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191.
Mohan KN Rani BS Selvam S Debarshi S Kadandale JS 《Cytogenetic and genome research》2007,119(3-4):255-262
By using ligation-mediated PCR products from mealybug DNA as tester and biotinylated fly DNA as driver, we recovered a fraction of the tester that remains hybridized to driver following high-stringency washing conditions. This fraction is expected to contain mealybug sequences conserved in the fly (MCF). Reciprocal experiments enabled the isolation of fly sequences conserved in the mealybug (FCM). Coding sequences among MCF show amino acid identities >40% with fly proteins, allowing a reliable identification of orthologs. Three sequences from the fly cytogenetic positions 98-99 were hybridized onto mealybug chromosomes and the results identified differences in synteny between the two species. Taken together, our results present a method for direct isolation of sequences conserved between an 'orphan' (mealybug) genome and a 'reference' (fly) genome and showed that these sequences can be used to study chromosome synteny in the mealybug. 相似文献
192.
Fatima Abreeq Husain Tajammul Suhel Mohammad Prasad Sheo Mohan Singh Vijay Pratap 《Journal of Plant Growth Regulation》2022,41(1):163-177
Journal of Plant Growth Regulation - It is a well-established fact that nitric oxide (NO) is a multifaceted signaling molecule, which plays diverse role in organisms. In the past two decades,... 相似文献
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Muthu Valliappan Dhaliwal Manpreet Sharma Arunima Nair Divya Kumar H. Mohan Rudramurthy Shivaprakash M. Sehgal Inderpaul Singh Choudhary Hansraj Panda Naresh Chakrabarti Arunaloke Agarwal Ritesh 《Mycopathologia》2022,187(4):355-362
Mycopathologia - In experimental models, the expression of glucose-regulated protein 78 (GRP78) in endothelial cells played a role in the pathogenesis of mucormycosis. However, the role of GRP78 in... 相似文献
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A Mechanism of Global Shape-dependent Recognition and Phosphorylation of Filamin by Protein Kinase A
Sujay Subbayya Ithychanda Xianyang Fang Maradumane L. Mohan Liang Zhu Kalyan C. Tirupula Sathyamangla V. Naga Prasad Yun-Xing Wang Sadashiva S. Karnik Jun Qin 《The Journal of biological chemistry》2015,290(13):8527-8538
Protein phosphorylation mediates essentially all aspects of cellular life. In humans, this is achieved by ∼500 kinases, each recognizing a specific consensus motif (CM) in the substrates. The majority of CMs are surface-exposed and are thought to be accessible to kinases for phosphorylation. Here we investigated the archetypical protein kinase A (PKA)-mediated phosphorylation of filamin, a major cytoskeletal protein that can adopt an autoinhibited conformation. Surprisingly, autoinhibited filamin is refractory to phosphorylation by PKA on a known Ser2152 site despite its CM being exposed and the corresponding isolated peptide being readily phosphorylated. Structural analysis revealed that although the CM fits into the PKA active site its surrounding regions sterically clash with the kinase. However, upon ligand binding, filamin undergoes a conformational adjustment, allowing rapid phosphorylation on Ser2152. These data uncover a novel ligand-induced conformational switch to trigger filamin phosphorylation. They further suggest a substrate shape-dependent filtering mechanism that channels specific exposed CM/kinase recognition in diverse signaling responses. 相似文献
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Expression of TGFβ superfamily components and other markers of oocyte quality in oocytes selected by brilliant cresyl blue staining: Relevance to early embryonic development
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