Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Rajesh Gumpena"'
Autor:
Tom E. Forshaw, Julie A. Reisz, Kimberly J. Nelson, Rajesh Gumpena, J. Reed Lawson, Thomas J. Jönsson, Hanzhi Wu, Jill E. Clodfelter, Lynnette C. Johnson, Cristina M. Furdui, W. Todd Lowther
Publikováno v:
Antioxidants, Vol 10, Iss 6, p 946 (2021)
Human peroxiredoxins (Prx) are a family of antioxidant enzymes involved in a myriad of cellular functions and diseases. During the reaction with peroxides (e.g., H2O2), the typical 2-Cys Prxs change oligomeric structure between higher order (do)decam
Externí odkaz:
https://doaj.org/article/d55fdb246166416a82421dcc5de5c96d
Publikováno v:
Acta Crystallogr F Struct Biol Commun
Yersinia pestis, the causative agent of bubonic plague, is one of the most lethal pathogens in recorded human history. Today, the concern is the possible misuse ofY. pestisas an agent in bioweapons and bioterrorism. Current therapies for the treatmen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::126c441072f7298c5e198b0464de24ee
https://doi.org/10.1107/s2053230x19011154
https://doi.org/10.1107/s2053230x19011154
Autor:
John Knight, Alexandre Caron, Jayakumar Surendradoss, Oliver Chong, David A. Powell, Joyce Wu, Valerie Dumais, Aaron H. Graff, Samuel Gaudreault, Ding Jinyue, Renata Oballa, Andrew T. King, Tim Tang, Rajesh Gumpena, Jennifer H Cox, W. Todd Lowther, Marc-Olivier Boily
Publikováno v:
ACS Med Chem Lett
[Image: see text] Both glycolate oxidase (GO) and lactate dehydrogenase A (LDHA) influence the endogenous synthesis of oxalate and are clinically validated targets for treatment of primary hyperoxaluria (PH). We investigated whether dual inhibition o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d2657ef881efc3975d21c823aaea40e
https://europepmc.org/articles/PMC8274068/
https://europepmc.org/articles/PMC8274068/
Autor:
Cristina M. Furdui, Jill E. Clodfelter, J. Reed Lawson, Julie A. Reisz, Hanzhi Wu, W. Todd Lowther, Rajesh Gumpena, Lynnette C. Johnson, Thomas J. Jönsson, Kimberly J. Nelson, Tom E. Forshaw
Publikováno v:
Antioxidants
Antioxidants, Vol 10, Iss 946, p 946 (2021)
Volume 10
Issue 6
Antioxidants, Vol 10, Iss 946, p 946 (2021)
Volume 10
Issue 6
Human peroxiredoxins (Prx) are a family of antioxidant enzymes involved in a myriad of cellular functions and diseases. During the reaction with peroxides (e.g., H2O2), the typical 2-Cys Prxs change oligomeric structure between higher order (do)decam
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df55ebfbd319a2cc77be07fa4504987b
https://pubmed.ncbi.nlm.nih.gov/34208049
https://pubmed.ncbi.nlm.nih.gov/34208049
Publikováno v:
Acta Crystallographica Section F Structural Biology Communications. 74:549-557
The production of high-quality crystals is the main bottleneck in determining the structures of proteins using X-ray crystallography. In addition to being recognized as a very effective solubility-enhancing fusion partner,Escherichia colimaltose-bind
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f67c990f3e2151ef9307acf24b984c38
https://doi.org/10.1107/s2053230x18009901
https://doi.org/10.1107/s2053230x18009901
Autor:
Joseph E. Tropea, Rajesh Gumpena, George T. Lountos, Scott Cherry, Sreejith Raran-Kurussi, David S. Waugh
Publikováno v:
Protein Science. 27:561-567
The dual specificity phosphatase DUSP1 was the first mitogen activated protein kinase phosphatase (MKP) to be identified. It dephosphorylates conserved tyrosine and threonine residues in the activation loops of mitogen activated protein kinases ERK2,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0f06b7a5c863fc3aeebf89e6bbfe355b
https://doi.org/10.1002/pro.3328
https://doi.org/10.1002/pro.3328
Autor:
Sean L. Simpson, Tom Hollis, Wayne O. Hemphill, Terrence L. Smalley, Fred W. Perrino, Fred Salsbury, Rajesh Gumpena, Scott Harvey, Jason M. Grayson
Publikováno v:
The FASEB Journal. 34:1-1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::73ab1a9532bd41d531e8c80e05fdd82a
https://doi.org/10.1096/fasebj.2020.34.s1.03452
https://doi.org/10.1096/fasebj.2020.34.s1.03452
Autor:
Aruna Jangam, Neshatul Haque, Anil Kumar Marapaka, Vijaykumar Pillalamarri, Anthony Addlagatta, Sandeep Chowdary Bala, Rajesh Gumpena
Publikováno v:
International journal of biological macromolecules. 120
Aminopeptidases catalyze the hydrolysis of amino acids from the N-terminus of protein or peptide substrates. M1 family aminopeptidases are important for the pathogenicity of bacteria and play critical role in many physiological processes such as prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef321c4a566b6ac7d33ffd885f551812
https://pubmed.ncbi.nlm.nih.gov/30172821
https://pubmed.ncbi.nlm.nih.gov/30172821
Autor:
Rajesh Gumpena, Roopa Jones Ganji, Ravikumar Reddi, Tarun Arya, Anil Kumar Marapaka, Anthony Addlagatta, Supriya Bhukya, Priyanka Sankoju
Publikováno v:
Protein Science. 24:823-831
Actinonin is a pseudotripeptide that displays a high affinity towards metalloproteases including peptide deformylases (PDFs) and M1 family aminopeptidases. PDF and M1 family aminopeptidases belong to thermolysin-metzincin superfamily. One of the majo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e43b79230efd00cec366a8120ea0cfe5
https://doi.org/10.1002/pro.2653
https://doi.org/10.1002/pro.2653
Autor:
Rajesh, Gumpena, George T, Lountos, Sreejith, Raran-Kurussi, Joseph E, Tropea, Scott, Cherry, David S, Waugh
Publikováno v:
Protein science : a publication of the Protein Society. 27(2)
The dual specificity phosphatase DUSP1 was the first mitogen activated protein kinase phosphatase (MKP) to be identified. It dephosphorylates conserved tyrosine and threonine residues in the activation loops of mitogen activated protein kinases ERK2,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c0814edacf2690935dfdae751578d635
https://pubmed.ncbi.nlm.nih.gov/29052270
https://pubmed.ncbi.nlm.nih.gov/29052270