Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Ezhilkani Subbian"'
Autor:
Sarma Rajeev Kumar, Einstein Mariya David, Gangigere Jagadish Pavithra, Gopalakrishnan Sajith Kumar, Kuppan Lesharadevi, Selvaraj Akshaya, Chavadi Basavaraddi, Gopal Navyashree, Panakanahalli Shivaramu Arpitha, Padmanabhan Sreedevi, Khan Zainuddin, Saiyyeda Firdous, Bondalakunta Ravindra Babu, Muralidhar Udagatti Prashanth, Ganesan Ravikumar, Palabhanvi Basavaraj, Sandeep Kumar Chavana, Vinod Munisanjeeviah Lakshmi Devi Kumar, Theivasigamani Parthasarathi, Ezhilkani Subbian
Publikováno v:
Frontiers in Plant Science, Vol 15 (2024)
IntroductionMore than half of the world’s population consumes rice as their primary food. The majority of rice production is concentrated in Asia, with the top 10 rice-growing countries accounting for 84% of the world’s total rice cultivation. Ho
Externí odkaz:
https://doaj.org/article/bd2189974af04c73a615ed444f9ded2a
Publikováno v:
Advances in Bioscience and Biotechnology. :73-88
Efficient and precise assembly of polypeptides into native functional states is critical for normal cellular processes. Understanding how a specific structure is encoded in the polypeptide sequence and what drives the structural progression to the na
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::68eaf72c776b804055048674640837e5
https://doi.org/10.4236/abb.2015.62008
https://doi.org/10.4236/abb.2015.62008
Autor:
Sean S. Molloy, Chien Hui Hung, Gary Thomas, Sylvain Feliciangeli, François Jean, Ujwal Shinde, Gregory K. Scott, Laurel Thomas, Ezhilkani Subbian
Publikováno v:
Journal of Biological Chemistry. 281:16108-16116
The folding and activation of furin occur through two pH- and compartment-specific autoproteolytic steps. In the endoplasmic reticulum (ER), profurin folds under the guidance of its prodomain and undergoes an autoproteolytic excision at the consensus
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36139a4d6ad2fa7502711e29e7df604e
https://doi.org/10.1074/jbc.m600760200
https://doi.org/10.1074/jbc.m600760200
Autor:
Vivian Hwa, William R. Skach, Teresa M. Buck, Ron G. Rosenfeld, Peter Rotwein, Ezhilkani Subbian, Ujwal Shinde, Dennis J. Chia
Publikováno v:
Journal of Biological Chemistry. 281:6552-6558
A predicted alanine to proline substitution in Stat5b that results in profound short stature, growth hormone insensitivity, and immunodeficiency represents the first natural mutation of this transcription factor in a human. To understand the mechanis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e7909f36d67e52a2cdb79c90569a005
https://doi.org/10.1074/jbc.m510903200
https://doi.org/10.1074/jbc.m510903200
Publikováno v:
Journal of Biological Chemistry. 278:15246-15251
Catalytic domains of several prokaryotic and eukaryotic protease families require dedicated N-terminal propeptide domains or “intramolecular chaperones” to facilitate correct folding. Amino acid sequence analysis of these families establishes thr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5bac3578f4c4e9664d05e9e704b9938c
https://doi.org/10.1074/jbc.m212003200
https://doi.org/10.1074/jbc.m212003200
Publikováno v:
BMC Cell Biology, Vol 7, Iss 1, p 7 (2006)
BMC Cell Biology
BMC Cell Biology
BackgroundThe family of c-Jun NH2-terminal kinases (JNK) plays important roles in embryonic development and in cellular responses to stress. Toxic metals and their compounds are potent activators of JNK in mammalian cells. The mechanism of mammalian
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a22ce42549a16fd240ba9b4f0266d936
https://doi.org/10.1186/1471-2121-7-7
https://doi.org/10.1186/1471-2121-7-7
Publikováno v:
Journal of molecular biology. 347(2)
Several secreted proteases are synthesized with N-terminal propeptides that function as intramolecular chaperones (IMCs) and direct the folding of proteases to their native functional states. Using subtilisin E as our model system, we had earlier est
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c1c3608b8201de3fd7545c5afc08fc9
https://pubmed.ncbi.nlm.nih.gov/15740747
https://pubmed.ncbi.nlm.nih.gov/15740747
Publikováno v:
Biochemistry. 43(45)
Subtilisin E (SbtE) is a member of the ubiquitous superfamily of serine proteases called subtilases and serves as a model for understanding propeptide-mediated protein folding mechanisms. Unlike most proteins that adopt thermodynamically stable confo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::644c1d1eceac05b2e939946aece27f4f
https://pubmed.ncbi.nlm.nih.gov/15533039
https://pubmed.ncbi.nlm.nih.gov/15533039
Publikováno v:
The Journal of biological chemistry. 278(17)
Catalytic domains of several prokaryotic and eukaryotic protease families require dedicated N-terminal propeptide domains or "intramolecular chaperones" to facilitate correct folding. Amino acid sequence analysis of these families establishes three i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5e09efec0698f46b7557678f1c42bef9
https://pubmed.ncbi.nlm.nih.gov/12582173
https://pubmed.ncbi.nlm.nih.gov/12582173
Autor:
Peter Rotwein, Ezhilkani Subbian, Ujwal Shinde, Teresa M. Buck, Vivian Hwa, Ron G. Rosenfeld, Dennis J. Chia, William R. Skach
Publikováno v:
Journal of Biological Chemistry. 281:15592
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eedeae8872fda4640336052fdb31de13
https://doi.org/10.1016/s0021-9258(20)56009-2
https://doi.org/10.1016/s0021-9258(20)56009-2