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Brigitte Wittmann-Liebold
Researcher at Max Planck Society
Publications - 192
Citations - 8881
Brigitte Wittmann-Liebold is an academic researcher from Max Planck Society. The author has contributed to research in topics: Ribosomal protein & Ribosome. The author has an hindex of 49, co-authored 192 publications receiving 8779 citations. Previous affiliations of Brigitte Wittmann-Liebold include Max Delbrück Center for Molecular Medicine & Russian Academy of Sciences.
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Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins.
TL;DR: The results indicate that this enzyme is probably identical to cyclophilin, a recently discovered mammalian protein which binds tightly to cyclosporin A (CsA), which is thought to be linked to the immunosuppressive action of CsA.
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Micro-sequence analysis of peptides and proteins using 4-NN-dimethylaminoazobenzene 4′-isothiocyanate/phenylisothiocyanate double coupling method
TL;DR: The pheny~sot~ocyanate (Edman) degradation has been a most valuable technique in amino acid sequence determination and contributed, to a great extent, to the sequence analysis of proteins which are available in only limited quantities.
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Complete nucleotide sequence and gene organization of the broad-host-range plasmid RSF1010
Peter Scholz,Volker Haring,Brigitte Wittmann-Liebold,Keith Ashman,Michael Bagdasarian,Eberhard Scherzinger +5 more
TL;DR: Analysis of the distribution of translation start and stop codons in the RSF1010 sequence has revealed the existence of more than 40 open reading frames potentially capable of encoding polypeptides of 60 or more amino acids.
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Two-dimensional gel electrophoresis as tool for proteomics studies in combination with protein identification by mass spectrometry.
TL;DR: Advances in proteomics have been possible through the development of advanced high‐resolution 2‐DE systems allowing resolution of up to 10 000 protein spots of entire cell lysates in combination with protein identification by new highly sensitive mass spectrometric techniques.
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The Primary Structure of an Acidic Protein from 50-S Ribosomes of Escherichia coli which is Involved in GTP Hydrolysis Dependent on Elongation Factors G and T
TL;DR: The distinctive clustering of hydrophobic and charged residues is quite remarkable and suggests that in situ certain of these regions may contain a binding site for components involved in peptide chain elongation.