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Identifying the elusive link between amino acid sequence and charge selectivity in pentameric ligand-gated ion channels.

Proceedings of the National Academy of Sciences of the United States of America

Cymes GD, Grosman C.
PMID: 27791102
Proc Natl Acad Sci U S A. 2016 Nov 08;113(45):E7106-E7115. doi: 10.1073/pnas.1608519113. Epub 2016 Oct 10.

Among neurotransmitter-gated ion channels, the superfamily of pentameric ligand-gated ion channels (pLGICs) is unique in that its members display opposite permeant-ion charge selectivities despite sharing the same structural fold. Although much effort has been devoted to the identification of...

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Cymes GD, Grosman C. Identifying the elusive link between amino acid sequence and charge selectivity in pentameric ligand-gated ion channels. Proc Natl Acad Sci U S A. 2016;113(45):E7106-E7115doi: 10.1073/pnas.1608519113.
Cymes, G. D., & Grosman, C. (2016). Identifying the elusive link between amino acid sequence and charge selectivity in pentameric ligand-gated ion channels. Proceedings of the National Academy of Sciences of the United States of America, 113(45), E7106-E7115. https://doi.org/10.1073/pnas.1608519113
Cymes, Gisela D, and Grosman, Claudio. "Identifying the elusive link between amino acid sequence and charge selectivity in pentameric ligand-gated ion channels." Proceedings of the National Academy of Sciences of the United States of America vol. 113,45 (2016): E7106-E7115. doi: https://doi.org/10.1073/pnas.1608519113
Cymes GD, Grosman C. Identifying the elusive link between amino acid sequence and charge selectivity in pentameric ligand-gated ion channels. Proc Natl Acad Sci U S A. 2016 Nov 08;113(45):E7106-E7115. doi: 10.1073/pnas.1608519113. Epub 2016 Oct 10. PMID: 27791102; PMCID: PMC5111664.
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Selectivity filters and cysteine-rich extracellular loops in voltage-gated sodium, calcium, and NALCN channels.

Frontiers in physiology

Stephens RF, Guan W, Zhorov BS, Spafford JD.
PMID: 26042044
Front Physiol. 2015 May 19;6:153. doi: 10.3389/fphys.2015.00153. eCollection 2015.

How nature discriminates sodium from calcium ions in eukaryotic channels has been difficult to resolve because they contain four homologous, but markedly different repeat domains. We glean clues from analyzing the changing pore region in sodium, calcium and NALCN...

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Stephens RF, Guan W, Zhorov BS, et al. Selectivity filters and cysteine-rich extracellular loops in voltage-gated sodium, calcium, and NALCN channels. Front Physiol. 2015;6:153doi: 10.3389/fphys.2015.00153.
Stephens, R. F., Guan, W., Zhorov, B. S., & Spafford, J. D. (2015). Selectivity filters and cysteine-rich extracellular loops in voltage-gated sodium, calcium, and NALCN channels. Frontiers in physiology, 6153. https://doi.org/10.3389/fphys.2015.00153
Stephens, Robert F, et al. "Selectivity filters and cysteine-rich extracellular loops in voltage-gated sodium, calcium, and NALCN channels." Frontiers in physiology vol. 6 (2015): 153. doi: https://doi.org/10.3389/fphys.2015.00153
Stephens RF, Guan W, Zhorov BS, Spafford JD. Selectivity filters and cysteine-rich extracellular loops in voltage-gated sodium, calcium, and NALCN channels. Front Physiol. 2015 May 19;6:153. doi: 10.3389/fphys.2015.00153. eCollection 2015. PMID: 26042044; PMCID: PMC4436565.
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A single fraction from Uncaria sinensis exerts neuroprotective effects against glutamate-induced neurotoxicity in primary cultured cortical neurons.

Anatomy & cell biology

Kim HN, Jang JY, Choi BT.
PMID: 26140220
Anat Cell Biol. 2015 Jun;48(2):95-103. doi: 10.5115/acb.2015.48.2.95. Epub 2015 Jun 26.

We identified a neuroprotective single fraction among 62 ones of hexane extract from Uncaria sinensis (JGH43IA) and investigated its effects and mechanisms in primary cortical neurons. Pretreatment with JGH43IA showed a significantly increase cell viability in a dose-dependent manner...

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Kim HN, Jang JY, Choi BT. A single fraction from Uncaria sinensis exerts neuroprotective effects against glutamate-induced neurotoxicity in primary cultured cortical neurons. Anat Cell Biol. 2015;48(2):95-103doi: 10.5115/acb.2015.48.2.95.
Kim, H. N., Jang, J. Y., & Choi, B. T. (2015). A single fraction from Uncaria sinensis exerts neuroprotective effects against glutamate-induced neurotoxicity in primary cultured cortical neurons. Anatomy & cell biology, 48(2), 95-103. https://doi.org/10.5115/acb.2015.48.2.95
Kim, Ha Neui, et al. "A single fraction from Uncaria sinensis exerts neuroprotective effects against glutamate-induced neurotoxicity in primary cultured cortical neurons." Anatomy & cell biology vol. 48,2 (2015): 95-103. doi: https://doi.org/10.5115/acb.2015.48.2.95
Kim HN, Jang JY, Choi BT. A single fraction from Uncaria sinensis exerts neuroprotective effects against glutamate-induced neurotoxicity in primary cultured cortical neurons. Anat Cell Biol. 2015 Jun;48(2):95-103. doi: 10.5115/acb.2015.48.2.95. Epub 2015 Jun 26. PMID: 26140220; PMCID: PMC4488647.
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A γ-glutamyl hydrolase lacking the signal peptide confers susceptibility to folates/antifolates in acute lymphoblastic leukemia cells.

FEBS letters

Wang S, Chen Y, Fang H, Xu Y, Ding M, Ma C, Lin Y, Cui Z, Sun H, Niu Q, Sun S, Zhou BS, Xiao N, Li H.
PMID: 35040120
FEBS Lett. 2022 Jan 17; doi: 10.1002/1873-3468.14285. Epub 2022 Jan 17.

A key cofactor of several enzymes implicated in DNA synthesis, repair, and methylation, folate has been shown to be required for normal cell growth and replication and is the basis for cancer chemotherapy using antifolates. γ-Glutamyl hydrolase (GGH) catalyzes...

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Wang S, Chen Y, Fang H, et al. A γ-glutamyl hydrolase lacking the signal peptide confers susceptibility to folates/antifolates in acute lymphoblastic leukemia cells. FEBS Lett. 2022;doi: 10.1002/1873-3468.14285.
Wang, S., Chen, Y., Fang, H., Xu, Y., Ding, M., Ma, C., Lin, Y., Cui, Z., Sun, H., Niu, Q., Sun, S., Zhou, B. S., Xiao, N., & Li, H. (2022). A γ-glutamyl hydrolase lacking the signal peptide confers susceptibility to folates/antifolates in acute lymphoblastic leukemia cells. FEBS letters, . https://doi.org/10.1002/1873-3468.14285
Wang, Shuxuan, et al. "A γ-glutamyl hydrolase lacking the signal peptide confers susceptibility to folates/antifolates in acute lymphoblastic leukemia cells." FEBS letters vol. (2022). doi: https://doi.org/10.1002/1873-3468.14285
Wang S, Chen Y, Fang H, Xu Y, Ding M, Ma C, Lin Y, Cui Z, Sun H, Niu Q, Sun S, Zhou BS, Xiao N, Li H. A γ-glutamyl hydrolase lacking the signal peptide confers susceptibility to folates/antifolates in acute lymphoblastic leukemia cells. FEBS Lett. 2022 Jan 17; doi: 10.1002/1873-3468.14285. Epub 2022 Jan 17. PMID: 35040120.
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Guanylyl cyclase-A phosphorylation decreases cardiac hypertrophy and improves systolic function in male, but not female, mice.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

Wagner BM, Robinson JW, Healy CL, Gauthier M, Dickey DM, Yee SP, Osborn JW, O'Connell TD, Potter LR.
PMID: 34859913
FASEB J. 2022 Jan;36(1):e22069. doi: 10.1096/fj.202100600RRR.

Atrial natriuretic peptide (NP) and BNP increase cGMP, which reduces blood pressure and cardiac hypertrophy by activating guanylyl cyclase (GC)-A, also known as NPR-A or Npr1. Although GC-A is highly phosphorylated, and dephosphorylation inactivates the enzyme, the significance of...

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Wagner BM, Robinson JW, Healy CL, et al. Guanylyl cyclase-A phosphorylation decreases cardiac hypertrophy and improves systolic function in male, but not female, mice. FASEB J. 2022;36(1):e22069doi: 10.1096/fj.202100600RRR.
Wagner, B. M., Robinson, J. W., Healy, C. L., Gauthier, M., Dickey, D. M., Yee, S. P., Osborn, J. W., O'Connell, T. D., & Potter, L. R. (2022). Guanylyl cyclase-A phosphorylation decreases cardiac hypertrophy and improves systolic function in male, but not female, mice. FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 36(1), e22069. https://doi.org/10.1096/fj.202100600RRR
Wagner, Brandon M, et al. "Guanylyl cyclase-A phosphorylation decreases cardiac hypertrophy and improves systolic function in male, but not female, mice." FASEB journal : official publication of the Federation of American Societies for Experimental Biology vol. 36,1 (2022): e22069. doi: https://doi.org/10.1096/fj.202100600RRR
Wagner BM, Robinson JW, Healy CL, Gauthier M, Dickey DM, Yee SP, Osborn JW, O'Connell TD, Potter LR. Guanylyl cyclase-A phosphorylation decreases cardiac hypertrophy and improves systolic function in male, but not female, mice. FASEB J. 2022 Jan;36(1):e22069. doi: 10.1096/fj.202100600RRR. PMID: 34859913.
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Structure guided mutagenesis reveals the substrate determinants of guanine deaminase.

Journal of structural biology

Singh J, Gaded V, Bitra A, Anand R.
PMID: 34010666
J Struct Biol. 2021 Sep;213(3):107747. doi: 10.1016/j.jsb.2021.107747. Epub 2021 May 16.

Guanine deaminases (GDs) are essential enzymes that regulate the overall nucleobase pool. Since the deamination of guanine to xanthine results in the production of a mutagenic base, these enzymes have evolved to be very specific in nature. Surprisingly, they...

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Singh J, Gaded V, Bitra A, et al. Structure guided mutagenesis reveals the substrate determinants of guanine deaminase. J Struct Biol. 2021;213(3):107747doi: 10.1016/j.jsb.2021.107747.
Singh, J., Gaded, V., Bitra, A., & Anand, R. (2021). Structure guided mutagenesis reveals the substrate determinants of guanine deaminase. Journal of structural biology, 213(3), 107747. https://doi.org/10.1016/j.jsb.2021.107747
Singh, Jayanti, et al. "Structure guided mutagenesis reveals the substrate determinants of guanine deaminase." Journal of structural biology vol. 213,3 (2021): 107747. doi: https://doi.org/10.1016/j.jsb.2021.107747
Singh J, Gaded V, Bitra A, Anand R. Structure guided mutagenesis reveals the substrate determinants of guanine deaminase. J Struct Biol. 2021 Sep;213(3):107747. doi: 10.1016/j.jsb.2021.107747. Epub 2021 May 16. PMID: 34010666.
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Guanylyl cyclase-A phosphorylation decreases cardiac hypertrophy and improves systolic function in male, but not female, mice.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

Wagner BM, Robinson JW, Healy CL, Gauthier M, Dickey DM, Yee SP, Osborn JW, O'Connell TD, Potter LR.
PMID: 34859913
FASEB J. 2022 Jan;36(1):e22069. doi: 10.1096/fj.202100600RRR.

Atrial natriuretic peptide (NP) and BNP increase cGMP, which reduces blood pressure and cardiac hypertrophy by activating guanylyl cyclase (GC)-A, also known as NPR-A or Npr1. Although GC-A is highly phosphorylated, and dephosphorylation inactivates the enzyme, the significance of...

Cite
Wagner BM, Robinson JW, Healy CL, et al. Guanylyl cyclase-A phosphorylation decreases cardiac hypertrophy and improves systolic function in male, but not female, mice. FASEB J. 2022;36(1):e22069doi: 10.1096/fj.202100600RRR.
Wagner, B. M., Robinson, J. W., Healy, C. L., Gauthier, M., Dickey, D. M., Yee, S. P., Osborn, J. W., O'Connell, T. D., & Potter, L. R. (2022). Guanylyl cyclase-A phosphorylation decreases cardiac hypertrophy and improves systolic function in male, but not female, mice. FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 36(1), e22069. https://doi.org/10.1096/fj.202100600RRR
Wagner, Brandon M, et al. "Guanylyl cyclase-A phosphorylation decreases cardiac hypertrophy and improves systolic function in male, but not female, mice." FASEB journal : official publication of the Federation of American Societies for Experimental Biology vol. 36,1 (2022): e22069. doi: https://doi.org/10.1096/fj.202100600RRR
Wagner BM, Robinson JW, Healy CL, Gauthier M, Dickey DM, Yee SP, Osborn JW, O'Connell TD, Potter LR. Guanylyl cyclase-A phosphorylation decreases cardiac hypertrophy and improves systolic function in male, but not female, mice. FASEB J. 2022 Jan;36(1):e22069. doi: 10.1096/fj.202100600RRR. PMID: 34859913.
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Cation and Anion Channelrhodopsins: Sequence Motifs and Taxonomic Distribution.

mBio

Govorunova EG, Sineshchekov OA, Li H, Wang Y, Brown LS, Palmateer A, Melkonian M, Cheng S, Carpenter E, Patterson J, Wong GK, Spudich JL.
PMID: 34281394
mBio. 2021 Aug 31;12(4):e0165621. doi: 10.1128/mBio.01656-21. Epub 2021 Jul 20.

Cation and anion channelrhodopsins (CCRs and ACRs, respectively) primarily from two algal species, Chlamydomonas reinhardtii and Guillardia theta, have become widely used as optogenetic tools to control cell membrane potential with light. We mined algal and other protist polynucleotide...

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Govorunova EG, Sineshchekov OA, Li H, et al. Cation and Anion Channelrhodopsins: Sequence Motifs and Taxonomic Distribution. mBio. 2021;12(4):e0165621doi: 10.1128/mBio.01656-21.
Govorunova, E. G., Sineshchekov, O. A., Li, H., Wang, Y., Brown, L. S., Palmateer, A., Melkonian, M., Cheng, S., Carpenter, E., Patterson, J., Wong, G. K., & Spudich, J. L. (2021). Cation and Anion Channelrhodopsins: Sequence Motifs and Taxonomic Distribution. mBio, 12(4), e0165621. https://doi.org/10.1128/mBio.01656-21
Govorunova, Elena G, et al. "Cation and Anion Channelrhodopsins: Sequence Motifs and Taxonomic Distribution." mBio vol. 12,4 (2021): e0165621. doi: https://doi.org/10.1128/mBio.01656-21
Govorunova EG, Sineshchekov OA, Li H, Wang Y, Brown LS, Palmateer A, Melkonian M, Cheng S, Carpenter E, Patterson J, Wong GK, Spudich JL. Cation and Anion Channelrhodopsins: Sequence Motifs and Taxonomic Distribution. mBio. 2021 Aug 31;12(4):e0165621. doi: 10.1128/mBio.01656-21. Epub 2021 Jul 20. PMID: 34281394; PMCID: PMC8406140.
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Preparation of detergent-lipase complexes utilizing water-soluble amphiphiles in single aqueous phase and catalysis of transesterifications in homogeneous organic solvents.

Journal of bioscience and bioengineering

Mine Y, Fukunaga K, Maruoka N, Nakao K, Sugimura Y.
PMID: 16232923
J Biosci Bioeng. 2000;90(6):631-6. doi: 10.1263/jbb.90.631.

A novel method of preparing detergent-enzyme complexes that can be employed in organic media was developed utilizing newly synthesized water-soluble nonionic gemini-type detergents, N,N-bis(3-D-gluconamidopropyl)-3-(dialkyl-L-glutamatecarbonyl)propanamides (BIG2CnCA: n = 10,12,14,16,18) and N,N-bis(3-D-lactonamidopropyl)-3-(dialkyl-L-glutamatecarbonyl)propanamides (BIL2CnCA: n = 16,18), and nonionic twin-headed detergents, N,N-bis(3-D-gluconamidopropyl)alkanamides...

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Mine Y, Fukunaga K, Maruoka N, et al. Preparation of detergent-lipase complexes utilizing water-soluble amphiphiles in single aqueous phase and catalysis of transesterifications in homogeneous organic solvents. J Biosci Bioeng. 2000;90(6):631-6doi: 10.1263/jbb.90.631.
Mine, Y., Fukunaga, K., Maruoka, N., Nakao, K., & Sugimura, Y. (2000). Preparation of detergent-lipase complexes utilizing water-soluble amphiphiles in single aqueous phase and catalysis of transesterifications in homogeneous organic solvents. Journal of bioscience and bioengineering, 90(6), 631-6. https://doi.org/10.1263/jbb.90.631
Mine, Y, et al. "Preparation of detergent-lipase complexes utilizing water-soluble amphiphiles in single aqueous phase and catalysis of transesterifications in homogeneous organic solvents." Journal of bioscience and bioengineering vol. 90,6 (2000): 631-6. doi: https://doi.org/10.1263/jbb.90.631
Mine Y, Fukunaga K, Maruoka N, Nakao K, Sugimura Y. Preparation of detergent-lipase complexes utilizing water-soluble amphiphiles in single aqueous phase and catalysis of transesterifications in homogeneous organic solvents. J Biosci Bioeng. 2000;90(6):631-6. doi: 10.1263/jbb.90.631. PMID: 16232923.
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Refined crystal structure of the catalytic domain of xylanase A from Pseudomonas fluorescens at 1.8 A resolution.

Acta crystallographica. Section D, Biological crystallography

Harris GW, Jenkins JA, Connerton I, Pickersgill RW.
PMID: 15299710
Acta Crystallogr D Biol Crystallogr. 1996 Mar 01;52:393-401. doi: 10.1107/S0907444995013540.

The three-dimensional structure of native xylanase A from Pseudomonas flouorescens subspecies cellulosa has been refined at 1.8 A resolution. The space group is P2(1)2(1)2(1) with four molecules in the asymmetric unit. The final model has an R factor of...

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Harris GW, Jenkins JA, Connerton I, et al. Refined crystal structure of the catalytic domain of xylanase A from Pseudomonas fluorescens at 1.8 A resolution. Acta Crystallogr D Biol Crystallogr. 1996;52:393-401doi: 10.1107/S0907444995013540.
Harris, G. W., Jenkins, J. A., Connerton, I., & Pickersgill, R. W. (1996). Refined crystal structure of the catalytic domain of xylanase A from Pseudomonas fluorescens at 1.8 A resolution. Acta crystallographica. Section D, Biological crystallography, 52393-401. https://doi.org/10.1107/S0907444995013540
Harris, G W, et al. "Refined crystal structure of the catalytic domain of xylanase A from Pseudomonas fluorescens at 1.8 A resolution." Acta crystallographica. Section D, Biological crystallography vol. 52 (1996): 393-401. doi: https://doi.org/10.1107/S0907444995013540
Harris GW, Jenkins JA, Connerton I, Pickersgill RW. Refined crystal structure of the catalytic domain of xylanase A from Pseudomonas fluorescens at 1.8 A resolution. Acta Crystallogr D Biol Crystallogr. 1996 Mar 01;52:393-401. doi: 10.1107/S0907444995013540. PMID: 15299710.
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Neutral Salt Addition Compounds of Alkaline Earth Glutamates and Aspartates.

The Biochemical journal

Anslow WK, King H.
PMID: 16743948
Biochem J. 1927;21(5):1168-78. doi: 10.1042/bj0211168.

No abstract available.

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Anslow WK, King H. Neutral Salt Addition Compounds of Alkaline Earth Glutamates and Aspartates. Biochem J. 1927;21(5):1168-78doi: 10.1042/bj0211168.
Anslow, W. K., & King, H. (1927). Neutral Salt Addition Compounds of Alkaline Earth Glutamates and Aspartates. The Biochemical journal, 21(5), 1168-78. https://doi.org/10.1042/bj0211168
Anslow, W K, and King, H. "Neutral Salt Addition Compounds of Alkaline Earth Glutamates and Aspartates." The Biochemical journal vol. 21,5 (1927): 1168-78. doi: https://doi.org/10.1042/bj0211168
Anslow WK, King H. Neutral Salt Addition Compounds of Alkaline Earth Glutamates and Aspartates. Biochem J. 1927;21(5):1168-78. doi: 10.1042/bj0211168. PMID: 16743948; PMCID: PMC1252038.
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Glutamic acid as anticancer agent: An overview.

Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society

Dutta S, Ray S, Nagarajan K.
PMID: 24227952
Saudi Pharm J. 2013 Oct;21(4):337-43. doi: 10.1016/j.jsps.2012.12.007.

The objective of the article is to highlight various roles of glutamic acid like endogenic anticancer agent, conjugates to anticancer agents, and derivatives of glutamic acid as possible anticancer agents. Besides these emphases are given especially for two endogenous...

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Dutta S, Ray S, Nagarajan K. Glutamic acid as anticancer agent: An overview. Saudi Pharm J. 2013;21(4):337-43doi: 10.1016/j.jsps.2012.12.007.
Dutta, S., Ray, S., & Nagarajan, K. (2013). Glutamic acid as anticancer agent: An overview. Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society, 21(4), 337-43. https://doi.org/10.1016/j.jsps.2012.12.007
Dutta, Satyajit, et al. "Glutamic acid as anticancer agent: An overview." Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society vol. 21,4 (2013): 337-43. doi: https://doi.org/10.1016/j.jsps.2012.12.007
Dutta S, Ray S, Nagarajan K. Glutamic acid as anticancer agent: An overview. Saudi Pharm J. 2013 Oct;21(4):337-43. doi: 10.1016/j.jsps.2012.12.007. PMID: 24227952; PMCID: PMC3824943.
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Showing 13 to 24 of 41 entries