User profiles for Stanley J. Opella

Stanley J. Opella

Professor of Chemistry and Biochemistry, University of California, San Diego
Verified email at ucsd.edu
Cited by 24260

Structure of the chemokine receptor CXCR1 in phospholipid bilayers

…, K Maier, AA De Angelis, FM Marassi, SJ Opella - Nature, 2012 - nature.com
CXCR1 is one of two high-affinity receptors for the CXC chemokine interleukin-8 (IL-8), a major
mediator of immune and inflammatory responses implicated in many disorders, including …

Structure determination of membrane proteins by NMR spectroscopy

SJ Opella, FM Marassi - Chemical reviews, 2004 - ACS Publications
Much of postgenomic biochemistry and all of structural biology are based on the premise
that the starting point for both understanding specific biochemical processes, such as affinity, …

Structure and orientation of the antibiotic peptide magainin in membranes by solid‐state nuclear magnetic resonance spectroscopy

B Bechinger, M Zasloff, SJ Opella - Protein Science, 1993 - Wiley Online Library
Magainin 2 is a 23‐residue peptide that forms an amphipathic α‐helix in membrane
environments. It functions as an antibiotic and is known to disrupt the electrochemical gradients …

[HTML][HTML] A solid-state NMR index of helical membrane protein structure and topology

FM Marassi, SJ Opella - … of magnetic resonance (San Diego, Calif …, 2000 - ncbi.nlm.nih.gov
The secondary structure and topology of membrane proteins can be described by inspection
of two-dimensional 1 H-15 N dipolar coupling/15 N chemical shift polarization inversion …

Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an α-helix in dodecylphosphocholine micelles, sodium dodecylsulfate …

J Gesell, M Zasloff, SJ Opella - Journal of biomolecular NMR, 1997 - Springer
Magainin2 is a 23-residue antibiotic peptide that disrupts the ionic gradient across certain
cellmembranes. Two-dimensional 1H NMR spectroscopy was used to investigate the structure …

Three-dimensional structure of the channel-forming trans-membrane domain of virus protein “u”(Vpu) from HIV-1

…, M Oblatt-Montal, M Montal, SJ Opella - Journal of molecular …, 2003 - Elsevier
The three-dimensional structure of the channel-forming trans-membrane domain of virus
protein “u” (Vpu) of HIV-1 was determined by NMR spectroscopy in micelle and bilayer samples…

Trapping the dynamic acyl carrier protein in fatty acid biosynthesis

…, F Ishikawa, B O'Dowd, JA McCammon, SJ Opella… - Nature, 2014 - nature.com
Acyl carrier protein (ACP) transports the growing fatty acid chain between enzymatic domains
of fatty acid synthase (FAS) during biosynthesis 1 . Because FAS enzymes operate on ACP…

High Resolution Solid State 13C NMR Spectroscopy of Sporopollenins from Different Plant Taxa

…, DM Schneider, J Labovitz, SJ Opella - Plant …, 1988 - academic.oup.com
The extremely chemically resistant component of the cell wall of spores, pollens, and some
microorganisms, sporopollenin, is generally accepted to be derived from carotenoids or …

Structures of the Reduced and Mercury-Bound Forms of MerP, the Periplasmic Protein from the Bacterial Mercury Detoxification System,

RA Steele, SJ Opella - Biochemistry, 1997 - ACS Publications
Bacteria carrying plasmids with the mer operon, which encodes the proteins responsible for
the bacterial mercury detoxification system, have the ability to transport Hg(II) across the cell …

Bicelle samples for solid-state NMR of membrane proteins

AA De Angelis, SJ Opella - Nature protocols, 2007 - nature.com
Magnetically aligned bicelles are an excellent medium for structure determination of isotopically
labeled membrane proteins by solid-state NMR spectroscopy. Bicelles are a mixture of …