Ramya L. Parimi
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Ramya L. Parimi has a total of 6 co-authors. Here are the top co-authors by number of shared publications:
- Hiran M. Thyagarajan
Department of Biology and Biotechnology, College of Science and Engineering, University of Houston-Clear Lake, 2700 Bay Area Blvd., Houston, TX 77058-1098, USA
1 shared publication - Karthik S. Prabhakara
Department of Biology and Biotechnology, College of Science and Engineering, University of Houston-Clear Lake, 2700 Bay Area Blvd., Houston, TX 77058-1098, USA
1 shared publication - Kavya Ganapathy
Department of Biology and Biotechnology, College of Science and Engineering, University of Houston-Clear Lake, 2700 Bay Area Blvd., Houston, TX 77058-1098, USA
1 shared publication - Kazi N. Islam
Department of Agricultural Research Development Program, Central State University, Wilberforce, USA
1 shared publication - Kirti K. Tiwari
Department of Biology and Biotechnology, College of Science and Engineering, University of Houston-Clear Lake, 2700 Bay Area Blvd., Houston, TX 77058-1098, USA
1 shared publication - Mohammad B. Rashid
University of Houston-Clear Lake, Houston, USA
1 shared publication
Latest Publications
- Open Access
- 24 March 2024
- Published by MDPI AG in Biomolecules
- Vol. 14 (4) , 388
Uncovering Novel Protein Partners of Inducible Nitric Oxide Synthase in Human Testis
Peroxidative damage to human spermatozoa has been shown to be the primary cause of male infertility. The possible role of nitric oxide (NO) in affecting sperm motility, capacitation, and acrosome reaction has been reported, too. The overproduction of NO by the enzyme inducible nitric oxide synthase (iNOS) could be responsible as it has been implicated in the pathogenesis of many diseases. There have been many studies on regulating iNOS function in various tissues, especially by protein–protein interaction; however, no study has looked for iNOS-interacting proteins in the human testis. Here, we have reported the identification of two proteins that interact with iNOS. We initially undertook a popular yeast two-hybrid assay to screen a human testis cDNA library in yeast using an iNOS-peptide fragment (amino acids 181–335) as bait. We verified our data using the mammalian chemiluminescent co-IP method; first, employing the same peptide and, then, a full-length protein co-expressed in HEK293 cells in addition to the candidate protein. In both cases, these two protein partners of iNOS were revealed: (a) sperm acrosome-associated 7 protein and (b) retinoblastoma tumor-suppressor binding protein.
- 24 March 2024
- Published by MDPI AG in Biomolecules
- Vol. 14 (4) , 388
Open AccessUncovering Novel Protein Partners of Inducible Nitric Oxide Synthase in Human Testis
Peroxidative damage to human spermatozoa has been shown to be the primary cause of male infertility. The possible role of nitric oxide (NO) in affecting sperm motility, capacitation, and acrosome reaction has been reported, too. The overproduction of NO by the enzyme inducible nitric oxide synthase (iNOS) could be responsible as it has been implicated in the pathogenesis of many diseases. There have been many studies on regulating iNOS function in various tissues, especially by protein–protein interaction; however, no study has looked for iNOS-interacting proteins in the human testis. Here, we have reported the identification of two proteins that interact with iNOS. We initially undertook a popular yeast two-hybrid assay to screen a human testis cDNA library in yeast using an iNOS-peptide fragment (amino acids 181–335) as bait. We verified our data using the mammalian chemiluminescent co-IP method; first, employing the same peptide and, then, a full-length protein co-expressed in HEK293 cells in addition to the candidate protein. In both cases, these two protein partners of iNOS were revealed: (a) sperm acrosome-associated 7 protein and (b) retinoblastoma tumor-suppressor binding protein.