About

Douglas Ohlendorf, PhD, is a Professor and Associate Head of Education at the University of Minnesota Medical School. His research interests focus on the structural foundations for biological function, emphasizing the importance of structure in understanding biological processes. His lab believes that a structure is worth a thousand pictures, highlighting the significance of structural analysis in biological research. He is involved in educational leadership within the medical school, contributing to the training and development of students and faculty. His work and leadership support the advancement of biomedical research and education at the university.

Research topics

• Medicine
• Gynecology

Selected publications

• Einfluss der Ergometrie sowie der sportlichen Belastung auf die Konzentration der Blutparameter Kreatininkinase, Laktatdehydrogenase und prostataspezifisches Antigen

  Zentralblatt für Arbeitsmedizin Arbeitsschutz und Ergonomie · 2021

  Senior authorCorresponding
  • Gynecology
  • Medicine

  Zusammenfassung Durch körperliche Aktivität oder auch im Rahmen einer Ergometrie (Laufband oder Fahrrad) wird die Muskulatur derart belastet, dass sich die Herz-Kreislauf-Funktion verändert. Hierdurch ist ca. 2 h nach der Belastung der Anstieg der Kreatininkinase (CK) und der Laktatdehydrogenase (LDH) im Blut als Indikator für die Muskelbeanspruchung messbar. Auch der Wert des prostataspezifischen Antigens (PSA), insbesondere bei Männern, ist ein diagnostischer Parameter zur Beurteilung der Prostatafunktion, der bei Belastung der Prostataregion, wie z. B. Rennradfahren, beeinträchtigt werden kann. CK samt Isoenzyme, LDH und PSA können gezielt als Indikatoren für körperliche Belastung eingesetzt werden, insofern eine Aussage zur Vitalität des Patienten formuliert werden soll.

  PublisherOA PDFDOI

• Welchen Einfluss hat die Blutgruppe auf unser Leben?

  Zentralblatt für Arbeitsmedizin Arbeitsschutz und Ergonomie · 2017-01-10

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  PublisherDOI

• Krebserkrankungen in Deutschland

  Zentralblatt für Arbeitsmedizin Arbeitsschutz und Ergonomie · 2016-06-02 · 14 citations

  article1st authorCorresponding
  PublisherDOI

• Social Freezing

  Zentralblatt für Arbeitsmedizin Arbeitsschutz und Ergonomie · 2014-11-27

  article1st authorCorresponding
  PublisherDOI

• Gesundheitsgefährdung durch Phosphor

  Zentralblatt für Arbeitsmedizin Arbeitsschutz und Ergonomie · 2014-10-23

  articleSenior author
  PublisherDOI

• Enterohämorrhagische Escherichia coli

  Zentralblatt für Arbeitsmedizin Arbeitsschutz und Ergonomie · 2014-06-23

  article
  PublisherDOI

• Korrelation von Beinlängendifferenzen, Oberkörperstatik und Kondylenposition

  Manuelle Medizin · 2013-02-13 · 5 citations

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  PublisherDOI

• Structure of a mutant β toxin from<i>Staphylococcus aureus</i>reveals domain swapping and conformational flexibility

  Acta Crystallographica Section F Structural Biology and Crystallization Communications · 2011-03-23 · 3 citations

  articleOpen access

  The 3.35 Å resolution crystal structure of a mutant form of the staphylococcal sphingomyelinase β toxin in which a conserved hydrophobic β-hairpin has been deleted is reported. It is shown that this mutation induces domain swapping of a C-terminal β-strand, leading to the formation of dimers linked by a conformationally flexible hinge region. Eight dimers are seen in the asymmetric unit, exhibiting a broad spectrum of conformations trapped in place by intermolecular contacts within the crystal lattice. Furthermore, the 16 monomers within each asymmetric unit exhibit a remarkable heterogeneity in thermal factors, which can be accounted for by the varying degrees to which each monomer interacts with other molecules in the crystal. This structure provides a unique example of the challenges associated with crystallographic study of flexible proteins.

  PublisherOA PDFDOI

• Beta toxin catalyzes formation of nucleoprotein matrix in staphylococcal biofilms

  Proceedings of the National Academy of Sciences · 2010-07-26 · 194 citations

  article

  Biofilms are surface-associated communities of microbes encompassed by an extracellular matrix. It is estimated that 80% of all bacterial infections involve biofilm formation, but the structure and regulation of biofilms are incompletely understood. Extracellular DNA (eDNA) is a major structural component in many biofilms of the pathogenic bacterium Staphylococcus aureus, but its role is enigmatic. Here, we demonstrate that beta toxin, a neutral sphingomyelinase and a virulence factor of S. aureus, forms covalent cross-links to itself in the presence of DNA (we refer to this as biofilm ligase activity, independent of sphingomyelinase activity) producing an insoluble nucleoprotein matrix in vitro. Furthermore, we show that beta toxin strongly stimulates biofilm formation in vivo as demonstrated by a role in causation of infectious endocarditis in a rabbit model. Together, these results suggest that beta toxin cross-linking in the presence of eDNA assists in forming the skeletal framework upon which staphylococcal biofilms are established.

  PublisherDOI

• X‐ray crystallographic analysis of adipocyte fatty acid binding protein (aP2) modified with 4‐hydroxy‐2‐nonenal

  Protein Science · 2010-05-27 · 35 citations

  articleOpen access

  Fatty acid binding proteins (FABP) have been characterized as facilitating the intracellular solubilization and transport of long-chain fatty acyl carboxylates via noncovalent interactions. More recent work has shown that the adipocyte FABP is also covalently modified in vivo on Cys117 with 4-hydroxy-2-nonenal (4-HNE), a bioactive aldehyde linked to oxidative stress and inflammation. To evaluate 4-HNE binding and modification, the crystal structures of adipocyte FABP covalently and noncovalently bound to 4-HNE have been solved to 1.9 A and 2.3 A resolution, respectively. While the 4-HNE in the noncovalently modified protein is coordinated similarly to a carboxylate of a fatty acid, the covalent form show a novel coordination through a water molecule at the polar end of the lipid. Other defining features between the two structures with 4-HNE and previously solved structures of the protein include a peptide flip between residues Ala36 and Lys37 and the rotation of the side chain of Phe57 into its closed conformation. Representing the first structure of an endogenous target protein covalently modified by 4-HNE, these results define a new class of in vivo ligands for FABPs and extend their physiological substrates to include bioactive aldehydes.

  PublisherOA PDFDOI

Recent grants

• NIH Grant R01GM046436

  NIH · $2.7M · 2005

• NIH Grant R01AI051607

  NIH · $1.0M · 2006

• NIH Grant R01GM054384

  NIH · $967k · 2001

Frequent coauthors

• Patrick M. Schlievert

  University of Iowa Health Care

  57 shared

• C.A. Earhart

  University of Minnesota

  56 shared

• Gregory A. Bohach

  University of Idaho

  34 shared

• John D. Lipscomb

  University of Minnesota

  32 shared

• Brian W. Matthews

  25 shared

• Yoshinori Takeda

  Juntendo University

  20 shared

• Gregory M. Vath

  University of Minnesota

  19 shared

• Timothy J. Tripp

  University of Minnesota Medical Center

  19 shared

Awards & honors

• Dr. James E. Rubin Medical Memorial Award
• Graduating Medical Student Research Award
• Veneziale-Steer Award
• Dr. Marvin and Hadassah Bacaner Research Awards
• Schmidt Steer Award