F
Friedrich Lottspeich
Researcher at Max Planck Society
Publications - 449
Citations - 31053
Friedrich Lottspeich is an academic researcher from Max Planck Society. The author has contributed to research in topics: Peptide sequence & Amino acid. The author has an hindex of 94, co-authored 449 publications receiving 30250 citations. Previous affiliations of Friedrich Lottspeich include Technische Universität Darmstadt & University of Marburg.
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Journal ArticleDOI
Covalent Structure of Fibrinogen
TL;DR: In genetically determined abnormal fibrinogens the correlation between the structural error and the dysfunction of the molecule may reveal the functional importance of single amino acid residues.
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The 'light' and 'medium' subunits of the photosynthetic reaction centre from Rhodopseudomonas viridis: isolation of the genes, nucleotide and amino acid sequence.
Hartmut Michel,Karl Aloys Weyer,H. Gruenberg,I. Dunger,Dieter Oesterhelt,Friedrich Lottspeich +5 more
TL;DR: The ‘light’ and the ‘medium’ subunits of the photosynthetic reaction centre from Rhodopseudomonas viridis were isolated and their amino‐terminal sequences, as well as the sequences of several chymotryptic peptides, determined.
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Archaebacterial DNA-dependent RNA polymerases testify to the evolution of the eukaryotic nuclear genome
Gabriela Pühler,Henrik Leffers,Felix Gropp,Peter Palm,Hans-Peter Klenk,Friedrich Lottspeich,Roger A. Garrett,Wolfram Zillig +7 more
TL;DR: Unrooted phylogenetic dendrograms derived from both distance matrix and parsimony analyses show the archaebacteria are a coherent group closely related to the eukaryotic nuclear RNA polymerase II and/or III lineages.
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Cofactor Requirements for Nuclear Export of Rev Response Element (Rre)–And Constitutive Transport Element (Cte)–Containing Retroviral Rnas An Unexpected Role for Actin
Wilma A. Hofmann,Beate Reichart,Andrea Ewald,Eleonora Müller,Iris Schmitt,Roland H. Stauber,Friedrich Lottspeich,Brigitte M. Jockusch,Ulrich Scheer,Joachim Hauber,Marie-Christine Dabauvalle +10 more
TL;DR: Evidence is provided that actin plays an important functional role in nuclear export not only of retroviral RNAs but also of host proteins such as protein kinase inhibitor (PKI).
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Primary structure of the Thermoplasma proteasome and its implications for the structure, function, and evolution of the multicatalytic proteinase.
TL;DR: It is suggested that the alpha-subunits have regulatory and targeting functions, while the beta-subunit carry the active sites in the archaebacterial proteasome.