotype. The TIMP family is an ancient one, with a single representative in lower eukaryotes and four members in mammals. Although much is known about their mechanism of action in proteinase regulation in mammalian cells, less is known about their functions in lower organisms. Recently, non-inhibitory functions of TIMPs have been identified in mammalian cells, including signaling roles downstream of specific receptors. There are clearly still questions to be answered with regard to their overall roles in biology.
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Keywords {🔍}

timp, timps, pubmed, metalloproteinases, article, google, scholar, cas, tissue, inhibitor, cell, human, gene, inhibitors, metalloproteinase, mmp, adam, domain, proteins, matrix, adamts, figure, murphy, mmps, activities, family, genes, site, research, protein, tissues, cells, extracellular, activity, central, growth, role, signaling, studies, expression, function, regulation, functions, inhibition, shown, sites, transcription, biol, nagase, authors,

Topics {✒️}

promoter-proximal gc-rich region transcription factors nf-κb carboxy-terminal hemopexin domain full size image transcription start points springer science+business media spatio-temporal expression patterns anti-parallel β strands ldl-receptor-related protein timp-3-deficient mammary gland nf-il6 binding sites central nervous system stetler-stevenson skeletal muscle-specific expression mmp catalytic cleft specific cell-binding partners transcription factor sp1 active-site cleft timps show tissue-specific arthritis research uk cancer research uk medical research council amino-terminal inhibitory domain privacy choices/manage cookies bmc evol biol authors’ original file leco kj erythroid-potentiating activity procollagen n-proteinase adamts-2 synapsin gene family catalytic cleft timp proteins share hemopexin domain myogenin-binding site parallel β strands anti-apoptotic effects mmp-independent timp regulation mediate serum induction cell-binding partners [7] single-domain proteins independent prognostic factor related subjects human synapsin genes phylogenetic analysis shows human timp2 gene twisted β barrel biochim biophys acta timp3-null mice suggests multiple sites beta strands arranged

Questions {❓}

Rivera S, Khrestchatisky M, Kaczmarek L, Rosenberg GA, Jaworski DM: Metzincin proteases and their inhibitors: foes or friends in nervous system physiology?

Schema {🗺️}

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         headline:Tissue inhibitors of metalloproteinases
         description:Orchestration of the growth and remodeling of tissues and responses of cells to their extracellular environment is mediated by metalloproteinases of the Metzincin clan. This group of proteins comprises several families of endopeptidases in which a zinc atom is liganded at the catalytic site to three histidine residues and an invariant methionine residue. Tissue inhibitors of metalloproteinases (TIMPs) are endogenous protein regulators of the matrix metalloproteinase (MMPs) family, and also of families such as the disintegrin metalloproteinases (ADAM and ADAMTS). TIMPs therefore have a pivotal role in determining the influence of the extracellular matrix, of cell adhesion molecules, and of many cytokines, chemokines and growth factors on cell phenotype. The TIMP family is an ancient one, with a single representative in lower eukaryotes and four members in mammals. Although much is known about their mechanism of action in proteinase regulation in mammalian cells, less is known about their functions in lower organisms. Recently, non-inhibitory functions of TIMPs have been identified in mammalian cells, including signaling roles downstream of specific receptors. There are clearly still questions to be answered with regard to their overall roles in biology.
         datePublished:2011-11-11T00:00:00Z
         dateModified:2011-11-11T00:00:00Z
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            Animal Genetics and Genomics
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            Plant Genetics and Genomics
            Microbial Genetics and Genomics
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      headline:Tissue inhibitors of metalloproteinases
      description:Orchestration of the growth and remodeling of tissues and responses of cells to their extracellular environment is mediated by metalloproteinases of the Metzincin clan. This group of proteins comprises several families of endopeptidases in which a zinc atom is liganded at the catalytic site to three histidine residues and an invariant methionine residue. Tissue inhibitors of metalloproteinases (TIMPs) are endogenous protein regulators of the matrix metalloproteinase (MMPs) family, and also of families such as the disintegrin metalloproteinases (ADAM and ADAMTS). TIMPs therefore have a pivotal role in determining the influence of the extracellular matrix, of cell adhesion molecules, and of many cytokines, chemokines and growth factors on cell phenotype. The TIMP family is an ancient one, with a single representative in lower eukaryotes and four members in mammals. Although much is known about their mechanism of action in proteinase regulation in mammalian cells, less is known about their functions in lower organisms. Recently, non-inhibitory functions of TIMPs have been identified in mammalian cells, including signaling roles downstream of specific receptors. There are clearly still questions to be answered with regard to their overall roles in biology.
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      dateModified:2011-11-11T00:00:00Z
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         TIMP Gene
         Catalytic Cleft
         Human TIMPs
         Hemopexin Domain
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         Animal Genetics and Genomics
         Human Genetics
         Plant Genetics and Genomics
         Microbial Genetics and Genomics
         Bioinformatics
         Evolutionary Biology
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         name:BioMed Central
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            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
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            affiliation:
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