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GRK2 targeted knock-down results in spontaneous hypertension, and altered vascular GPCR signaling.

The Journal of biological chemistry

Tutunea-Fatan E, Caetano FA, Gros R, Ferguson SS.
PMID: 27664063
J Biol Chem. 2016 Sep 23;291(39):20822. doi: 10.1074/jbc.A114.615658.

No abstract available.

Cite
Tutunea-Fatan E, Caetano FA, Gros R, et al. GRK2 targeted knock-down results in spontaneous hypertension, and altered vascular GPCR signaling. J Biol Chem. 2016;291(39):20822doi: 10.1074/jbc.A114.615658.
Tutunea-Fatan, E., Caetano, F. A., Gros, R., & Ferguson, S. S. (2016). GRK2 targeted knock-down results in spontaneous hypertension, and altered vascular GPCR signaling. The Journal of biological chemistry, 291(39), 20822. https://doi.org/10.1074/jbc.A114.615658
Tutunea-Fatan, Elena, et al. "GRK2 targeted knock-down results in spontaneous hypertension, and altered vascular GPCR signaling." The Journal of biological chemistry vol. 291,39 (2016): 20822. doi: https://doi.org/10.1074/jbc.A114.615658
Tutunea-Fatan E, Caetano FA, Gros R, Ferguson SS. GRK2 targeted knock-down results in spontaneous hypertension, and altered vascular GPCR signaling. J Biol Chem. 2016 Sep 23;291(39):20822. doi: 10.1074/jbc.A114.615658. PMID: 27664063; PMCID: PMC5034070.
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The transcription factor SPDEF suppresses prostate tumor metastasis.

The Journal of biological chemistry

Steffan JJ, Koul S, Meacham RB, Koul HK.
PMID: 27664067
J Biol Chem. 2016 Sep 23;291(39):20826. doi: 10.1074/jbc.A112.379396.

No abstract available.

Cite
Steffan JJ, Koul S, Meacham RB, et al. The transcription factor SPDEF suppresses prostate tumor metastasis. J Biol Chem. 2016;291(39):20826doi: 10.1074/jbc.A112.379396.
Steffan, J. J., Koul, S., Meacham, R. B., & Koul, H. K. (2016). The transcription factor SPDEF suppresses prostate tumor metastasis. The Journal of biological chemistry, 291(39), 20826. https://doi.org/10.1074/jbc.A112.379396
Steffan, Joshua J, et al. "The transcription factor SPDEF suppresses prostate tumor metastasis." The Journal of biological chemistry vol. 291,39 (2016): 20826. doi: https://doi.org/10.1074/jbc.A112.379396
Steffan JJ, Koul S, Meacham RB, Koul HK. The transcription factor SPDEF suppresses prostate tumor metastasis. J Biol Chem. 2016 Sep 23;291(39):20826. doi: 10.1074/jbc.A112.379396. PMID: 27664067; PMCID: PMC5034074.
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Masochistic enzymology: Dennis Vance's work on phosphatidylcholine.

The Journal of biological chemistry

Carman G, Taylor A.
PMID: 28455407
J Biol Chem. 2017 Apr 28;292(17):7160. doi: 10.1074/jbc.A117.000002.

No abstract available.

Cite
Carman G, Taylor A. Masochistic enzymology: Dennis Vance's work on phosphatidylcholine. J Biol Chem. 2017;292(17):7160doi: 10.1074/jbc.A117.000002.
Carman, G., & Taylor, A. (2017). Masochistic enzymology: Dennis Vance's work on phosphatidylcholine. The Journal of biological chemistry, 292(17), 7160. https://doi.org/10.1074/jbc.A117.000002
Carman, George, and Taylor, Alexandra. "Masochistic enzymology: Dennis Vance's work on phosphatidylcholine." The Journal of biological chemistry vol. 292,17 (2017): 7160. doi: https://doi.org/10.1074/jbc.A117.000002
Carman G, Taylor A. Masochistic enzymology: Dennis Vance's work on phosphatidylcholine. J Biol Chem. 2017 Apr 28;292(17):7160. doi: 10.1074/jbc.A117.000002. PMID: 28455407; PMCID: PMC5409481.
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High resolution structures of the human ABO(H) blood group enzymes in complex with donor analogs reveal that the enzymes utilize multiple donor conformations to bind substrates in a stepwise manner.

The Journal of biological chemistry

Gagnon SM, Meloncelli PJ, Zheng RB, Haji-Ghassemi O, Johal AR, Borisova SN, Lowary TL, Evans SV.
PMID: 27037406
J Biol Chem. 2016 Apr 01;291(14):7229. doi: 10.1074/jbc.A115.682401.

No abstract available.

Cite
Gagnon SM, Meloncelli PJ, Zheng RB, et al. High resolution structures of the human ABO(H) blood group enzymes in complex with donor analogs reveal that the enzymes utilize multiple donor conformations to bind substrates in a stepwise manner. J Biol Chem. 2016;291(14):7229doi: 10.1074/jbc.A115.682401.
Gagnon, S. M., Meloncelli, P. J., Zheng, R. B., Haji-Ghassemi, O., Johal, A. R., Borisova, S. N., Lowary, T. L., & Evans, S. V. (2016). High resolution structures of the human ABO(H) blood group enzymes in complex with donor analogs reveal that the enzymes utilize multiple donor conformations to bind substrates in a stepwise manner. The Journal of biological chemistry, 291(14), 7229. https://doi.org/10.1074/jbc.A115.682401
Gagnon, Susannah M L, et al. "High resolution structures of the human ABO(H) blood group enzymes in complex with donor analogs reveal that the enzymes utilize multiple donor conformations to bind substrates in a stepwise manner." The Journal of biological chemistry vol. 291,14 (2016): 7229. doi: https://doi.org/10.1074/jbc.A115.682401
Gagnon SM, Meloncelli PJ, Zheng RB, Haji-Ghassemi O, Johal AR, Borisova SN, Lowary TL, Evans SV. High resolution structures of the human ABO(H) blood group enzymes in complex with donor analogs reveal that the enzymes utilize multiple donor conformations to bind substrates in a stepwise manner. J Biol Chem. 2016 Apr 01;291(14):7229. doi: 10.1074/jbc.A115.682401. PMID: 27037406; PMCID: PMC4817156.
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The intestinal epithelial cell differentiation marker intestinal alkaline phosphatase (ALPi) is selectively induced by histone deacetylase inhibitors (HDACi) in colon cancer cells in a Kruppel-like factor 5 (KLF5)-dependent manner.

The Journal of biological chemistry

Shin J, Carr A, Corner GA, Tögel L, Dávalos-Salas M, Tran H, Chueh AC, Al-Obaidi S, Chionh F, Ahmed N, Buchanan DD, Young JP, Malo MS, Hodin RA, Arango D, Sieber OM, Augenlicht LH, Dhillon AS, Weber TK, Mariadason JM.
PMID: 26092983
J Biol Chem. 2015 Jun 19;290(25):15392. doi: 10.1074/jbc.A114.557546.

No abstract available.

Cite
Shin J, Carr A, Corner GA, et al. The intestinal epithelial cell differentiation marker intestinal alkaline phosphatase (ALPi) is selectively induced by histone deacetylase inhibitors (HDACi) in colon cancer cells in a Kruppel-like factor 5 (KLF5)-dependent manner. J Biol Chem. 2015;290(25):15392doi: 10.1074/jbc.A114.557546.
Shin, J., Carr, A., Corner, G. A., Tögel, L., Dávalos-Salas, M., Tran, H., Chueh, A. C., Al-Obaidi, S., Chionh, F., Ahmed, N., Buchanan, D. D., Young, J. P., Malo, M. S., Hodin, R. A., Arango, D., Sieber, O. M., Augenlicht, L. H., Dhillon, A. S., Weber, T. K., & Mariadason, J. M. (2015). The intestinal epithelial cell differentiation marker intestinal alkaline phosphatase (ALPi) is selectively induced by histone deacetylase inhibitors (HDACi) in colon cancer cells in a Kruppel-like factor 5 (KLF5)-dependent manner. The Journal of biological chemistry, 290(25), 15392. https://doi.org/10.1074/jbc.A114.557546
Shin, Joongho, et al. "The intestinal epithelial cell differentiation marker intestinal alkaline phosphatase (ALPi) is selectively induced by histone deacetylase inhibitors (HDACi) in colon cancer cells in a Kruppel-like factor 5 (KLF5)-dependent manner." The Journal of biological chemistry vol. 290,25 (2015): 15392. doi: https://doi.org/10.1074/jbc.A114.557546
Shin J, Carr A, Corner GA, Tögel L, Dávalos-Salas M, Tran H, Chueh AC, Al-Obaidi S, Chionh F, Ahmed N, Buchanan DD, Young JP, Malo MS, Hodin RA, Arango D, Sieber OM, Augenlicht LH, Dhillon AS, Weber TK, Mariadason JM. The intestinal epithelial cell differentiation marker intestinal alkaline phosphatase (ALPi) is selectively induced by histone deacetylase inhibitors (HDACi) in colon cancer cells in a Kruppel-like factor 5 (KLF5)-dependent manner. J Biol Chem. 2015 Jun 19;290(25):15392. doi: 10.1074/jbc.A114.557546. PMID: 26092983; PMCID: PMC4505454.
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Proinsulin C-peptide regulates ribosomal RNA expression.

The Journal of biological chemistry

Lindahl E, Nyman U, Zaman F, Palmberg C, Cascante A, Shafqat J, Takigawa M, Sävendahl L, Jörnvall H, Joseph B.
PMID: 28283590
J Biol Chem. 2017 Mar 10;292(10):4382. doi: 10.1074/jbc.A109.053587.

No abstract available.

Cite
Lindahl E, Nyman U, Zaman F, et al. Proinsulin C-peptide regulates ribosomal RNA expression. J Biol Chem. 2017;292(10):4382doi: 10.1074/jbc.A109.053587.
Lindahl, E., Nyman, U., Zaman, F., Palmberg, C., Cascante, A., Shafqat, J., Takigawa, M., Sävendahl, L., Jörnvall, H., & Joseph, B. (2017). Proinsulin C-peptide regulates ribosomal RNA expression. The Journal of biological chemistry, 292(10), 4382. https://doi.org/10.1074/jbc.A109.053587
Lindahl, Emma, et al. "Proinsulin C-peptide regulates ribosomal RNA expression." The Journal of biological chemistry vol. 292,10 (2017): 4382. doi: https://doi.org/10.1074/jbc.A109.053587
Lindahl E, Nyman U, Zaman F, Palmberg C, Cascante A, Shafqat J, Takigawa M, Sävendahl L, Jörnvall H, Joseph B. Proinsulin C-peptide regulates ribosomal RNA expression. J Biol Chem. 2017 Mar 10;292(10):4382. doi: 10.1074/jbc.A109.053587. PMID: 28283590; PMCID: PMC5354506.
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Structural and biochemical insight into the mechanism of Rv2837c from Mycobacterium tuberculosis as a c-di-NMP phosphodiesterase.

The Journal of biological chemistry

He Q, Wang F, Liu S, Zhu D, Cong H, Gao F, Li B, Wang H, Lin Z, Liao J, Gu L.
PMID: 27371563
J Biol Chem. 2016 Jul 01;291(27):14386-14387. doi: 10.1074/jbc.A115.699801.

No abstract available.

Cite
He Q, Wang F, Liu S, et al. Structural and biochemical insight into the mechanism of Rv2837c from Mycobacterium tuberculosis as a c-di-NMP phosphodiesterase. J Biol Chem. 2016;291(27):14386-14387doi: 10.1074/jbc.A115.699801.
He, Q., Wang, F., Liu, S., Zhu, D., Cong, H., Gao, F., Li, B., Wang, H., Lin, Z., Liao, J., & Gu, L. (2016). Structural and biochemical insight into the mechanism of Rv2837c from Mycobacterium tuberculosis as a c-di-NMP phosphodiesterase. The Journal of biological chemistry, 291(27), 14386-14387. https://doi.org/10.1074/jbc.A115.699801
He, Qing, et al. "Structural and biochemical insight into the mechanism of Rv2837c from Mycobacterium tuberculosis as a c-di-NMP phosphodiesterase." The Journal of biological chemistry vol. 291,27 (2016): 14386-14387. doi: https://doi.org/10.1074/jbc.A115.699801
He Q, Wang F, Liu S, Zhu D, Cong H, Gao F, Li B, Wang H, Lin Z, Liao J, Gu L. Structural and biochemical insight into the mechanism of Rv2837c from Mycobacterium tuberculosis as a c-di-NMP phosphodiesterase. J Biol Chem. 2016 Jul 01;291(27):14386-14387. doi: 10.1074/jbc.A115.699801. PMID: 27371563; PMCID: PMC4933192.
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Myostatin induces DNA damage in skeletal muscle of streptozotocin-induced type 1 diabetic mice.

The Journal of biological chemistry

Sriram S, Subramanian S, Juvvuna PK, McFarlane C, Salerno MS, Kambadur R, Sharma M.
PMID: 26546691
J Biol Chem. 2015 Nov 06;290(45):27012. doi: 10.1074/jbc.A113.483115.

No abstract available.

Cite
Sriram S, Subramanian S, Juvvuna PK, et al. Myostatin induces DNA damage in skeletal muscle of streptozotocin-induced type 1 diabetic mice. J Biol Chem. 2015;290(45):27012doi: 10.1074/jbc.A113.483115.
Sriram, S., Subramanian, S., Juvvuna, P. K., McFarlane, C., Salerno, M. S., Kambadur, R., & Sharma, M. (2015). Myostatin induces DNA damage in skeletal muscle of streptozotocin-induced type 1 diabetic mice. The Journal of biological chemistry, 290(45), 27012. https://doi.org/10.1074/jbc.A113.483115
Sriram, Sandhya, et al. "Myostatin induces DNA damage in skeletal muscle of streptozotocin-induced type 1 diabetic mice." The Journal of biological chemistry vol. 290,45 (2015): 27012. doi: https://doi.org/10.1074/jbc.A113.483115
Sriram S, Subramanian S, Juvvuna PK, McFarlane C, Salerno MS, Kambadur R, Sharma M. Myostatin induces DNA damage in skeletal muscle of streptozotocin-induced type 1 diabetic mice. J Biol Chem. 2015 Nov 06;290(45):27012. doi: 10.1074/jbc.A113.483115. PMID: 26546691; PMCID: PMC4646411.
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Cytomegalovirus promoter up-regulation is the major cause of increased protein levels of unstable reporter proteins after treatment of living cells with proteasome inhibitors.

The Journal of biological chemistry

[No authors listed]
PMID: 27129194
J Biol Chem. 2016 Apr 22;291(17):8985. doi: 10.1074/jbc.A109.004101.

No abstract available.

Cite
Cytomegalovirus promoter up-regulation is the major cause of increased protein levels of unstable reporter proteins after treatment of living cells with proteasome inhibitors. J Biol Chem. 2016;291(17):8985doi: 10.1074/jbc.A109.004101.
(2016). Cytomegalovirus promoter up-regulation is the major cause of increased protein levels of unstable reporter proteins after treatment of living cells with proteasome inhibitors. The Journal of biological chemistry, 291(17), 8985. https://doi.org/10.1074/jbc.A109.004101
"Cytomegalovirus promoter up-regulation is the major cause of increased protein levels of unstable reporter proteins after treatment of living cells with proteasome inhibitors." The Journal of biological chemistry vol. 291,17 (2016): 8985. doi: https://doi.org/10.1074/jbc.A109.004101
Cytomegalovirus promoter up-regulation is the major cause of increased protein levels of unstable reporter proteins after treatment of living cells with proteasome inhibitors. J Biol Chem. 2016 Apr 22;291(17):8985. doi: 10.1074/jbc.A109.004101. PMID: 27129194; PMCID: PMC4861467.
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Mediator, TATA-binding protein, and RNA polymerase II contribute to low histone occupancy at active gene promoters in yeast.

The Journal of biological chemistry

Ansari SA, Paul E, Sommer S, Lieleg C, He Q, Daly AZ, Rode KA, Barber WT, Ellis LC, LaPorta E, Orzechowski AM, Taylor E, Reeb T, Wong J, Korber P, Morse RH.
PMID: 27197204
J Biol Chem. 2016 May 06;291(19):9938. doi: 10.1074/jbc.A113.529354.

No abstract available.

Cite
Ansari SA, Paul E, Sommer S, et al. Mediator, TATA-binding protein, and RNA polymerase II contribute to low histone occupancy at active gene promoters in yeast. J Biol Chem. 2016;291(19):9938doi: 10.1074/jbc.A113.529354.
Ansari, S. A., Paul, E., Sommer, S., Lieleg, C., He, Q., Daly, A. Z., Rode, K. A., Barber, W. T., Ellis, L. C., LaPorta, E., Orzechowski, A. M., Taylor, E., Reeb, T., Wong, J., Korber, P., & Morse, R. H. (2016). Mediator, TATA-binding protein, and RNA polymerase II contribute to low histone occupancy at active gene promoters in yeast. The Journal of biological chemistry, 291(19), 9938. https://doi.org/10.1074/jbc.A113.529354
Ansari, Suraiya A, et al. "Mediator, TATA-binding protein, and RNA polymerase II contribute to low histone occupancy at active gene promoters in yeast." The Journal of biological chemistry vol. 291,19 (2016): 9938. doi: https://doi.org/10.1074/jbc.A113.529354
Ansari SA, Paul E, Sommer S, Lieleg C, He Q, Daly AZ, Rode KA, Barber WT, Ellis LC, LaPorta E, Orzechowski AM, Taylor E, Reeb T, Wong J, Korber P, Morse RH. Mediator, TATA-binding protein, and RNA polymerase II contribute to low histone occupancy at active gene promoters in yeast. J Biol Chem. 2016 May 06;291(19):9938. doi: 10.1074/jbc.A113.529354. PMID: 27197204; PMCID: PMC4858997.
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Palmitoylation of MPP1 (membrane-palmitoylated protein 1)/p55 is crucial for lateral membrane organization in erythroid cells.

The Journal of biological chemistry

Łach A, Grzybek M, Heger E, Korycka J, Wolny M, Kubiak J, Kolondra A, Bogusławska DM, Augoff K, Majkowski M, Podkalicka J, Kaczor J, Stefanko A, Kuliczkowski K, Sikorski AF.
PMID: 29475958
J Biol Chem. 2018 Feb 23;293(8):2786. doi: 10.1074/jbc.W118.002209.

No abstract available.

Cite
Łach A, Grzybek M, Heger E, et al. Palmitoylation of MPP1 (membrane-palmitoylated protein 1)/p55 is crucial for lateral membrane organization in erythroid cells. J Biol Chem. 2018;293(8):2786doi: 10.1074/jbc.W118.002209.
Łach, A., Grzybek, M., Heger, E., Korycka, J., Wolny, M., Kubiak, J., Kolondra, A., Bogusławska, D. M., Augoff, K., Majkowski, M., Podkalicka, J., Kaczor, J., Stefanko, A., Kuliczkowski, K., & Sikorski, A. F. (2018). Palmitoylation of MPP1 (membrane-palmitoylated protein 1)/p55 is crucial for lateral membrane organization in erythroid cells. The Journal of biological chemistry, 293(8), 2786. https://doi.org/10.1074/jbc.W118.002209
Łach, Agnieszka, et al. "Palmitoylation of MPP1 (membrane-palmitoylated protein 1)/p55 is crucial for lateral membrane organization in erythroid cells." The Journal of biological chemistry vol. 293,8 (2018): 2786. doi: https://doi.org/10.1074/jbc.W118.002209
Łach A, Grzybek M, Heger E, Korycka J, Wolny M, Kubiak J, Kolondra A, Bogusławska DM, Augoff K, Majkowski M, Podkalicka J, Kaczor J, Stefanko A, Kuliczkowski K, Sikorski AF. Palmitoylation of MPP1 (membrane-palmitoylated protein 1)/p55 is crucial for lateral membrane organization in erythroid cells. J Biol Chem. 2018 Feb 23;293(8):2786. doi: 10.1074/jbc.W118.002209. PMID: 29475958; PMCID: PMC5827442.
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The ERK signaling cascade inhibits gonadotropin-stimulated steroidogenesis.

The Journal of biological chemistry

Seger R, Hanoch T, Rosenberg R, Dantes A, Merz WE, Strauss JF, Amsterdam A.
PMID: 28550133
J Biol Chem. 2017 May 26;292(21):8847. doi: 10.1074/jbc.A117.006852.

No abstract available.

Cite
Seger R, Hanoch T, Rosenberg R, et al. The ERK signaling cascade inhibits gonadotropin-stimulated steroidogenesis. J Biol Chem. 2017;292(21):8847doi: 10.1074/jbc.A117.006852.
Seger, R., Hanoch, T., Rosenberg, R., Dantes, A., Merz, W. E., Strauss, J. F., & Amsterdam, A. (2017). The ERK signaling cascade inhibits gonadotropin-stimulated steroidogenesis. The Journal of biological chemistry, 292(21), 8847. https://doi.org/10.1074/jbc.A117.006852
Seger, Rony, et al. "The ERK signaling cascade inhibits gonadotropin-stimulated steroidogenesis." The Journal of biological chemistry vol. 292,21 (2017): 8847. doi: https://doi.org/10.1074/jbc.A117.006852
Seger R, Hanoch T, Rosenberg R, Dantes A, Merz WE, Strauss JF, Amsterdam A. The ERK signaling cascade inhibits gonadotropin-stimulated steroidogenesis. J Biol Chem. 2017 May 26;292(21):8847. doi: 10.1074/jbc.A117.006852. PMID: 28550133; PMCID: PMC5448111.
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Showing 1 to 12 of 3505 entries