Results 21 to 30 of about 183 (125)

A substrate-bound structure of cyanobacterial biliverdin reductase identifies stacked substrates as critical for activity

Nature Communications, 2017
Biliverdin reductase (BVR) catalyses the last step in haem degradation. Here the authors present the crystal structure of cyanobacterial BVR bound to its substrate biliverdin and oxidised cofactor NADP+, which was used to propose the catalytic mechanism ...
Haruna Takao, Kei Hirabayashi, Yuki Nishigaya, Haruna Kouriki, Tetsuko Nakaniwa, Yoshinori Hagiwara, Jiro Harada, Hideaki Sato, Toshimasa Yamazaki, Yoichi Sakakibara, Masahito Suiko, Yujiro Asada, Yasuhiro Takahashi, Ken Yamamoto, Keiichi Fukuyama, Masakazu Sugishima, Kei Wada   +16 more
doaj   +1 more source

The Heme Oxygenase/Biliverdin Reductase System as Effector of the Neuroprotective Outcomes of Herb-Based Nutritional Supplements

Frontiers in Pharmacology, 2019
Over the last few years, several preclinical studies have shown that some herbal products, such as ferulic acid, Ginkgo biloba, and resveratrol, exert neuroprotective effects through the modulation of the heme oxygenase/biliverdin reductase system ...
Emanuela Mhillaj, Vincenzo Cuomo, Luigia Trabace, Cesare Mancuso, Cesare Mancuso   +4 more
doaj   +1 more source

The Role of Bilirubin and the Other “Yellow Players” in Neurodegenerative Diseases

Antioxidants, 2020
Bilirubin is a yellow endogenous derivate of the heme catabolism. Since the 1980s, it has been recognized as one of the most potent antioxidants in nature, able to counteract 10,000× higher intracellular concentrations of H2O2.
Sri Jayanti, Libor Vítek, Claudio Tiribelli, Silvia Gazzin   +3 more
doaj   +1 more source

Identifying structural and dynamic changes during the Biliverdin Reductase B catalytic cycle

Frontiers in Molecular Biosciences, 2023
Biliverdin Reductase B (BLVRB) is an NADPH-dependent reductase that catalyzes the reduction of multiple substrates and is therefore considered a critical cellular redox regulator.
Eunjeong Lee, Matthew J. McLeod, Jasmina S. Redzic, Barbara Marcolin, Robert E. Thorne, Pratul Agarwal, Elan Zohar Eisenmesser   +6 more
doaj   +1 more source

Biliverdin inhibits activation of NF‐κB: Reversal of inhibition by human biliverdin reductase [PDF]

International Journal of Cancer, 2007
AbstracthBVR functions in the cell as a reductase and as a kinase. In the first capacity, it reduces biliverdin, the product of HO activity, to the effective intracellular antioxidant, bilirubin; as a dual‐specificity kinase (S/T/Y) it activates the MAPK and IGF/IRK receptor signal transduction pathways. NF‐κB and the MAPK pathway are activated by ROS,
Peter E M, Gibbs, Mahin D, Maines
openaire   +2 more sources

Heme oxygenase-1 deficiency presenting with interstitial lung disease and hemophagocytic flares

Pediatric Rheumatology Online Journal, 2020
Background Heme oxygenase-1 (HMOX1) catalyzes the metabolism of heme into carbon monoxide, ferrous iron, and biliverdin. Through biliverdin reductase, biliverdin becomes bilirubin.
Alice S. Chau, Bonnie L. Cole, Jason S. Debley, Kabita Nanda, Aaron B. I. Rosen, Michael J. Bamshad, Deborah A. Nickerson, Troy R. Torgerson, Eric J. Allenspach   +8 more
doaj   +1 more source

Zika virus remodelled ER membranes contain proviral factors involved in redox and methylation pathways

Nature Communications, 2023
Zika virus (ZIKV) has emerged as a global health issue, yet neither antiviral therapy nor a vaccine are available. ZIKV is an enveloped RNA virus, replicating in the cytoplasm in close association with ER membranes.
Solène Denolly, Alexey Stukalov, Uladzimir Barayeu, Alina N. Rosinski, Paraskevi Kritsiligkou, Sebastian Joecks, Tobias P. Dick, Andreas Pichlmair, Ralf Bartenschlager   +8 more
doaj   +1 more source

Breakdown products of heme catabolism as senescence index in sea lamprey (Petromyzon marinus Linnaeus, 1758)

Frontiers in Marine Science, 2015
Biliverdin and bilirubin are breakdown products of normal heme catabolism, caused by the body's clearance of aged red blood cells which contain hemoglobin.
Sandra Barca, Sergio Silva, María José Servia   +2 more
doaj   +1 more source

Spectrophotometric Assessment of Heme Oxygenase-1 Activity in Leishmania-infected Macrophages

Bio-Protocol, 2020
Heme oxygenase-1 (HO-1) is a stress responsive enzyme that metabolizes heme and releases free iron, carbon monoxide (CO), and biliverdin (BV), which rapidly undergoes conversion to bilirubin (BL). Estimation of bilirubin is the basis of HO-1 assay.
Moumita Basu, Shriya Saha, Anindita Ukil
doaj   +1 more source

Reactive Oxygen Species (ROS) and Antioxidants as Immunomodulators in Exercise: Implications for Heme Oxygenase and Bilirubin

Antioxidants, 2022
Exercise is commonly prescribed as a lifestyle treatment for chronic metabolic diseases as it functions as an insulin sensitizer, cardio-protectant, and essential lifestyle tool for effective weight maintenance. Exercise boosts the production of reactive
David Travis Thomas, Nicholas R. DelCimmuto, Kyle D. Flack, David E. Stec, Terry D. Hinds   +4 more
doaj   +1 more source