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Tammo Diercks

Bio: Tammo Diercks is an academic researcher from Technische Universität München. The author has contributed to research in topics: Nuclear magnetic resonance spectroscopy & Glycan. The author has an hindex of 20, co-authored 50 publications receiving 1211 citations.


Papers
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Journal ArticleDOI
TL;DR: Its unmatched screening sensitivity, combined with the abundance of available information on the structure and nature of molecular binding, justifies the growing interest in this dynamically expanding NMR application.

122 citations

Journal ArticleDOI
TL;DR: The structure provides a detailed model of the ligand-binding site and has led to the proposal of a site for pro-MMP-9 association, which has allowed us to investigate a mechanism by which a cell-surface receptor might distinguish between apo and holo-HNGAL through conformational changes at the open end of the barrel.

99 citations

Journal ArticleDOI
TL;DR: The results suggest that VAT-N is a precursor of the aspartic proteinases that has acquired peptide-binding activity while remaining proteolytically incompetent.

92 citations

Journal ArticleDOI
TL;DR: Two 3D-NOESY spectra are reported which, in concert with other commonly used spectra, provide a convenient strategy for NOE assignment and exploit the extra dispersion of the heteronucleus and considerably simplifying assignment.
Abstract: The question is addressed of how maximal structural NOE data on double labelled proteins can be acquired with a minimal set of NOESY experiments. Two 3D-NOESY spectra are reported which, in concert with other commonly used spectra, provide a convenient strategy for NOE assignment. The 3D CNH-NOESY and 3D NCH-NOESY provide NOE connectivities between amide protons and carbon-bound protons and constitute orthogonal heteronuclear filters which eliminate diagonal signals, considerably improving spectral quality. Two different heteronuclear chemical shift dimensions are recorded in the spectra, thus exploiting the extra dispersion of the heteronucleus and considerably simplifying assignment.

87 citations


Cited by
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Journal Article
TL;DR: This volume is keyed to high resolution electron microscopy, which is a sophisticated form of structural analysis, but really morphology in a modern guise, the physical and mechanical background of the instrument and its ancillary tools are simply and well presented.
Abstract: I read this book the same weekend that the Packers took on the Rams, and the experience of the latter event, obviously, colored my judgment. Although I abhor anything that smacks of being a handbook (like, \"How to Earn a Merit Badge in Neurosurgery\") because too many volumes in biomedical science already evince a boyscout-like approach, I must confess that parts of this volume are fast, scholarly, and significant, with certain reservations. I like parts of this well-illustrated book because Dr. Sj6strand, without so stating, develops certain subjects on technique in relation to the acquisition of judgment and sophistication. And this is important! So, given that the author (like all of us) is somewhat deficient in some areas, and biased in others, the book is still valuable if the uninitiated reader swallows it in a general fashion, realizing full well that what will be required from the reader is a modulation to fit his vision, propreception, adaptation and response, and the kind of problem he is undertaking. A major deficiency of this book is revealed by comparison of its use of physics and of chemistry to provide understanding and background for the application of high resolution electron microscopy to problems in biology. Since the volume is keyed to high resolution electron microscopy, which is a sophisticated form of structural analysis, but really morphology in a modern guise, the physical and mechanical background of The instrument and its ancillary tools are simply and well presented. The potential use of chemical or cytochemical information as it relates to biological fine structure , however, is quite deficient. I wonder when even sophisticated morphol-ogists will consider fixation a reaction and not a technique; only then will the fundamentals become self-evident and predictable and this sine qua flon will become less mystical. Staining reactions (the most inadequate chapter) ought to be something more than a technique to selectively enhance contrast of morphological elements; it ought to give the structural addresses of some of the chemical residents of cell components. Is it pertinent that auto-radiography gets singled out for more complete coverage than other significant aspects of cytochemistry by a high resolution microscopist, when it has a built-in minimal error of 1,000 A in standard practice? I don't mean to blind-side (in strict football terminology) Dr. Sj6strand's efforts for what is \"routinely used in our laboratory\"; what is done is usually well done. It's just that …

3,197 citations

Journal ArticleDOI
14 Sep 2006-Nature
TL;DR: The observed, outward-facing conformation reflects the ATP-bound state, with the two nucleotide-binding domains in close contact and the two transmembrane domains forming a central cavity—presumably the drug translocation pathway—that is shielded from the inner leaflet of the lipid bilayer and from the cytoplasm, but exposed to the outer leaflet and the extracellular space.
Abstract: Multidrug transporters of the ABC family facilitate the export of diverse cytotoxic drugs across cell membranes. This is clinically relevant, as tumour cells may become resistant to agents used in chemotherapy. To understand the molecular basis of this process, we have determined the 3.0 A crystal structure of a bacterial ABC transporter (Sav1866) from Staphylococcus aureus. The homodimeric protein consists of 12 transmembrane helices in an arrangement that is consistent with cross-linking studies and electron microscopic imaging of the human multidrug resistance protein MDR1, but critically different from that reported for the bacterial lipid flippase MsbA. The observed, outward-facing conformation reflects the ATP-bound state, with the two nucleotide-binding domains in close contact and the two transmembrane domains forming a central cavity—presumably the drug translocation pathway—that is shielded from the inner leaflet of the lipid bilayer and from the cytoplasm, but exposed to the outer leaflet and the extracellular space. Multidrug efflux transporters cause serious problems in cancer chemotherapy and in the treatment of bacterial infections. A puzzling aspect of their biology is how a single transporter can recognize and transport such a wide variety of structurally dissimilar compounds. The publication of the crystal structures of two quite different multidrug efflux transporters will help to solve the mystery. In the first study, the structure of AcrB — a multidrug efflux transporter from E. coli — was determined. Its three constituent subunits were captured at different steps in the transport cycle: prior to substrate binding, substrate-bound, and post-extrusion. The voluminous multidrug binding pocket handles multiple substrates via multi-site binding. The second study determined the structure of an ATP-driven multidrug transporter from S. aureus. The clinical relevance of this 'ABC' family of transporters derives from the fact that they catalyse the extrusion of various cytotoxic compounds used in cancer therapy. The structure, with the transporter in the outward-facing conformation, is a useful model of human homologues and may initiate the rational design of drugs aimed at interfering with the extrusion of agents used in chemotherapy.

1,244 citations

Journal ArticleDOI
TL;DR: It is proposed that NGAL participates in the antibacterial iron depletion strategy of the innate immune system by tightly binds bacterial catecholate-type ferric siderophores through a cyclically permuted, hybrid electrostatic/cation-pi interaction and is a potent bacteriostatic agent in iron-limiting conditions.

1,231 citations