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Role of adaptor proteins in secretory granule biogenesis and maturation.

Frontiers in endocrinology

Bonnemaison ML, Eipper BA, Mains RE.
PMID: 23966980
Front Endocrinol (Lausanne). 2013 Aug 14;4:101. doi: 10.3389/fendo.2013.00101. eCollection 2013.

In the regulated secretory pathway, secretory granules (SGs) store peptide hormones that are released on demand. SGs are formed at the trans-Golgi network and must undergo a maturation process to become responsive to secretagogues. The production of mature SGs...

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Bonnemaison ML, Eipper BA, Mains RE. Role of adaptor proteins in secretory granule biogenesis and maturation. Front Endocrinol (Lausanne). 2013;4:101doi: 10.3389/fendo.2013.00101.
Bonnemaison, M. L., Eipper, B. A., & Mains, R. E. (2013). Role of adaptor proteins in secretory granule biogenesis and maturation. Frontiers in endocrinology, 4101. https://doi.org/10.3389/fendo.2013.00101
Bonnemaison, Mathilde L, et al. "Role of adaptor proteins in secretory granule biogenesis and maturation." Frontiers in endocrinology vol. 4 (2013): 101. doi: https://doi.org/10.3389/fendo.2013.00101
Bonnemaison ML, Eipper BA, Mains RE. Role of adaptor proteins in secretory granule biogenesis and maturation. Front Endocrinol (Lausanne). 2013 Aug 14;4:101. doi: 10.3389/fendo.2013.00101. eCollection 2013. PMID: 23966980; PMCID: PMC3743005.
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Effects of copper occupancy on the conformational landscape of peptidylglycine α-hydroxylating monooxygenase.

Communications biology

Maheshwari S, Shimokawa C, Rudzka K, Kline CD, Eipper BA, Mains RE, Gabelli SB, Blackburn N, Amzel LM.
PMID: 30271955
Commun Biol. 2018 Jun 25;1:74. doi: 10.1038/s42003-018-0082-y. eCollection 2018.

The structures of metalloproteins that use redox-active metals for catalysis are usually exquisitely folded in a way that they are prearranged to accept their metal cofactors. Peptidylglycine α-hydroxylating monooxygenase (PHM) is a dicopper enzyme that catalyzes hydroxylation of the...

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Maheshwari S, Shimokawa C, Rudzka K, et al. Effects of copper occupancy on the conformational landscape of peptidylglycine α-hydroxylating monooxygenase. Commun Biol. 2018;1:74doi: 10.1038/s42003-018-0082-y.
Maheshwari, S., Shimokawa, C., Rudzka, K., Kline, C. D., Eipper, B. A., Mains, R. E., Gabelli, S. B., Blackburn, N., & Amzel, L. M. (2018). Effects of copper occupancy on the conformational landscape of peptidylglycine α-hydroxylating monooxygenase. Communications biology, 174. https://doi.org/10.1038/s42003-018-0082-y
Maheshwari, Sweta, et al. "Effects of copper occupancy on the conformational landscape of peptidylglycine α-hydroxylating monooxygenase." Communications biology vol. 1 (2018): 74. doi: https://doi.org/10.1038/s42003-018-0082-y
Maheshwari S, Shimokawa C, Rudzka K, Kline CD, Eipper BA, Mains RE, Gabelli SB, Blackburn N, Amzel LM. Effects of copper occupancy on the conformational landscape of peptidylglycine α-hydroxylating monooxygenase. Commun Biol. 2018 Jun 25;1:74. doi: 10.1038/s42003-018-0082-y. eCollection 2018. PMID: 30271955; PMCID: PMC6123673.
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PERK-mediated expression of peptidylglycine α-amidating monooxygenase supports angiogenesis in glioblastoma.

Oncogenesis

Soni H, Bode J, Nguyen CDL, Puccio L, Neßling M, Piro RM, Bub J, Phillips E, Ahrends R, Eipper BA, Tews B, Goidts V.
PMID: 32054826
Oncogenesis. 2020 Feb 13;9(2):18. doi: 10.1038/s41389-020-0201-8.

PKR-like kinase (PERK) plays a significant role in inducing angiogenesis in various cancer types including glioblastoma. By proteomics analysis of the conditioned medium from a glioblastoma cell line treated with a PERK inhibitor, we showed that peptidylglycine α-amidating monooxygenase...

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Soni H, Bode J, Nguyen CDL, et al. PERK-mediated expression of peptidylglycine α-amidating monooxygenase supports angiogenesis in glioblastoma. Oncogenesis. 2020;9(2):18doi: 10.1038/s41389-020-0201-8.
Soni, H., Bode, J., Nguyen, C. D. L., Puccio, L., Neßling, M., Piro, R. M., Bub, J., Phillips, E., Ahrends, R., Eipper, B. A., Tews, B., & Goidts, V. (2020). PERK-mediated expression of peptidylglycine α-amidating monooxygenase supports angiogenesis in glioblastoma. Oncogenesis, 9(2), 18. https://doi.org/10.1038/s41389-020-0201-8
Soni, Himanshu, et al. "PERK-mediated expression of peptidylglycine α-amidating monooxygenase supports angiogenesis in glioblastoma." Oncogenesis vol. 9,2 (2020): 18. doi: https://doi.org/10.1038/s41389-020-0201-8
Soni H, Bode J, Nguyen CDL, Puccio L, Neßling M, Piro RM, Bub J, Phillips E, Ahrends R, Eipper BA, Tews B, Goidts V. PERK-mediated expression of peptidylglycine α-amidating monooxygenase supports angiogenesis in glioblastoma. Oncogenesis. 2020 Feb 13;9(2):18. doi: 10.1038/s41389-020-0201-8. PMID: 32054826; PMCID: PMC7018722.
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Proteases Shape the .

Proteomes

Luxmi R, Blaby-Haas C, Kumar D, Rauniyar N, King SM, Mains RE, Eipper BA.
PMID: 30249063
Proteomes. 2018 Sep 23;6(4). doi: 10.3390/proteomes6040036.

The recent identification of catalytically active peptidylglycine α-amidating monooxygenase (PAM) in Chlamydomonas reinhardtii, a unicellular green alga, suggested the presence of a PAM-like gene and peptidergic signaling in the last eukaryotic common ancestor (LECA). We identified prototypical neuropeptide precursors...

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Luxmi R, Blaby-Haas C, Kumar D, et al. Proteases Shape the . Proteomes. 2018;6(4)doi: 10.3390/proteomes6040036.
Luxmi, R., Blaby-Haas, C., Kumar, D., Rauniyar, N., King, S. M., Mains, R. E., & Eipper, B. A. (2018). Proteases Shape the . Proteomes, 6(4), . https://doi.org/10.3390/proteomes6040036
Luxmi, Raj, et al. "Proteases Shape the ." Proteomes vol. 6,4 (2018). doi: https://doi.org/10.3390/proteomes6040036
Luxmi R, Blaby-Haas C, Kumar D, Rauniyar N, King SM, Mains RE, Eipper BA. Proteases Shape the . Proteomes. 2018 Sep 23;6(4). doi: 10.3390/proteomes6040036. PMID: 30249063; PMCID: PMC6313938.
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Synaptic plasticity, a symphony in GEF.

ACS chemical neuroscience

Kiraly DD, Eipper-Mains JE, Mains RE, Eipper BA.
PMID: 20543890
ACS Chem Neurosci. 2010 May 19;1(5):348-365. doi: 10.1021/cn100012x.

Dendritic spines are the postsynaptic sites for the majority of excitatory synapses in the mammalian forebrain. While many spines display great stability, others change shape in a matter of seconds to minutes. These rapid alterations in dendritic spine number...

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Kiraly DD, Eipper-Mains JE, Mains RE, et al. Synaptic plasticity, a symphony in GEF. ACS Chem Neurosci. 2010;1(5):348-365doi: 10.1021/cn100012x.
Kiraly, D. D., Eipper-Mains, J. E., Mains, R. E., & Eipper, B. A. (2010). Synaptic plasticity, a symphony in GEF. ACS chemical neuroscience, 1(5), 348-365. https://doi.org/10.1021/cn100012x
Kiraly, Drew D, et al. "Synaptic plasticity, a symphony in GEF." ACS chemical neuroscience vol. 1,5 (2010): 348-365. doi: https://doi.org/10.1021/cn100012x
Kiraly DD, Eipper-Mains JE, Mains RE, Eipper BA. Synaptic plasticity, a symphony in GEF. ACS Chem Neurosci. 2010 May 19;1(5):348-365. doi: 10.1021/cn100012x. PMID: 20543890; PMCID: PMC2882301.
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Showing 1 to 5 of 5 entries