0000000001131311

AUTHOR

Arnd Gerhards

showing 2 related works from this author

Diagnostic Performance of Multiparametric Magnetic Resonance Imaging and Fusion Targeted Biopsy to Detect Significant Prostate Cancer

2017

Background/aim Multiparametric magnetic resonance imaging combined with ultrasound-fusion-targeted biopsy of the prostate intends to increase diagnostic precision, which has to be clarified. Patients and methods We performed multiparametric magnetic resonance imaging followed by ultrasound-fusion-guided perineal biopsy in 99 male patients with elevated prostate-specific-antigen and previous negative standard biopsy-procedures. Results In 33/99 patients (33%) no malignancy could be confirmed by histopathology. Low-grade carcinomas (Gleason-Score 6+7a) were found in 42/66 (64%) and high-grade carcinomas (Gleason-Score ≥7b) in 24/66 (36%) men. A high-grade carcinoma corresponded to PI-RADS 4 o…

Image-Guided BiopsyMaleCancer Researchmedicine.medical_specialty030232 urology & nephrologyMalignancySensitivity and Specificity03 medical and health sciencesProstate cancer0302 clinical medicineProstateBiopsymedicineCarcinomaHumansEndoscopic Ultrasound-Guided Fine Needle AspirationMultiparametric Magnetic Resonance ImagingAgedAged 80 and overmedicine.diagnostic_testbusiness.industryProstateProstatic NeoplasmsReproducibility of ResultsMagnetic resonance imagingGeneral MedicineMiddle AgedProstate-Specific Antigenmedicine.diseaseMagnetic Resonance Imagingmedicine.anatomical_structureOncology030220 oncology & carcinogenesisHistopathologyRadiologyNeoplasm GradingbusinessAnticancer Research
researchProduct

Interaction ofEscherichia colihemolysin with biological membranes

2001

Escherichia coli hemolysin (HlyA) is a membrane-permeabilizing protein belonging to the family of RTX-toxins. Lytic activity depends on binding of Ca2(+) to the C-terminus of the molecule. The N-terminus of HlyA harbors hydrophobic sequences that are believed to constitute the membrane-inserting domain. In this study, 13 HlyA cysteine-replacement mutants were constructed and labeled with the polarity-sensitive fluorescent probe 6-bromoacetyl-2-dimethylaminonaphthalene (badan). The fluorescence emission of the label was examined in soluble and membrane-bound toxin. Binding effected a major blue shift in the emission of six residues within the N-terminal hydrophobic domain, indicating inserti…

Conformational changeProtein ConformationPlasma protein bindingBiologymedicine.disease_causeHemolysisBiochemistryHemolysin ProteinsProtein structureBacterial Proteins2-NaphthylamineEscherichia colimedicineCysteineCloning MolecularLipid bilayerEscherichia coliFluorescent DyesEscherichia coli ProteinsCell MembraneErythrocyte MembraneBiological membraneProtein Structure TertiarySpectrometry FluorescenceMembraneBiochemistryMutagenesisLiposomesChromatography GelCalciumElectrophoresis Polyacrylamide GelProtein BindingBinding domainEuropean Journal of Biochemistry
researchProduct