0000000000435293

AUTHOR

Carlo Schmitz

showing 4 related works from this author

The C-terminal region of human plasma fetuin-B is dispensable for the raised-elephant-trunk mechanism of inhibition of astacin metallopeptidases

2019

© The Author(s) 2019.

0301 basic medicineProteasesProtein Conformationlcsh:MedicineAstacoideaCrystallography X-RayCleavage (embryo)Protein Structure SecondaryArticleMice03 medical and health sciencesScissile bondHydrolaseAnimalsHumansAmino Acid Sequencelcsh:ScienceProtein secondary structureX-ray crystallographyBinding SitesMultidisciplinary030102 biochemistry & molecular biologyChemistrylcsh:RMetalloendopeptidasesProteasesFetuinFetuin-BCell biologyZincFertility030104 developmental biologyProteolysisMetalloproteaseslcsh:QAstacinLinkerScientific Reports
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The E-modulus of the oocyte is a non-destructive measure of zona pellucida hardening

2021

Reproduction 162(4), 259-266 (2021). doi:10.1530/REP-21-0122

Maleendocrine systemEmbryologyZonaModulusCleavage (embryo)Zona Pellucida GlycoproteinsMiceEndocrinologyHuman fertilizationmedicineAnimalsZona pellucidaElastic modulusZona Pellucidareproductive and urinary physiologybiologyurogenital systemChemistryResearchObstetrics and GynecologyCell Biologybiology.organism_classificationOocyteSpermatozoaSpermFetuin-Bmedicine.anatomical_structureReproductive Medicineembryonic structuresOocytesBiophysicsFemaleReproduction
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Mammalian plasma fetuin-B is a selective inhibitor of ovastacin and meprin metalloproteinases

2019

AbstractVertebrate fetuins are multi-domain plasma-proteins of the cystatin-superfamily. Human fetuin-A is also known as AHSG, α2-Heremans-Schmid-glycoprotein. Gene-knockout in mice identified fetuin-A as essential for calcified-matrix-metabolism and bone-mineralization. Fetuin-B deficient mice, on the other hand, are female infertile due to zona pellucida ‘hardening’ caused by the metalloproteinase ovastacin in unfertilized oocytes. In wildtype mice fetuin-B inhibits the activity of ovastacin thus maintaining oocytes fertilizable. Here we asked, if fetuins affect further proteases as might be expected from their evolutionary relation to single-domain-cystatins, known as proteinase-inhibito…

0301 basic medicineProteasesGlycosylationalpha-2-HS-Glycoproteinmedicine.medical_treatmentProteolysislcsh:MedicineAstacoideaMatrix metalloproteinaseArticle03 medical and health sciencesMicePlasma0302 clinical medicinemedicineAnimalsHumansFibrinolysinZona pellucidalcsh:ScienceMammalsMetalloproteinaseMultidisciplinaryProteasemedicine.diagnostic_testChemistrylcsh:RWild typeMetalloendopeptidasesFetuinFetuin-BRecombinant ProteinsCell biology030104 developmental biologymedicine.anatomical_structureMatrix Metalloproteinase 9FertilizationProteolysisMetalloproteasesCattlelcsh:Q030217 neurology & neurosurgery
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Structure of mammalian plasma fetuin-B and its mechanism of selective metallopeptidase inhibition

2018

The co-crystal structure of the metallopeptidase astacin with its specific protein inhibitor fetuin-B reveals a novel mechanism of inhibition.

Crystallographymammalian fertilizationmetallopeptidaseResearch Papersstructure determination570 Life sciencesenzyme mechanismsprotein inhibitorQD901-999multi-protein complexessperm–egg fusionpolyspermyprotein structureX-ray crystallography570 Biowissenschaften
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