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Showing 1 to 12 of 13 entries
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Murburn Concept: A Molecular Explanation for Hormetic and Idiosyncratic Dose Responses.

Dose-response : a publication of International Hormesis Society

Parashar A, Gideon DA, Manoj KM.
PMID: 29770107
Dose Response. 2018 May 09;16(2):1559325818774421. doi: 10.1177/1559325818774421. eCollection 2018.

Recently, electron transfers and catalyses in a bevy of redox reactions mediated by hemeproteins were explained by murburn concept. The term "murburn" is abstracted from "

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Parashar A, Gideon DA, Manoj KM. Murburn Concept: A Molecular Explanation for Hormetic and Idiosyncratic Dose Responses. Dose Response. 2018;16(2):1559325818774421doi: 10.1177/1559325818774421.
Parashar, A., Gideon, D. A., & Manoj, K. M. (2018). Murburn Concept: A Molecular Explanation for Hormetic and Idiosyncratic Dose Responses. Dose-response : a publication of International Hormesis Society, 16(2), 1559325818774421. https://doi.org/10.1177/1559325818774421
Parashar, Abhinav, et al. "Murburn Concept: A Molecular Explanation for Hormetic and Idiosyncratic Dose Responses." Dose-response : a publication of International Hormesis Society vol. 16,2 (2018): 1559325818774421. doi: https://doi.org/10.1177/1559325818774421
Parashar A, Gideon DA, Manoj KM. Murburn Concept: A Molecular Explanation for Hormetic and Idiosyncratic Dose Responses. Dose Response. 2018 May 09;16(2):1559325818774421. doi: 10.1177/1559325818774421. eCollection 2018. PMID: 29770107; PMCID: PMC5946624.
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Recent Approaches for Manipulating Globin Gene Expression in Treating Hemoglobinopathies.

Frontiers in genome editing

Mussolino C, Strouboulis J.
PMID: 34713248
Front Genome Ed. 2021 Aug 02;3:618111. doi: 10.3389/fgeed.2021.618111. eCollection 2021.

Tissue oxygenation throughout life depends on the activity of hemoglobin (Hb) one of the hemeproteins that binds oxygen in the lungs and secures its delivery throughout the body. Hb is composed of four monomers encoded by eight different genes...

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Mussolino C, Strouboulis J. Recent Approaches for Manipulating Globin Gene Expression in Treating Hemoglobinopathies. Front Genome Ed. 2021;3:618111doi: 10.3389/fgeed.2021.618111.
Mussolino, C., & Strouboulis, J. (2021). Recent Approaches for Manipulating Globin Gene Expression in Treating Hemoglobinopathies. Frontiers in genome editing, 3618111. https://doi.org/10.3389/fgeed.2021.618111
Mussolino, Claudio, and Strouboulis, John. "Recent Approaches for Manipulating Globin Gene Expression in Treating Hemoglobinopathies." Frontiers in genome editing vol. 3 (2021): 618111. doi: https://doi.org/10.3389/fgeed.2021.618111
Mussolino C, Strouboulis J. Recent Approaches for Manipulating Globin Gene Expression in Treating Hemoglobinopathies. Front Genome Ed. 2021 Aug 02;3:618111. doi: 10.3389/fgeed.2021.618111. eCollection 2021. PMID: 34713248; PMCID: PMC8525358.
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Rational Design of Novel Pyridinol-Fused Ring Acetaminophen Analogues.

ACS medicinal chemistry letters

Shchepin RV, Liu W, Yin H, Zagol-Ikapitte I, Amin T, Jeong BS, Roberts LJ, Oates JA, Porter NA, Boutaud O.
PMID: 24482730
ACS Med Chem Lett. 2013 Aug 08;4(8):710-714. doi: 10.1021/ml4000904.

Acetaminophen (ApAP) is an electron donor capable of reducing radicals generated by redox cycling of hemeproteins. It acts on the prostaglandin H synthases (cyclooxygenases; COXs) to reduce the protoporphyrin radical cation in the peroxidase site of the enzyme, thus...

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Shchepin RV, Liu W, Yin H, et al. Rational Design of Novel Pyridinol-Fused Ring Acetaminophen Analogues. ACS Med Chem Lett. 2013;4(8):710-714doi: 10.1021/ml4000904.
Shchepin, R. V., Liu, W., Yin, H., Zagol-Ikapitte, I., Amin, T., Jeong, B. S., Roberts, L. J., Oates, J. A., Porter, N. A., & Boutaud, O. (2013). Rational Design of Novel Pyridinol-Fused Ring Acetaminophen Analogues. ACS medicinal chemistry letters, 4(8), 710-714. https://doi.org/10.1021/ml4000904
Shchepin, Roman V, et al. "Rational Design of Novel Pyridinol-Fused Ring Acetaminophen Analogues." ACS medicinal chemistry letters vol. 4,8 (2013): 710-714. doi: https://doi.org/10.1021/ml4000904
Shchepin RV, Liu W, Yin H, Zagol-Ikapitte I, Amin T, Jeong BS, Roberts LJ, Oates JA, Porter NA, Boutaud O. Rational Design of Novel Pyridinol-Fused Ring Acetaminophen Analogues. ACS Med Chem Lett. 2013 Aug 08;4(8):710-714. doi: 10.1021/ml4000904. PMID: 24482730; PMCID: PMC3904457.
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Alternate Heme Ligation Steers Activity and Selectivity in Engineered Cytochrome P450-Catalyzed Carbene-Transfer Reactions.

Journal of the American Chemical Society

Chen K, Zhang SQ, Brandenberg OF, Hong X, Arnold FH.
PMID: 30372623
J Am Chem Soc. 2018 Dec 05;140(48):16402-16407. doi: 10.1021/jacs.8b09613. Epub 2018 Nov 01.

We report a biocatalytic platform of engineered cytochrome P450 enzymes to carry out carbene-transfer reactions using a lactone-based carbene precursor. By simply altering the heme-ligating residue, we obtained two enzymes that catalyze olefin cyclopropanation (Ser) or S-H bond insertion...

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Chen K, Zhang SQ, Brandenberg OF, et al. Alternate Heme Ligation Steers Activity and Selectivity in Engineered Cytochrome P450-Catalyzed Carbene-Transfer Reactions. J Am Chem Soc. 2018;140(48):16402-16407doi: 10.1021/jacs.8b09613.
Chen, K., Zhang, S. Q., Brandenberg, O. F., Hong, X., & Arnold, F. H. (2018). Alternate Heme Ligation Steers Activity and Selectivity in Engineered Cytochrome P450-Catalyzed Carbene-Transfer Reactions. Journal of the American Chemical Society, 140(48), 16402-16407. https://doi.org/10.1021/jacs.8b09613
Chen, Kai, et al. "Alternate Heme Ligation Steers Activity and Selectivity in Engineered Cytochrome P450-Catalyzed Carbene-Transfer Reactions." Journal of the American Chemical Society vol. 140,48 (2018): 16402-16407. doi: https://doi.org/10.1021/jacs.8b09613
Chen K, Zhang SQ, Brandenberg OF, Hong X, Arnold FH. Alternate Heme Ligation Steers Activity and Selectivity in Engineered Cytochrome P450-Catalyzed Carbene-Transfer Reactions. J Am Chem Soc. 2018 Dec 05;140(48):16402-16407. doi: 10.1021/jacs.8b09613. Epub 2018 Nov 01. PMID: 30372623.
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Heme on innate immunity and inflammation.

Frontiers in pharmacology

Dutra FF, Bozza MT.
PMID: 24904418
Front Pharmacol. 2014 May 27;5:115. doi: 10.3389/fphar.2014.00115. eCollection 2014.

Heme is an essential molecule expressed ubiquitously all through our tissues. Heme plays major functions in cellular physiology and metabolism as the prosthetic group of diverse proteins. Once released from cells and from hemeproteins free heme causes oxidative damage...

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Dutra FF, Bozza MT. Heme on innate immunity and inflammation. Front Pharmacol. 2014;5:115doi: 10.3389/fphar.2014.00115.
Dutra, F. F., & Bozza, M. T. (2014). Heme on innate immunity and inflammation. Frontiers in pharmacology, 5115. https://doi.org/10.3389/fphar.2014.00115
Dutra, Fabianno F, and Bozza, Marcelo T. "Heme on innate immunity and inflammation." Frontiers in pharmacology vol. 5 (2014): 115. doi: https://doi.org/10.3389/fphar.2014.00115
Dutra FF, Bozza MT. Heme on innate immunity and inflammation. Front Pharmacol. 2014 May 27;5:115. doi: 10.3389/fphar.2014.00115. eCollection 2014. PMID: 24904418; PMCID: PMC4035012.
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SAXS structure of homodimeric oxyHemoglobin III from bivalve Lucina pectinata.

Biopolymers

Marchany-Rivera D, Estremera-Andújar RA, Nieves-Marrero C, Ruiz-Martínez CR, Bauer W, López-Garriga J.
PMID: 33792032
Biopolymers. 2021 Jun;112(6):e23427. doi: 10.1002/bip.23427. Epub 2021 Apr 01.

Hemoglobin III (HbIII) is one of the two oxygen reactive hemoproteins present in the bivalve, Lucina pectinata. The clam inhabits a sulfur-rich environment and HbIII is the only hemoprotein present in the system which does not yet have a...

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Marchany-Rivera D, Estremera-Andújar RA, Nieves-Marrero C, et al. SAXS structure of homodimeric oxyHemoglobin III from bivalve Lucina pectinata. Biopolymers. 2021;112(6):e23427doi: 10.1002/bip.23427.
Marchany-Rivera, D., Estremera-Andújar, R. A., Nieves-Marrero, C., Ruiz-Martínez, C. R., Bauer, W., & López-Garriga, J. (2021). SAXS structure of homodimeric oxyHemoglobin III from bivalve Lucina pectinata. Biopolymers, 112(6), e23427. https://doi.org/10.1002/bip.23427
Marchany-Rivera, Darya, et al. "SAXS structure of homodimeric oxyHemoglobin III from bivalve Lucina pectinata." Biopolymers vol. 112,6 (2021): e23427. doi: https://doi.org/10.1002/bip.23427
Marchany-Rivera D, Estremera-Andújar RA, Nieves-Marrero C, Ruiz-Martínez CR, Bauer W, López-Garriga J. SAXS structure of homodimeric oxyHemoglobin III from bivalve Lucina pectinata. Biopolymers. 2021 Jun;112(6):e23427. doi: 10.1002/bip.23427. Epub 2021 Apr 01. PMID: 33792032; PMCID: PMC8265735.
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Mechanisms of Neuronal Damage in Acute Hepatic Porphyrias.

Diagnostics (Basel, Switzerland)

Ricci A, Di Pierro E, Marcacci M, Ventura P.
PMID: 34943446
Diagnostics (Basel). 2021 Nov 26;11(12). doi: 10.3390/diagnostics11122205.

Porphyrias are a group of congenital and acquired diseases caused by an enzymatic impairment in the biosynthesis of heme. Depending on the specific enzyme involved, different types of porphyrias (i.e., chronic vs. acute, cutaneous vs. neurovisceral, hepatic vs. erythropoietic)...

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Ricci A, Di Pierro E, Marcacci M, et al. Mechanisms of Neuronal Damage in Acute Hepatic Porphyrias. Diagnostics (Basel). 2021;11(12)doi: 10.3390/diagnostics11122205.
Ricci, A., Di Pierro, E., Marcacci, M., & Ventura, P. (2021). Mechanisms of Neuronal Damage in Acute Hepatic Porphyrias. Diagnostics (Basel, Switzerland), 11(12), . https://doi.org/10.3390/diagnostics11122205
Ricci, Andrea, et al. "Mechanisms of Neuronal Damage in Acute Hepatic Porphyrias." Diagnostics (Basel, Switzerland) vol. 11,12 (2021). doi: https://doi.org/10.3390/diagnostics11122205
Ricci A, Di Pierro E, Marcacci M, Ventura P. Mechanisms of Neuronal Damage in Acute Hepatic Porphyrias. Diagnostics (Basel). 2021 Nov 26;11(12). doi: 10.3390/diagnostics11122205. PMID: 34943446; PMCID: PMC8700611.
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Hemeprotein amplifies the innate immune receptors of Ctenopharyngodon idellus kidney cells through NF-κB- and MAPK-dependent reactive oxygen species generation.

Developmental and comparative immunology

Lu Z, Tang M, Zhang M, Li Y, Shi F, Zhan F, Zhao L, Li J, Lin L, Qin Z.
PMID: 34273355
Dev Comp Immunol. 2022 Jan;126:104207. doi: 10.1016/j.dci.2021.104207. Epub 2021 Jul 15.

Infectious bacterial and viral diseases that cause hemolysis are considered life-threatening to grass carp (Ctenopharyngodon idellus), which is a species used in aquaculture worldwide. After heme and hemeproteins (Hb) are released as a result of hemolysis, the effect of...

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Lu Z, Tang M, Zhang M, et al. Hemeprotein amplifies the innate immune receptors of Ctenopharyngodon idellus kidney cells through NF-κB- and MAPK-dependent reactive oxygen species generation. Dev Comp Immunol. 2021;126:104207doi: 10.1016/j.dci.2021.104207.
Lu, Z., Tang, M., Zhang, M., Li, Y., Shi, F., Zhan, F., Zhao, L., Li, J., Lin, L., & Qin, Z. (2022). Hemeprotein amplifies the innate immune receptors of Ctenopharyngodon idellus kidney cells through NF-κB- and MAPK-dependent reactive oxygen species generation. Developmental and comparative immunology, 126104207. https://doi.org/10.1016/j.dci.2021.104207
Lu, Zhijie, et al. "Hemeprotein amplifies the innate immune receptors of Ctenopharyngodon idellus kidney cells through NF-κB- and MAPK-dependent reactive oxygen species generation." Developmental and comparative immunology vol. 126 (2022): 104207. doi: https://doi.org/10.1016/j.dci.2021.104207
Lu Z, Tang M, Zhang M, Li Y, Shi F, Zhan F, Zhao L, Li J, Lin L, Qin Z. Hemeprotein amplifies the innate immune receptors of Ctenopharyngodon idellus kidney cells through NF-κB- and MAPK-dependent reactive oxygen species generation. Dev Comp Immunol. 2022 Jan;126:104207. doi: 10.1016/j.dci.2021.104207. Epub 2021 Jul 15. PMID: 34273355.
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Hyperspectral absorption microscopy using photoacoustic remote sensing.

Optics express

Bell K, Mukhangaliyeva L, Khalili L, Haji Reza P.
PMID: 34614681
Opt Express. 2021 Jul 19;29(15):24338-24348. doi: 10.1364/OE.430403.

An improved method of remote optical absorption spectroscopy and hyperspectral optical absorption imaging is described which takes advantage of the photoacoustic remote sensing detection architecture. A wide collection of photoacoustic excitation wavelengths ranging from 210 nm to 1550 nm...

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Bell K, Mukhangaliyeva L, Khalili L, et al. Hyperspectral absorption microscopy using photoacoustic remote sensing. Opt Express. 2021;29(15):24338-24348doi: 10.1364/OE.430403.
Bell, K., Mukhangaliyeva, L., Khalili, L., & Haji Reza, P. (2021). Hyperspectral absorption microscopy using photoacoustic remote sensing. Optics express, 29(15), 24338-24348. https://doi.org/10.1364/OE.430403
Bell, Kevan, et al. "Hyperspectral absorption microscopy using photoacoustic remote sensing." Optics express vol. 29,15 (2021): 24338-24348. doi: https://doi.org/10.1364/OE.430403
Bell K, Mukhangaliyeva L, Khalili L, Haji Reza P. Hyperspectral absorption microscopy using photoacoustic remote sensing. Opt Express. 2021 Jul 19;29(15):24338-24348. doi: 10.1364/OE.430403. PMID: 34614681.
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Hemoproteins-nickel foam hybrids as effective supercapacitors.

Chemical communications (Cambridge, England)

Khairy M, El-Safty SA.
PMID: 24346228
Chem Commun (Camb). 2014 Feb 09;50(11):1356-8. doi: 10.1039/c3cc48155g.

The immobilization of hemeproteins onto a nickel foam electrode was developed for the first time, and the electrode exhibits remarkable electrochemical performance with higher capacitance and stability compared to synthetic pseudocapacitors.

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Khairy M, El-Safty SA. Hemoproteins-nickel foam hybrids as effective supercapacitors. Chem Commun (Camb). 2014;50(11):1356-8doi: 10.1039/c3cc48155g.
Khairy, M., & El-Safty, S. A. (2014). Hemoproteins-nickel foam hybrids as effective supercapacitors. Chemical communications (Cambridge, England), 50(11), 1356-8. https://doi.org/10.1039/c3cc48155g
Khairy, Mohamed, and El-Safty, Sherif A. "Hemoproteins-nickel foam hybrids as effective supercapacitors." Chemical communications (Cambridge, England) vol. 50,11 (2014): 1356-8. doi: https://doi.org/10.1039/c3cc48155g
Khairy M, El-Safty SA. Hemoproteins-nickel foam hybrids as effective supercapacitors. Chem Commun (Camb). 2014 Feb 09;50(11):1356-8. doi: 10.1039/c3cc48155g. PMID: 24346228.
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Mechanisms of Neuronal Damage in Acute Hepatic Porphyrias.

Diagnostics (Basel, Switzerland)

Ricci A, Di Pierro E, Marcacci M, Ventura P.
PMID: 34943446
Diagnostics (Basel). 2021 Nov 26;11(12). doi: 10.3390/diagnostics11122205.

Porphyrias are a group of congenital and acquired diseases caused by an enzymatic impairment in the biosynthesis of heme. Depending on the specific enzyme involved, different types of porphyrias (i.e., chronic vs. acute, cutaneous vs. neurovisceral, hepatic vs. erythropoietic)...

Cite
Ricci A, Di Pierro E, Marcacci M, et al. Mechanisms of Neuronal Damage in Acute Hepatic Porphyrias. Diagnostics (Basel). 2021;11(12)doi: 10.3390/diagnostics11122205.
Ricci, A., Di Pierro, E., Marcacci, M., & Ventura, P. (2021). Mechanisms of Neuronal Damage in Acute Hepatic Porphyrias. Diagnostics (Basel, Switzerland), 11(12), . https://doi.org/10.3390/diagnostics11122205
Ricci, Andrea, et al. "Mechanisms of Neuronal Damage in Acute Hepatic Porphyrias." Diagnostics (Basel, Switzerland) vol. 11,12 (2021). doi: https://doi.org/10.3390/diagnostics11122205
Ricci A, Di Pierro E, Marcacci M, Ventura P. Mechanisms of Neuronal Damage in Acute Hepatic Porphyrias. Diagnostics (Basel). 2021 Nov 26;11(12). doi: 10.3390/diagnostics11122205. PMID: 34943446.
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Extremely weak linear electron-phonon coupling in iron-free hemeproteins studied by phase-modulated photon echo.

Physical review. B, Condensed matter

Kushida T, Lin JW, Saikan S, Tada T, Tani T.
PMID: 9998647
Phys Rev B Condens Matter. 1991 Oct 01;44(14):7356-7361. doi: 10.1103/physrevb.44.7356.

No abstract available.

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Kushida T, Lin JW, Saikan S, et al. Extremely weak linear electron-phonon coupling in iron-free hemeproteins studied by phase-modulated photon echo. Phys Rev B Condens Matter. 1991;44(14):7356-7361doi: 10.1103/physrevb.44.7356.
Kushida, T., Lin, J. W., Saikan, S., Tada, T., & Tani, T. (1991). Extremely weak linear electron-phonon coupling in iron-free hemeproteins studied by phase-modulated photon echo. Physical review. B, Condensed matter, 44(14), 7356-7361. https://doi.org/10.1103/physrevb.44.7356
Kushida, et al. "Extremely weak linear electron-phonon coupling in iron-free hemeproteins studied by phase-modulated photon echo." Physical review. B, Condensed matter vol. 44,14 (1991): 7356-7361. doi: https://doi.org/10.1103/physrevb.44.7356
Kushida T, Lin JW, Saikan S, Tada T, Tani T. Extremely weak linear electron-phonon coupling in iron-free hemeproteins studied by phase-modulated photon echo. Phys Rev B Condens Matter. 1991 Oct 01;44(14):7356-7361. doi: 10.1103/physrevb.44.7356. PMID: 9998647.
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