Aya Ryuzoji

Eli Lilly (United States)

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Dorothy M. Morré

Purdue University West Lafayette

Sara Dick

Valparaiso University

Angela J. Okragly

Eli Lilly (United States)

Robert J. Benschop

Eli Lilly (United States)

Isabella H. Wulur

Eli Lilly (United States)

Andrew D. Mesecar

Purdue University West Lafayette

D. James Morré

Purdue University West Lafayette

Julia P. Luciano

Purdue University West Lafayette

Robert Van Horn

University of Rhode Island

Terry W. Moore

University of Illinois Chicago

Cooperative Institutions

University of Illinois Chicago

Purdue University West Lafayette

Eli Lilly (United States)

University of Illinois Urbana-Champaign

Johns Hopkins University

Illinois College

State Street (United States)

Yahoo (United Kingdom)

University of Alabama at Birmingham

Rutgers, The State University of New Jersey

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Crystal structure of 2,2'-(naphthalene-1,4-diylbis(((4-methoxyphenyl)sulfonyl)azanediyl))diacetamide bound to human Keap1 Kelch domain

Julia P. Luciano Aya Ryuzoji Andrew D. Mesecar

Sulfonyl

10.2210/pdb4xmb/pdb

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Citations (1)

Probing the structural requirements of non-electrophilic naphthalene-based Nrf2 activators

European Journal of Medicinal Chemistry (2015)

Atul D. Jain Haranatha R. Potteti Benjamin G. Richardson Laura J. Kingsley Julia P. Luciano

Docking (animal)

Sulforaphane

10.1016/j.ejmech.2015.08.049

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Citations (91)

Identification of the constitutive ultradian oscillator of the circadian clock (ENOX1) in Saccharomyces cerevisiae

Advances in Biological Chemistry (2013)

Sara Dick Aya Ryuzoji Dorothy M. Morré D. James Morré

A yeast (Saccharomyces cerevisiae) deletion library was screened based on NADH fluorescence using a 384 well plate assay and robotics to identify a yeast isolate lacking the 24 min periodic cell surface oxidase. The oxidase was shown previously to be a candidate ultradian oscillator of the yeast’s biological clock. The cDNA was cloned from a yeast overexpression library and the encoded protein was expressed in bacteria and characterized. Glyceraldehyde-3-phosphate dehydrogenase activity was used as the cellular circadian indicator. The identified gene was YML117W which encodes a ca 126 kDa putative RNA-binding protein. The candidate ENOX1 activity from yeast had functional characteristics similar to those of other constitutive ENOX1 proteins of eukaryotes exhibiting oscillating activities with a temperature independent period length of 24 min phased by melatonin and low frequency electromagnetic fields and susceptible to inhibition by the ENOX1 inhibitor, simalikalactone D. The YML117W deletion mutant cells lacked the ENOX1 clock output present in wild type yeast. The findings identify YML117W as the ENOX1 of Saccharomyces cerevisiae and support its proposed function as an ultradian oscillator of the yeast biological clock.

10.4236/abc.2013.33036

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Citations (7)

Binding, Neutralization and Internalization of the Interleukin-13 Antibody, Lebrikizumab

Dermatology and Therapy (2023)

Angela J. Okragly Aya Ryuzoji Isabella H. Wulur Montanea Daniels Robert D. Van Horn

IL-13 is the primary upregulated cytokine in atopic dermatitis (AD) skin and is the pathogenic mediator driving AD pathophysiology. Lebrikizumab, tralokinumab and cendakimab are therapeutic monoclonal antibodies (mAb) that target IL-13.We undertook studies to compare in vitro binding affinities and cell-based functional activities of lebrikizumab, tralokinumab and cendakimab.Lebrikizumab bound IL-13 with higher affinity (as determined using surface plasma resonance) and slower off-rate. It was more potent in neutralizing IL-13-induced effects in STAT6 reporter and primary dermal fibroblast periostin secretion assays than either tralokinumab or cendakimab. Live imaging confocal microscopy was employed to determine the mAb effects on IL-13 internalization into cells via the decoy receptor IL-13Rα2, using A375 and HaCaT cells. The results showed that only the IL-13/lebrikizumab complex was internalized and co-localized with lysosomes, whereas IL-13/tralokinumab or IL-13/cendakimab complexes did not internalize.Lebrikizumab is a potent, neutralizing high-affinity antibody with a slow disassociation rate from IL-13. Additionally, lebrikizumab does not interfere with IL-13 clearance. Lebrikizumab has a different mode of action to both tralokinumab and cendakimab, possibly contributing to the clinical efficacy observed by lebrikizumab in Ph2b/3 AD studies.

Internalization

Periostin

Transcytosis

Interleukin 13

Mediator

10.1007/s13555-023-00947-7

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Citations (15)

ESDR109 - Lebrikizumab Allows Interleukin-13 Membrane Binding and Subsequent Internalization through the Decoy Receptor Interleukin-13 Receptor Alpha 2

Isabella H. Wulur Robert Van Horn Aya Ryuzoji Angela J. Okragly Chetan B. Patel

Decoy

Internalization

Interleukin-1 receptor

Alpha (finance)

Interleukin-4 receptor

10.26226/m.62fa0091165d7b0019592ac8

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Citations (3)

Ultradian oscillators of the circadian clock in Saccharomyces cerevisiae

Advances in Biological Chemistry (2013)

Sara Dick Aya Ryuzoji Dorothy M. Morré D. James Morré

The yeast, Saccharomyces cerevisiae, has an ENOX1 activity with a period length of 24 min similar to that of other eukaryotes. In contrast to other eukaryotes, however, Saccharomyces cerevisiae has a second ENOX1-like activity with a period length of 25 min. The latter is distinguishable from the traditional ENOX1 on the basis of the longer period length along with resistance to an ENOX1 inhibitor, simalikalactone D, and failure to be phased by melatonin. In addition, two periods are apparent in measurements of oxygen consumption indicating that the consumption of oxygen to water occurs independently by homodimers of both of the two forms of ENOX. Based on the measurements of glyceraldehyde-3- phosphate dehydrogenase, S. cerevisiae exhibits circadian activity maxima at 24 and 25 h together with a 40 h period possibly representing the 40 min metabolic rhythm of yeast not observed in our measurement of oxygen consumption and normally observed only with continuous cultures. The findings are indicative of at least three independent time-keeping systems being operative in a single cell.

10.4236/abc.2013.31008

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Citations (8)

Molecular Cloning and Characterization of a Candidate ENOX Protein of Saccharomyces cerevisiae with a 25 Min Period Insensitive to Simalikalactone D Inhibition and Melatonin

Advances in Biological Chemistry (2014)

Aya Ryuzoji Debby H. Parisi Sara Dick James Kim Dorothy M. Morré

A yeast deletion library was screened based on NADH fluorescence using a 384-well plate assay to identify a yeast isolate lacking a previously identified cell surface oxidase exhibiting an oscillatory pattern with a period length of 25 min and resistant to the ENOX1-specific inhibitor simalikalactone D (YNOX for yeast-specific ENOX = ENOX4). The cDNA was cloned from a yeast over expression library using NADH fluorescence analyzed by Fast Fourier transform and decomposition fits. The objective was to identify and sequence an ENOX homologue in Saccharomyces cerevisiae with a 25 min rather than a 24 min period length (YNOX). The finding identified YDR005C as the yeast ENOX protein with a temperature-independent 25 min period length and insensitive to inhibition by simalikalactone D. The encoded protein was expressed in bacteria and characterized. Gel slices corresponding to 55 kDa and 39 kDa His-tagged proteins exhibited 25 min oscillatory patterns not inhibited by 1 μM simalikalactone D for both NADH oxidation and reduced coenzyme Q10 oxidation as well as a protein disulfide-thiol interchange activity which alternated with the oxidative activities. Activities were phased by low-frequency electromagnetic fields but, in contrast, to yeast ENOX1, not by addition of melatonin. The assay in the presence of D2O shifted the length of the oscillatory period from 25 min to 32 min. The YDR005C deletion mutant cells lacked the ENOX4 clock output present in the wild type yeast.

10.4236/abc.2014.45039

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Citations (1)