Article in Bioorganic & medicinal chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 54% of its field
1 · What the graph read from it
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
2 · The registry
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
3 · Its place in the literature
Who cites it
1 citing paper in PubMed, 4 citations in OpenAlex.
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
5 · Who and what money
Authors and funding
8 authors at 3 institutions in 1 country.
Luong NguyenDepartment of Pharmaceutical Sciences, The State University of New York at Buffalo, Buffalo, NY 14214, United States.
Daniel C SchultzDepartment of Medicinal Chemistry, University of Florida, Gainesville, FL 32610, United States.
Simon S TerzyanLaboratory of Biomolecular Structure and Function, Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, United States.
Mohammad RezaeiDepartment of Medicinal Chemistry, University of Florida, Gainesville, FL 32610, United States.
Jinhua SongbDepartment of Medicinal Chemistry, University of Florida, Gainesville, FL 32610, United States.
Chenglong LiDepartment of Medicinal Chemistry, University of Florida, Gainesville, FL 32610, United States.
Youngjae YouDepartment of Pharmaceutical Sciences, The State University of New York at Buffalo, Buffalo, NY 14214, United States.
Marie H HaniganDepartment of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, United States. Electronic address: marie-hanigan@ouhsc.edu.
University of Florida · USUniversity at Buffalo, State University of New York · USUniversity of Oklahoma Health Sciences Center · US
Funding
A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Ritimukta Sarangi · 2020 to 2026
$43.3M
X-ray Scattering Technology CoreP30GM133893 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI Sean McSweeney · 2019 to 2026
$38.6M
Tissue Pathology Shared ResourceP30CA225520 · NCI · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI Wade Williams · 2018 to 2026
$27.1M
Structure-Function Studies of MsvR, a Methanogen-Specific Transcriptional RegulaP20GM103640 · NIGMS · UNIVERSITY OF OKLAHOMA · PI THOMAS, LEONARD M · 2012 to 2021
$20.4M
Mechanistic studies of gamma-glutamyl transpeptidase inhibition: A novel approach to modulating serum levels of cysteineR01GM125952 · NIGMS · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI HANIGAN, MARIE H · 2018 to 2020
Inhibitors of gamma-glutamyl transpeptidase (GGT1, aka gamma-glutamyl transferase) are needed for the treatment of cancer, cardiovascular illness and other diseases. Compounds that inhibit GGT1 have been evaluated in the clinic, but no inhibitor has successfully demonstrated specific and systemic GGT1 inhibition. All have severe side effects. L-2-amino-4‑boronobutanoic acid (l-ABBA), a glutamate analog, is the most potent GGT1 inhibitor in vitro. In this study, we have solved the crystal structure of human GGT1 (hGGT1) with ABBA bound in the active site. The structure was interrogated to identify interactions between the enzyme and the inhibitor. Based on these data, a series of novel ABBA analogs were designed and synthesized. Their inhibitory activity against the hydrolysis and transpeptidation activities of hGGT1 were determined. The lead compounds were crystalized with hGGT1 and the structures solved. The kinetic data and structures of the complexes provide new insights into the critical role of protein structure dynamics in developing compounds for inhibition of hGGT1.
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.
Design and evaluation of novel analogs of 2-amino-4-boronobutanoic acid (ABBA) as inhibitors of human gamma-glutamyl transpeptidase. · full record | OpenQuestion