Institution
Bielefeld University
Education•Bielefeld, Nordrhein-Westfalen, Germany•
About: Bielefeld University is a education organization based out in Bielefeld, Nordrhein-Westfalen, Germany. It is known for research contribution in the topics: Population & Quantum chromodynamics. The organization has 10123 authors who have published 26576 publications receiving 728250 citations. The organization is also known as: University of Bielefeld & UNIVERSITAET BIELEFELD.
Topics: Population, Quantum chromodynamics, Gene, Context (language use), Quark
Papers published on a yearly basis
Papers
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TL;DR: In this article, the complete matrix elements for all final states were reduced to a few compact generic functions in the Electroweak Standard Model for polarized massless fermions. But their results are limited to the case where the fermion mass obeys all Ward identities.
338 citations
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TL;DR: It is suggested the establishment of a home care-dominated geriatric care system, and a proactive role for researchers on aging in reforming geriatric Care through policy dialogs, and the creation of a nurturing environment conducive to healthy aging in China.
338 citations
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TL;DR: The article surveys the current literature and attempts a mostly comprehensive coverage of present day knowledge and concepts on Prx mechanism, regulation, and function and thus on the whole Prx systems in plants.
Abstract: Peroxiredoxins (Prx) are central elements of the antioxidant defense system and the dithiol-disulfide redox regulatory network of the plant and cyanobacterial cell. They employ a thiol-based catalytic mechanism to reduce H2O2, alkylhydroperoxide, and peroxinitrite. In plants and cyanobacteria, there exist 2-CysPrx, 1-CysPrx, PrxQ, and type II Prx. Higher plants typically contain at least one plastid 2-CysPrx, one nucleo-cytoplasmic 1-CysPrx, one chloroplast PrxQ, and one each of cytosolic, mitochondrial, and plastidic type II Prx. Cyanobacteria express variable sets of three or more Prxs. The catalytic cycle consists of three steps: (i) peroxidative reduction, (ii) resolving step, and (iii) regeneration using diverse electron donors such as thioredoxins, glutaredoxins, cyclophilins, glutathione, and ascorbic acid. Prx proteins undergo major conformational changes in dependence of their redox state. Thus, they not only modulate cellular reactive oxygen species- and reactive nitrogen species-dependent signaling, but depending on the Prx type they sense the redox state, transmit redox information to binding partners, and function as chaperone. They serve in context of photosynthesis and respiration, but also in metabolism and development of all tissues, for example, in nodules as well as during seed and fruit development. The article surveys the current literature and attempts a mostly comprehensive coverage of present day knowledge and concepts on Prx mechanism, regulation, and function and thus on the whole Prx systems in plants.
337 citations
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TL;DR: The purification of a specific PSI–IsiA supercomplex is reported, which is abundant under conditions of iron limitation and provides a structural characterization of an additional chlorophyll-containing, membrane-integral antenna in a cyanobacterial photosystem.
Abstract: Cyanobacteria are abundant throughout most of the world's water bodies and contribute significantly to global primary productivity through oxygenic photosynthesis. This reaction is catalysed by two membrane-bound protein complexes, photosystem I (PSI) and photosystem II (PSII), which both contain chlorophyll-binding subunits functioning as an internal antenna1. In addition, phycobilisomes act as peripheral antenna systems, but no additional light-harvesting systems have been found under normal growth conditions. Iron deficiency, which is often the limiting factor for cyanobacterial growth in aquatic ecosystems2, leads to the induction of additional proteins such as IsiA (ref. 3). Although IsiA has been implicated in chlorophyll storage, energy absorption and protection against excessive light, its precise molecular function and association to other proteins is unknown. Here we report the purification of a specific PSI–IsiA supercomplex, which is abundant under conditions of iron limitation. Electron microscopy shows that this supercomplex consists of trimeric PSI surrounded by a closed ring of 18 IsiA proteins binding around 180 chlorophyll molecules. We provide a structural characterization of an additional chlorophyll-containing, membrane-integral antenna in a cyanobacterial photosystem.
336 citations
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Uppsala University1, University of Warsaw2, Bielefeld University3, CERN4, Max Planck Society5, Paul Scherrer Institute6, University of Padua7, University of Neuchâtel8, University of Freiburg9, University of Geneva10, Yale University11, University of Mainz12, University of California, Santa Cruz13, University of Bonn14, Istituto Superiore di Sanità15, Osaka University16, Heidelberg University17, Stockholm University18, University of Erlangen-Nuremberg19, University of Mons20, Dresden University of Technology21, European Synchrotron Radiation Facility22, Warsaw University of Technology23
TL;DR: In this article, the muon-proton and muon deuteron inclusive deep inelastic scattering cross sections were measured in the kinematic range 0.002 < x < 0.60 and 0.5 < Q(2) < 75 GeV2 at incident muon energies of 90, 120, 200 and 280 GeV.
334 citations
Authors
Showing all 10375 results
Name | H-index | Papers | Citations |
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Stefan Grimme | 113 | 680 | 105087 |
Alfred Pühler | 102 | 658 | 45871 |
James Barber | 102 | 642 | 42397 |
Swagata Mukherjee | 101 | 1048 | 46234 |
Hans-Joachim Werner | 98 | 317 | 48508 |
Krzysztof Redlich | 98 | 609 | 32693 |
Graham C. Walker | 93 | 381 | 36875 |
Christian Meyer | 93 | 1081 | 38149 |
Muhammad Farooq | 92 | 1341 | 37533 |
Jean Willy Andre Cleymans | 90 | 542 | 27685 |
Bernhard T. Baune | 90 | 608 | 50706 |
Martin Wikelski | 89 | 420 | 25821 |
Niklas Luhmann | 85 | 421 | 42743 |
Achim Müller | 85 | 926 | 35874 |
Oliver T. Wolf | 83 | 337 | 24211 |