D
David H. Goetz
Researcher at University of California, San Francisco
Publications - 19
Citations - 3049
David H. Goetz is an academic researcher from University of California, San Francisco. The author has contributed to research in topics: Siderocalin & Urokinase receptor. The author has an hindex of 15, co-authored 19 publications receiving 2809 citations. Previous affiliations of David H. Goetz include University of California & University of California, Berkeley.
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Journal ArticleDOI
The Neutrophil Lipocalin NGAL Is a Bacteriostatic Agent that Interferes with Siderophore-Mediated Iron Acquisition
David H. Goetz,Margaret A. Holmes,Niels Borregaard,Martin E. Bluhm,Kenneth N. Raymond,Roland K. Strong +5 more
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.
Journal ArticleDOI
An iron delivery pathway mediated by a lipocalin
Jun Yang,David H. Goetz,Jau Yi Li,Wenge Wang,Kiyoshi Mori,Daria Setlik,Tonggong Du,Hediye Erdjument-Bromage,Paul Tempst,Roland K. Strong,Jonathan Barasch +10 more
TL;DR: It is shown that a member of the lipocalin superfamily (24p3/Ngal) delivers iron to the cytoplasm where it activates or represses iron-responsive genes and identifies an iron delivery pathway active in development and cell physiology.
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A Mammalian Siderophore Synthesized by an Enzyme with a Bacterial Homolog Involved in Enterobactin Production
TL;DR: The results reveal features of intracellular iron homeostasis that are conserved from bacteria through humans, and find that the murine enzyme responsible for 2,5-DHBA synthesis, BDH2, is the homolog of bacterial EntA, which catalyzes 2,3- DHBA production during enterobactin biosynthesis.
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IAR3 Encodes an Auxin Conjugate Hydrolase from Arabidopsis
TL;DR: The Arabidopsis iar3 mutant that displays reduced sensitivity to IAA–Ala is described, and plants overexpressing IAR3 or ILR1 are more sensitive than is the wild type to certain IAA-amino acid conjugates, reflecting the overlapping substrate specificities of the corresponding enzymes.
Journal ArticleDOI
Ligand preference inferred from the structure of neutrophil gelatinase associated lipocalin
David H. Goetz,Sirkku T. Willie,Roger S. Armen,Tomas Bratt,Niels Borregaard,Roland K. Strong +5 more
TL;DR: The size, shape, and character of the NGAL calyx, as well as the low relative affinity for N-formylated tripeptides, suggest that neither the copurified fatty acid nor any of the proposed ligands are likely to be the preferred ligand of this protein.