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Institution

University of Konstanz

EducationKonstanz, Baden-Württemberg, Germany
About: University of Konstanz is a education organization based out in Konstanz, Baden-Württemberg, Germany. It is known for research contribution in the topics: Population & Membrane. The organization has 12115 authors who have published 27401 publications receiving 951162 citations. The organization is also known as: University of Constance & Universität Konstanz.
Topics: Population, Membrane, Politics, Laser, Gene


Papers
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Journal ArticleDOI
TL;DR: It is shown here that ornithine-δ-aminotransferase (δOAT, At5g46180), the enzyme converting Orn to pyrroline-5-carboxylate (P5C), is localised in mitochondria and is essential for Arg catabolism.
Abstract: Like many other plant species, Arabidopsis uses arginine (Arg) as a storage and transport form of nitrogen, and proline (Pro) as a compatible solute in the defence against abiotic stresses causing water deprivation. Arg catabolism produces ornithine (Orn) inside mitochondria, which was discussed controversially as a precursor for Pro biosynthesis, alternative to glutamate (Glu). We show here that ornithine-δ-aminotransferase (δOAT, At5g46180), the enzyme converting Orn to pyrroline-5-carboxylate (P5C), is localised in mitochondria and is essential for Arg catabolism. Wildtype plants could readily catabolise supplied Arg and Orn and were able to use these amino acids as the only nitrogen source. Deletion mutants of δOAT, however, accumulated urea cycle intermediates when fed with Arg or Orn and were not able to utilize nitrogen provided as Arg or Orn. Utilisation of urea and stress induced Pro accumulation were not affected in T-DNA insertion mutants with a complete loss of δOAT expression. Our findings indicate that δOAT feeds P5C exclusively into the catabolic branch of Pro metabolism, which yields Glu as an end product. Conversion of Orn to Glu is an essential route for recovery of nitrogen stored or transported as Arg. Pro biosynthesis occurs predominantly or exclusively via the Glu pathway in Arabidopsis and does not depend on Glu produced by Arg and Orn catabolism.

181 citations

Journal ArticleDOI
TL;DR: The proteins of the outer membrane from rat liver mitochondria have been subfractionated by means of density gradient centrifugation and it was observed that a polypeptide of Mr 32 000 renders asolectin vesicles permeable to ADP and forms pores in bilayer membrane.

181 citations

Journal ArticleDOI
TL;DR: Sequence analysis of PIG cDNAs revealed similarities to genes encoding proteins involved in amino acid transport, thiamine biosynthesis, short-chain dehydrogenases, metallothioneins, cytochrome P-450 monooxygenases, and peptidyl-prolyl isomerases.
Abstract: Rust fungi are plant parasites that depend on living host tissue for growth. For invasion of leaves, dikaryotic urediospores differentiate germ tubes and infection structures that penetrate through stomata. Biotrophic growth occurs by intercellular mycelia that form haustoria within host cells. A cDNA library was constructed from haustoria isolated from broad bean leaves infected by Uromyces fabae. Differential screening revealed that a high proportion (19%) of the haustorial cDNAs are specifically expressed in planta but are not expressed, or are much weaker, in germlings or infection structures produced in vitro. A total of 31 different in planta-induced genes (PIGs) were identified. Some of the PIGs are highly expressed in haustoria. The PIGs are single or low copy number genes in the rust genome. A variety of developmentally regulated expression patterns of PIG mRNAs were observed. Sequence analysis of PIG cDNAs revealed similarities to genes encoding proteins involved in amino acid transport, thiamine biosynthesis, short-chain dehydrogenases, metallothioneins, cytochrome P-450 monooxygenases, and peptidyl-prolyl isomerases.

181 citations

Journal ArticleDOI
TL;DR: When free radicals cause dissociation of the octamer, VDAC interacts with the ANT with the same results as described above: Bax-dependent cytochrome c release and risk of permeability transition pore opening.
Abstract: The outer mitochondrial membrane pore (VDAC) changes its structure either voltage-dependently in artificial membranes or physiologically by interaction with the adenine nucleotide translocase (ANT) in the c-conformation. This interaction creates contact sites and leads in addition to a specific organisation of cytochrome c in the VDAC-ANT complexes. The VDAC structure that is specific for contact sites generates a signal at the surface for several proteins in the cytosol to bind with high capacity, such as hexokinase, glycerol kinase and Bax. If the VDAC binding site is not occupied by hexokinase, the VDAC-ANT complex has two critical qualities: firstly, Bax gets access to cytochrome c and secondly the ANT is set in its c-conformation that easily changes conformation into an unspecific channel (uniporter) causing permeability transition. Activity of bound hexokinase protects against both, it hinders Bax binding and employs the ANT as anti-porter. The octamer of mitochondrial creatine kinase binds to VDAC from the inner surface of the outer membrane. This firstly restrains interaction between VDAC and ANT and secondly changes the VDAC structure into low affinity for hexokinase and Bax. Cytochrome c in the creatine kinase complex will be differently organised, not accessible to Bax and the ANT is run as anti-porter by the active creatine kinase octamer. However, when, for example, free radicals cause dissociation of the octamer, VDAC interacts with the ANT with the same results as described above: Bax-dependent cytochrome c release and risk of permeability transition pore opening.

180 citations

Journal ArticleDOI
TL;DR: This is the 54th report of a series of workshops organised by the European Centre for the Validation of Alternative Methods, at which selected groups of independent international experts would review the current status of various types of in vitro tests and their potential uses, and make recommendations about the best ways forward.
Abstract: This is the 54th report of a series of workshops organised by the European Centre for the Validation of Alternative Methods (ECVAM). The main objective of ECVAM, as defined in 1993 by its Scientific Advisory Committee, is to promote the scientific and regulatory acceptance of alternative methods which are of importance to the biosciences, and which reduce, refine or replace the use of laboratory animals. One of the first priorities set by ECVAM was the implementation of procedures that would enable it to become well informed about the state-of-the-art of non-animal test development and validation, and of opportunities for the possible incorporation of alternative methods into regulatory procedures. It was decided that this would be best achieved through a programme of ECVAM workshops, each addressing a specific topic, and at which selected groups of independent international experts would review the current status of various types of in vitro tests and their potential uses, and make recommendations about the best ways forward. A workshop on Metabolism: a bottleneck in in vitro toxicological test development, was held at ECVAM on 26–29 January 2004, with participants Metabolism: A Bottleneck in In Vitro Toxicological Test Development

180 citations


Authors

Showing all 12272 results

NameH-indexPapersCitations
Robert E. W. Hancock15277588481
Lloyd J. Old152775101377
Andrew White1491494113874
Stefanie Dimmeler14757481658
Rudolf Amann14345985525
Niels Birbaumer14283577853
Thomas P. Russell141101280055
Emmanuelle Perez138155099016
Shlomo Havlin131101383347
Bruno S. Frey11990065368
Roald Hoffmann11687059470
Michael G. Fehlings116118957003
Yves Van de Peer11549461479
Axel Meyer11251151195
Manuela Campanelli11167548563
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
202360
2022202
20211,361
20201,299
20191,166
20181,082