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Institution

University of Marburg

EducationMarburg, Germany
About: University of Marburg is a education organization based out in Marburg, Germany. It is known for research contribution in the topics: Population & Gene. The organization has 23195 authors who have published 42907 publications receiving 1506069 citations. The organization is also known as: Philipps University of Marburg & Philipps-Universität.
Topics: Population, Gene, Crystal structure, Laser, Catalysis


Papers
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Journal ArticleDOI
TL;DR: The present findings would support a recently proposed hypothesis that the 110-kD protein (which displays properties of an actin-activated, myosin-like ATPase) might also be involved in the transport of vesicles through the terminal web.
Abstract: In the present study we have used immunogold labeling of ultrathin sections of the intact chicken and human intestinal epithelium to obtain further insight into the molecular structure of the brush-border cytoskeleton. Actin, villin, and fimbrin were found within the entire microvillus filament bundle, from the tip to the basal end of the rootlets, but were virtually absent from the space between the rootlets. This suggests that the bulk of actin in the brush border is kept in a polymerized and cross-linked state and that horizontally deployed actin filaments are virtually absent. About 70% of the label specific for the 110-kD protein that links the microvillus core bundle to the lipid bilayer was found overlying the microvilli. The remaining label was associated with rootlets and the interrootlet space, where some label was regularly observed in association with vesicles. Since the terminal web did not contain any significant amounts of tubulin and microtubules, the present findings would support a recently proposed hypothesis that the 110-kD protein (which displays properties of an actin-activated, myosin-like ATPase) might also be involved in the transport of vesicles through the terminal web. Label specific for myosin and alpha-actinin was confined to the interrootlet space and was absent from the rootlets. About 10-15% of the myosin label and 70-80% of the alpha-actinin label was observed within the circumferential band of actin filaments at the zonula adherens, where myosin and alpha-actinin displayed a clustered, interrupted pattern that resembles the spacing of these proteins observed in other contractile systems. This circular filament ring did not contain villin, fimbrin, or the 110-kD protein. Finally, actin-specific label was observed in close association with the cytoplasmic aspect of the zonula occludens, suggesting that tight junctions are structurally connected to the microfilament system.

236 citations

Journal ArticleDOI
TL;DR: The essential character of Fe/S clusters in Rli1p explains the indispensable character of mitochondria in eukaryotes and is associated with ribosomes and with Hcr1p, a protein involved in rRNA processing and translation initiation.
Abstract: Mitochondria perform a central function in the biogenesis of cellular iron–sulphur (Fe/S) proteins. It is unknown to date why this biosynthetic pathway is indispensable for life, the more so as no essential mitochondrial Fe/S proteins are known. Here, we show that the soluble ATP-binding cassette (ABC) protein Rli1p carries N-terminal Fe/S clusters that require the mitochondrial and cytosolic Fe/S protein biogenesis machineries for assembly. Mutations in critical cysteine residues of Rli1p abolish association with Fe/S clusters and lead to loss of cell viability. Hence, the essential character of Fe/S clusters in Rli1p explains the indispensable character of mitochondria in eukaryotes. We further report that Rli1p is associated with ribosomes and with Hcr1p, a protein involved in rRNA processing and translation initiation. Depletion of Rli1p causes a nuclear export defect of the small and large ribosomal subunits and subsequently a translational arrest. Thus, ribosome biogenesis and function are intimately linked to the crucial role of mitochondria in the maturation of the essential Fe/S protein Rli1p.

236 citations

Journal ArticleDOI
TL;DR: In agreement with its known aerobic function, no obvious oxygen- or nitrate-dependent pta regulation was observed and a model for the regulation of the anaerobic fermentation genes in B. subtilis is proposed.
Abstract: Bacillus subtilis grows in the absence of oxygen using nitrate ammonification and various fermentation processes. Lactate, acetate, and 2,3-butanediol were identified in the growth medium as the major anaerobic fermentation products by using high-performance liquid chromatography. Lactate formation was found to be dependent on the lctEP locus, encoding lactate dehydrogenase and a putative lactate permease. Mutation of lctE results in drastically reduced anaerobic growth independent of the presence of alternative electron acceptors, indicating the importance of NADH reoxidation by lactate dehydrogenase for the overall anaerobic energy metabolism. Anaerobic formation of 2,3-butanediol via acetoin involves acetolactate synthase and decarboxylase encoded by the alsSD operon. Mutation of alsSD has no significant effect on anaerobic growth. Anaerobic acetate synthesis from acetyl coenzyme A requires phosphotransacetylase encoded by pta. Similar to the case for lctEP, mutation of pta significantly reduces anaerobic fermentative and respiratory growth. The expression of both lctEP and alsSD is strongly induced under anaerobic conditions. Anaerobic lctEP and alsSD induction was found to be partially dependent on the gene encoding the redox regulator Fnr. The observed fnr dependence might be the result of Fnr-induced arfM (ywiD) transcription and subsequent lctEP and alsSD activation by the regulator ArfM (YwiD). The two-component regulatory system encoded by resDE is also involved in anaerobic lctEP induction. No direct resDE influence on the redox regulation of alsSD was observed. The alternative electron acceptor nitrate represses anaerobic lctEP and alsSD transcription. Nitrate repression requires resDE- and fnr-dependent expression of narGHJI, encoding respiratory nitrate reductase. The gene alsR, encoding a regulator potentially responding to changes of the intracellular pH and to acetate, is essential for anaerobic lctEP and alsSD expression. In agreement with its known aerobic function, no obvious oxygen- or nitrate-dependent pta regulation was observed. A model for the regulation of the anaerobic fermentation genes in B. subtilis is proposed.

236 citations

Journal Article
TL;DR: The primary structure of this novel MBL-associated plasma protein of 19 kDa is presented, and it is demonstrated that MAp19 and MASP-2 are encoded by two different mRNA species generated by alternative splicing/polyadenylation from one structural gene.
Abstract: Mannan-binding lectin (MBL) forms a multimolecular complex with at least two MBL-associated serine proteases, MASP-1 and MASP-2. This complex initiates the MBL pathway of complement activation by binding to carbohydrate structures present on bacteria, yeast, and viruses. MASP-1 and MASP-2 are composed of modular structural motifs similar to those of the C1q-associated serine proteases C1r and C1s. Another protein of 19 kDa with the same N-terminal sequence as the 76-kDa MASP-2 protein is consistently detected as part of the MBL/MASP complex. In this study, we present the primary structure of this novel MBL-associated plasma protein of 19 kDa, MAp19, and demonstrate that MAp19 and MASP-2 are encoded by two different mRNA species generated by alternative splicing/polyadenylation from one structural gene.

236 citations

Journal ArticleDOI
TL;DR: In this paper, the psychometric properties of a self-report inventory for measuring individual differences in four components of justice sensitivity (JS): victim sensitivity, observer sensitivity, beneficiary sensitivity, and perpetrator sensitivity were investigated.
Abstract: This article investigates the psychometric properties of a self-report inventory for measuring individual differences in four components of justice sensitivity (JS): victim sensitivity, observer sensitivity, beneficiary sensitivity, and perpetrator sensitivity. A representative sample (N = 2510) was employed to (a) estimate the reliability of a newly developed perpetrator sensitivity scale, (b) test the factorial validity of this scale together with three previously developed scales (victim, observer, and beneficiary sensitivity), (c) estimate correlations between JS and demographic variables (gender, age, education, employment status, marital status, and residency in East versus West Germany), and (d) provide normative data for the computation of standard scores. A demographically heterogeneous convenience sample (N = 327) was used to locate the JS dimensions in the personality space of narrow facet factors. Results from confirmatory factor analyses demonstrated the factorial validity of the JS scales. Regression analyses with JS scales as criteria and personality facet scales as predictors suggested that JS cannot be reduced to combinations of personality facets. Demographic effects were small, explaining a maximum of 1.4% of JS variance. Women and East Germans were found to be more justice sensitive than men and West Germans, respectively. Victim sensitivity decreased with age; perpetrator sensitivity decreased with education. Taken together, our results corroborate the validity of the JS Inventory and contribute to a better psychological understanding of JS.

236 citations


Authors

Showing all 23488 results

NameH-indexPapersCitations
John C. Morris1831441168413
Russel J. Reiter1691646121010
Martin J. Blaser147820104104
Christopher T. Walsh13981974314
Markus Cristinziani131114084538
James C. Paulson12644352152
Markus F. Neurath12493462376
Nicholas W. Wood12361466270
Florian Lang116142166496
Howard I. Maibach116182160765
Thomas G. Ksiazek11339846108
Frank Glorius11366349305
Eberhard Ritz111110961530
Manfred T. Reetz11095942941
Wolfgang H. Oertel11065351147
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
2023142
2022412
20212,104
20201,918
20191,749
20181,592