Biliverdin (BioDeep_00000003103)

 

Secondary id: BioDeep_00000229671, BioDeep_00000307699

human metabolite Endogenous BioNovoGene_Lab2019


代谢物信息卡片


3-(2-{[(2Z)-3-(2-carboxyethyl)-5-{[(2Z)-4-ethenyl-3-methyl-5-oxo-2,5-dihydro-1H-pyrrol-2-ylidene]methyl}-4-methyl-2H-pyrrol-2-ylidene]methyl}-5-{[(2Z)-3-ethenyl-4-methyl-5-oxo-2,5-dihydro-1H-pyrrol-2-ylidene]methyl}-4-methyl-1H-pyrrol-3-yl)propanoic acid

化学式: C33H34N4O6 (582.2478)
中文名称: 胆绿素
谱图信息: 最多检出来源 Homo sapiens(lipidsearch) 22.73%

Reviewed

Last reviewed on 2024-07-01.

Cite this Page

Biliverdin. BioDeep Database v3. PANOMIX ltd, a top metabolomics service provider from China. https://query.biodeep.cn/s/biliverdin (retrieved 2024-12-27) (BioDeep RN: BioDeep_00000003103). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0).

分子结构信息

SMILES: C=CC1=C(C)C(=CC2=NC(=Cc3[nH]c(C=C4NC(=O)C(C)=C4C=C)c(C)c3CCC(=O)O)C(CCC(=O)O)=C2C)NC1=O
InChI: InChI=1S/C33H34N4O6/c1-7-20-19(6)32(42)37-27(20)14-25-18(5)23(10-12-31(40)41)29(35-25)15-28-22(9-11-30(38)39)17(4)24(34-28)13-26-16(3)21(8-2)33(43)36-26/h7-8,13-15,34-35H,1-2,9-12H2,3-6H3,(H,37,42)(H,38,39)(H,40,41)/b24-13+,27-14-,28-15-

描述信息

Biliverdin is a green pigment formed as a byproduct of hemoglobin breakdown. It consists of four linearly connected pyrrole rings (a tetrapyrrole). Biliverdin is formed when the heme group in hemoglobin is cleaved at its alpha-methene bridge. The resulting biliverdin is then reduced to bilirubin, a yellow pigment, by the enzyme biliverdin reductase. The changing color of a bruise from deep purple to yellow over time is a graphical indicator of this reaction. Biosynthesized from hemoglobin as a precursor of bilirubin. Occurs in the bile of amphibia and of birds, but not in normal human bile or serum. [HMDB]
Biliverdin is a green pigment formed as a byproduct of hemoglobin breakdown. It consists of four linearly connected pyrrole rings (a tetrapyrrole). Biliverdin is formed when the heme group in hemoglobin is cleaved at its alpha-methene bridge. The resulting biliverdin is then reduced to bilirubin, a yellow pigment, by the enzyme biliverdin reductase. The changing color of a bruise from deep purple to yellow over time is a graphical indicator of this reaction. Biliverdin occurs in the bile of amphibia and of birds, but not in normal human bile or serum.

Biliverdin. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=114-25-0 (retrieved 2024-07-01) (CAS RN: 114-25-0). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0).

同义名列表

18 个代谢物同义名

3-(2-{[(2Z)-3-(2-carboxyethyl)-5-{[(2Z)-4-ethenyl-3-methyl-5-oxo-2,5-dihydro-1H-pyrrol-2-ylidene]methyl}-4-methyl-2H-pyrrol-2-ylidene]methyl}-5-{[(2Z)-3-ethenyl-4-methyl-5-oxo-2,5-dihydro-1H-pyrrol-2-ylidene]methyl}-4-methyl-1H-pyrrol-3-yl)propanoic acid; 8,12-Bis(2-carboxyethyl)-2,7,13,17-tetramethyl-3,18-divinylbilin-1(19)(21H,24H)-dione; 1,3,6,7-Tetramethyl-4,5-dicarboxyethyl-2,8-divinylbilenone; BILIVERDINE IX ALPHA; Biliverdin IX alpha; Protobiliverdin IX; Biliverdin ixalpha; BILIVERDINE IX α; Dehydrobilirubin; BILIVERDINE IX a; Biliverdin IX a; Biliverdin IX α; Biliverdin IX; Uteroverdine; Biliverdine; biliverdin; Biliverdin; Biliverdin



数据库引用编号

25 个数据库交叉引用编号

分类词条

相关代谢途径

Reactome(0)

BioCyc(0)

PlantCyc(0)

代谢反应

24 个相关的代谢反应过程信息。

Reactome(5)

BioCyc(0)

WikiPathways(0)

Plant Reactome(0)

INOH(0)

PlantCyc(0)

COVID-19 Disease Map(1)

PathBank(18)

PharmGKB(0)

3 个相关的物种来源信息

在这里通过桑基图来展示出与当前的这个代谢物在我们的BioDeep知识库中具有相关联信息的其他代谢物。在这里进行关联的信息来源主要有:

  • PubMed: 来源于PubMed文献库中的文献信息,我们通过自然语言数据挖掘得到的在同一篇文献中被同时提及的相关代谢物列表,这个列表按照代谢物同时出现的文献数量降序排序,取前10个代谢物作为相关研究中关联性很高的代谢物集合展示在桑基图中。
  • NCBI Taxonomy: 通过文献数据挖掘,得到的代谢物物种来源信息关联。这个关联信息同样按照出现的次数降序排序,取前10个代谢物作为高关联度的代谢物集合展示在桑吉图上。
  • Chemical Taxonomy: 在物质分类上处于同一个分类集合中的其他代谢物
  • Chemical Reaction: 在化学反应过程中,存在为当前代谢物相关联的生化反应过程中的反应底物或者反应产物的关联代谢物信息。

点击图上的相关代谢物的名称,可以跳转到相关代谢物的信息页面。

亚细胞结构定位 关联基因列表
Cytoplasm 11 ALB, ANG, MAPK14, MARK2, NFE2L2, NFKB1, NOS2, PTGS2, TLR4, TNK1, XDH
Peripheral membrane protein 3 CYP1B1, PTGS2, TNK1
Endosome membrane 1 TLR4
Endoplasmic reticulum membrane 4 CYP1B1, HMOX1, PTGDS, PTGS2
Nucleus 9 ALB, ANG, HMOX1, MAPK14, MPO, NFE2L2, NFKB1, NOS2, PPARA
cytosol 9 ALB, ANG, HMOX1, MAPK14, MB, NFE2L2, NFKB1, NOS2, XDH
dendrite 1 MARK2
centrosome 2 ALB, NFE2L2
nucleoplasm 8 HMOX1, MAPK14, MARK2, MPO, NFE2L2, NFKB1, NOS2, PPARA
RNA polymerase II transcription regulator complex 1 NFE2L2
Cell membrane 2 TLR4, TNF
Cytoplasmic side 1 HMOX1
cell surface 2 TLR4, TNF
glutamatergic synapse 1 MAPK14
Golgi apparatus 3 ALB, NFE2L2, PTGDS
growth cone 1 ANG
neuronal cell body 2 ANG, TNF
Cytoplasm, cytosol 2 NFE2L2, NOS2
Lysosome 1 MPO
plasma membrane 6 MARK2, NFE2L2, NOS2, TLR4, TNF, TNK1
Membrane 5 CYP1B1, HMOX1, MARK2, TLR4, TNK1
caveola 1 PTGS2
extracellular exosome 4 ALB, MB, MPO, PTGDS
endoplasmic reticulum 3 ALB, HMOX1, PTGS2
extracellular space 9 ALB, ANG, CXCL8, HMOX1, IL6, MPO, PTGDS, TNF, XDH
perinuclear region of cytoplasm 4 HMOX1, NOS2, PTGDS, TLR4
mitochondrion 4 CYP1B1, MAPK14, MARK2, NFKB1
protein-containing complex 2 ALB, PTGS2
intracellular membrane-bounded organelle 2 CYP1B1, MPO
Microsome membrane 2 CYP1B1, PTGS2
Single-pass type I membrane protein 1 TLR4
Secreted 5 ALB, ANG, CXCL8, IL6, PTGDS
extracellular region 9 ALB, ANG, CXCL8, IL6, MAPK14, MPO, NFKB1, PTGDS, TNF
mitochondrial outer membrane 1 HMOX1
anchoring junction 1 ALB
transcription regulator complex 1 NFKB1
Nucleus membrane 1 PTGDS
nuclear membrane 1 PTGDS
external side of plasma membrane 2 TLR4, TNF
actin cytoskeleton 1 ANG
nucleolus 1 ANG
sarcoplasm 1 MB
Cytoplasm, P-body 1 NOS2
P-body 1 NOS2
Early endosome 1 TLR4
recycling endosome 1 TNF
Single-pass type II membrane protein 1 TNF
Cytoplasm, perinuclear region 2 NOS2, PTGDS
Membrane raft 1 TNF
Peroxisome 2 NOS2, XDH
basement membrane 1 ANG
sarcoplasmic reticulum 1 XDH
peroxisomal matrix 1 NOS2
secretory granule 1 MPO
lateral plasma membrane 1 MARK2
nuclear speck 1 MAPK14
Nucleus inner membrane 1 PTGS2
Nucleus outer membrane 1 PTGS2
nuclear inner membrane 1 PTGS2
nuclear outer membrane 1 PTGS2
Cell projection, ruffle 1 TLR4
ruffle 1 TLR4
receptor complex 1 TLR4
neuron projection 1 PTGS2
ciliary basal body 1 ALB
chromatin 3 NFE2L2, NFKB1, PPARA
mediator complex 1 NFE2L2
phagocytic cup 2 TLR4, TNF
Chromosome 1 ANG
centriole 1 ALB
Nucleus, nucleolus 1 ANG
spindle pole 2 ALB, MAPK14
actin filament 1 MARK2
blood microparticle 1 ALB
Cell projection, dendrite 1 MARK2
Cytoplasm, Stress granule 1 ANG
cytoplasmic stress granule 1 ANG
azurophil granule 1 MPO
lipopolysaccharide receptor complex 1 TLR4
ficolin-1-rich granule lumen 1 MAPK14
secretory granule lumen 2 MAPK14, NFKB1
endoplasmic reticulum lumen 3 ALB, IL6, PTGS2
platelet alpha granule lumen 1 ALB
specific granule lumen 1 NFKB1
endocytic vesicle 1 ANG
azurophil granule lumen 1 MPO
Single-pass type IV membrane protein 1 HMOX1
phagocytic vesicle lumen 1 MPO
protein-DNA complex 1 NFE2L2
Rough endoplasmic reticulum 1 PTGDS
[Tumor necrosis factor, soluble form]: Secreted 1 TNF
Cytoplasm, sarcoplasm 1 MB
cortical cytoskeleton 1 NOS2
angiogenin-PRI complex 1 ANG
interleukin-6 receptor complex 1 IL6
[Nuclear factor NF-kappa-B p105 subunit]: Cytoplasm 1 NFKB1
[Nuclear factor NF-kappa-B p50 subunit]: Nucleus 1 NFKB1
I-kappaB/NF-kappaB complex 1 NFKB1
NF-kappaB p50/p65 complex 1 NFKB1
ciliary transition fiber 1 ALB
microtubule bundle 1 MARK2
[C-domain 2]: Secreted 1 TNF
[Tumor necrosis factor, membrane form]: Membrane 1 TNF
[C-domain 1]: Secreted 1 TNF


文献列表

  • Yu Zhou, Longlong Wang, Maria Carmen Rubio, Carmen Pérez-Rontomé, Yumiao Zhou, Yongmei Qi, Tao Tian, Weiqing Zhang, Qiuling Fan, Manuel Becana, Deqiang Duanmu. Heme catabolism mediated by heme oxygenase in uninfected interstitial cells enables efficient symbiotic nitrogen fixation in Lotus japonicus nodules. The New phytologist. 2023 Jun; ?(?):. doi: 10.1111/nph.19074. [PMID: 37329247]
  • Federica Frascogna, Benjamin Ledermann, Jana Hartmann, Eugenio Pérez Patallo, Fjoralba Zeqiri, Eckhard Hofmann, Nicole Frankenberg-Dinkel. On the evolution of the plant phytochrome chromophore biosynthesis. Plant physiology. 2023 Jun; ?(?):. doi: 10.1093/plphys/kiad327. [PMID: 37311159]
  • Kazuya Ishikawa, Xiaonan Xie, Yasuhide Osaki, Atsushi Miyawaki, Keiji Numata, Yutaka Kodama. Bilirubin is produced nonenzymatically in plants to maintain chloroplast redox status. Science advances. 2023 06; 9(23):eadh4787. doi: 10.1126/sciadv.adh4787. [PMID: 37285441]
  • Huanhuan Wang, Ying Ge, Lei Zhang, Yinghui Wei, Qinghai Li, Xuedong Zhang, Yuchun Pan. The pigments in eggshell with different colour and the pigment regulatory gene expression in corresponding chicken's shell gland. Animal : an international journal of animal bioscience. 2023 Mar; 17(5):100776. doi: 10.1016/j.animal.2023.100776. [PMID: 37043933]
  • Qiong Li, Siyuan Qin, Hailong Tian, Ruolan Liu, Ling Qiao, Shanshan Liu, Bowen Li, Mei Yang, Jiayan Shi, Edouard C Nice, Jingquan Li, Tingyuan Lang, Canhua Huang. Nano-Econazole Enhanced PD-L1 Checkpoint Blockade for Synergistic Antitumor Immunotherapy against Pancreatic Ductal Adenocarcinoma. Small (Weinheim an der Bergstrasse, Germany). 2023 Mar; ?(?):e2207201. doi: 10.1002/smll.202207201. [PMID: 36899444]
  • Husheem Michael, Vishal Srivastava, Loic Deblais, Joshua O Amimo, Juliet Chepngeno, Linda J Saif, Gireesh Rajashekara, Anastasia N Vlasova. The Combined Escherichia coli Nissle 1917 and Tryptophan Treatment Modulates Immune and Metabolome Responses to Human Rotavirus Infection in a Human Infant Fecal Microbiota-Transplanted Malnourished Gnotobiotic Pig Model. mSphere. 2022 Oct; 7(5):e0027022. doi: 10.1128/msphere.00270-22. [PMID: 36073800]
  • Samrat Rakshit, Nisha Sahu, Satendra Kumar Nirala, Monika Bhadauria. Protective activity of purpurin against d-galactosamine and lipopolysaccharide-induced hepatorenal injury by upregulation of heme oxygenase-1 in the RBC degradation cycle. Journal of biochemical and molecular toxicology. 2022 Oct; 36(10):e23168. doi: 10.1002/jbt.23168. [PMID: 35838105]
  • Xing Chen, Shuchun Chen, Qingjuan Ren, Shu Niu, Lin Yue, Xiaoyu Pan, Zelin Li, Ruiyi Zhu, Zhuoya Jia, Xiaoyi Chen, Ruoxi Zhen, Jiangli Ban. A metabonomics-based renoprotective mechanism analysis of empagliflozin in obese mice. Biochemical and biophysical research communications. 2022 09; 621(?):122-129. doi: 10.1016/j.bbrc.2022.06.091. [PMID: 35820282]
  • Yuan-Yu Lin, Jon Y Takemoto, Cheng-Wei T Chang, Ching-An Peng. Mesobiliverdin IXα ameliorates osteoporosis via promoting osteogenic differentiation of mesenchymal stem cells. Biochemical and biophysical research communications. 2022 09; 619(?):56-61. doi: 10.1016/j.bbrc.2022.06.042. [PMID: 35738065]
  • Clara G Altomare, Daniel C Adelsberg, Juan Manuel Carreno, Iden A Sapse, Fatima Amanat, Ali H Ellebedy, Viviana Simon, Florian Krammer, Goran Bajic. Structure of a Vaccine-Induced, Germline-Encoded Human Antibody Defines a Neutralizing Epitope on the SARS-CoV-2 Spike N-Terminal Domain. mBio. 2022 06; 13(3):e0358021. doi: 10.1128/mbio.03580-21. [PMID: 35467422]
  • Jianfeng Mei, Xia Wu, Sujing Zheng, Yu Yi, Xudong Wang, Guoqing Ying. Production of bilirubin by biotransformation of biliverdin using recombinant Escherichia coli cells. Bioprocess and biosystems engineering. 2022 Mar; 45(3):563-571. doi: 10.1007/s00449-021-02679-4. [PMID: 35066674]
  • David A Hanna, Courtney M Moore, Liu Liu, Xiaojing Yuan, Iramofu M Dominic, Angela S Fleischhacker, Iqbal Hamza, Stephen W Ragsdale, Amit R Reddi. Heme oxygenase-2 (HO-2) binds and buffers labile ferric heme in human embryonic kidney cells. The Journal of biological chemistry. 2022 02; 298(2):101549. doi: 10.1016/j.jbc.2021.101549. [PMID: 34973332]
  • Xiaqing Zhu, Shuren Feng, Zhongyi Jiang, Huayue Zhang, Yanyan Wang, Haitao Yang, Zefang Wang. An ultra-red fluorescent biosensor for highly sensitive and rapid detection of biliverdin. Analytica chimica acta. 2021 Aug; 1174(?):338709. doi: 10.1016/j.aca.2021.338709. [PMID: 34247733]
  • Annachiara Rosa, Valerie E Pye, Carl Graham, Luke Muir, Jeffrey Seow, Kevin W Ng, Nicola J Cook, Chloe Rees-Spear, Eleanor Parker, Mariana Silva Dos Santos, Carolina Rosadas, Alberto Susana, Hefin Rhys, Andrea Nans, Laura Masino, Chloe Roustan, Evangelos Christodoulou, Rachel Ulferts, Antoni G Wrobel, Charlotte-Eve Short, Michael Fertleman, Rogier W Sanders, Judith Heaney, Moira Spyer, Svend Kjær, Andy Riddell, Michael H Malim, Rupert Beale, James I MacRae, Graham P Taylor, Eleni Nastouli, Marit J van Gils, Peter B Rosenthal, Massimo Pizzato, Myra O McClure, Richard S Tedder, George Kassiotis, Laura E McCoy, Katie J Doores, Peter Cherepanov. SARS-CoV-2 can recruit a heme metabolite to evade antibody immunity. Science advances. 2021 05; 7(22):. doi: 10.1126/sciadv.abg7607. [PMID: 33888467]
  • Isha Khurana, Prince Allawadhi, Amit Khurana, Amit Kumar Srivastava, Umashanker Navik, Anil Kumar Banothu, Kala Kumar Bharani. Can bilirubin nanomedicine become a hope for the management of COVID-19?. Medical hypotheses. 2021 Apr; 149(?):110534. doi: 10.1016/j.mehy.2021.110534. [PMID: 33640714]
  • Natasha M Nesbitt, Lisa E Malone, Zhaoyan Liu, Alexander Jares, Dmitri V Gnatenko, Yupo Ma, Wei Zhu, Wadie F Bahou. Divergent erythroid megakaryocyte fates in Blvrb-deficient mice establish non-overlapping cytoprotective functions during stress hematopoiesis. Free radical biology & medicine. 2021 02; 164(?):164-174. doi: 10.1016/j.freeradbiomed.2020.12.015. [PMID: 33359909]
  • Rei Tohda, Hideaki Tanaka, Risa Mutoh, Xuhong Zhang, Young-Ho Lee, Tsuyoshi Konuma, Takahisa Ikegami, Catharina T Migita, Genji Kurisu. Crystal structure of higher plant heme oxygenase-1 and its mechanism of interaction with ferredoxin. The Journal of biological chemistry. 2021 Jan; 296(?):100217. doi: 10.1074/jbc.ra120.016271. [PMID: 33839679]
  • Yueyi Li, Yan Dong, Li Meng, Panpan Yu, Penghui Zhao, Miao Gong, Qiang Gao, Haishui Shi, Cuili Meng, Yuan Gao. Effects of Exogenous Biliverdin Treatment on Neurobehaviors in Mice. Biological & pharmaceutical bulletin. 2021; 44(3):325-331. doi: 10.1248/bpb.b20-00340. [PMID: 33642542]
  • Ryan G Shiels, Wenu Hewage, Evan N Pennell, Josif Vidimce, Gary Grant, Andrew G Pearson, Karl-Heinz Wagner, Michael Morgan, Andrew C Bulmer. Biliverdin and bilirubin sulfonate inhibit monosodium urate induced sterile inflammation in the rat. European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences. 2020 Dec; 155(?):105546. doi: 10.1016/j.ejps.2020.105546. [PMID: 32927072]
  • Michael W Butler, Ellen M Armour, Jennifer A Minnick, Marissa L Rossi, Sydney F Schock, Scott E Berger, Justin K Hines. Effects of stress-induced increases of corticosterone on circulating triglyceride levels, biliverdin concentration, and heme oxygenase expression. Comparative biochemistry and physiology. Part A, Molecular & integrative physiology. 2020 02; 240(?):110608. doi: 10.1016/j.cbpa.2019.110608. [PMID: 31704186]
  • Masakazu Sugishima, Kei Wada, Keiichi Fukuyama, Ken Yamamoto. Crystal structure of phytochromobilin synthase in complex with biliverdin IXα, a key enzyme in the biosynthesis of phytochrome. The Journal of biological chemistry. 2020 01; 295(3):771-782. doi: 10.1074/jbc.ra119.011431. [PMID: 31822504]
  • Sanu K Anand, Manna Rachel Mathew, K Girish Kumar. A Simple and Cost Effective Turn off Fluorescence Sensor for Biliverdin and Bilirubin Based on L-Cysteine Modulated Copper Nanoclusters. Journal of fluorescence. 2020 Jan; 30(1):63-70. doi: 10.1007/s10895-019-02470-5. [PMID: 31858352]
  • Wen-Jing Yi, Yu-Shuai Han, Li-Liang Wei, Li-Ying Shi, Huai Huang, Ting-Ting Jiang, Zhi-Bin Li, Jing Chen, Yu-Ting Hu, Hui-Hui Tu, Ji-Cheng Li. l-Histidine, arachidonic acid, biliverdin, and l-cysteine-glutathione disulfide as potential biomarkers for cured pulmonary tuberculosis. Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie. 2019 Aug; 116(?):108980. doi: 10.1016/j.biopha.2019.108980. [PMID: 31125821]
  • Jessica L Baylor, Michael W Butler. Immune challenge-induced oxidative damage may be mitigated by biliverdin. The Journal of experimental biology. 2019 03; 222(Pt 6):. doi: 10.1242/jeb.200055. [PMID: 30770399]
  • Mathula Thangarajh, Aiping Zhang, Kirandeep Gill, Habtom W Ressom, Zhenzhi Li, Rency S Varghese, Eric P Hoffman, Kanneboyina Nagaraju, Yetrib Hathout, Simina M Boca. Discovery of potential urine-accessible metabolite biomarkers associated with muscle disease and corticosteroid response in the mdx mouse model for Duchenne. PloS one. 2019; 14(7):e0219507. doi: 10.1371/journal.pone.0219507. [PMID: 31310630]
  • Lovely Mahawar, Gyan Singh Shekhawat. Haem oxygenase: A functionally diverse enzyme of photosynthetic organisms and its role in phytochrome chromophore biosynthesis, cellular signalling and defence mechanisms. Plant, cell & environment. 2018 03; 41(3):483-500. doi: 10.1111/pce.13116. [PMID: 29220548]
  • Bhavisha A Bakrania, Frank T Spradley, Simon C Satchell, David E Stec, John M Rimoldi, Rama S V Gadepalli, Joey P Granger. Heme oxygenase-1 is a potent inhibitor of placental ischemia-mediated endothelin-1 production in cultured human glomerular endothelial cells. American journal of physiology. Regulatory, integrative and comparative physiology. 2018 03; 314(3):R427-R432. doi: 10.1152/ajpregu.00370.2017. [PMID: 29212810]
  • Weiyu Chen, Ghassan J Maghzal, Anita Ayer, Cacang Suarna, Louise L Dunn, Roland Stocker. Absence of the biliverdin reductase-a gene is associated with increased endogenous oxidative stress. Free radical biology & medicine. 2018 02; 115(?):156-165. doi: 10.1016/j.freeradbiomed.2017.11.020. [PMID: 29195835]
  • Zhiqian Ma, Fengxing Pu, Xiaobin Zhang, Yunhuan Yan, Lijuan Zhao, Angke Zhang, Na Li, En-Min Zhou, Shuqi Xiao. Carbon monoxide and biliverdin suppress bovine viral diarrhoea virus replication. The Journal of general virology. 2017 Dec; 98(12):2982-2992. doi: 10.1099/jgv.0.000955. [PMID: 29087274]
  • Rita Hargitai, Nóra Boross, Susanne Hámori, Eszter Neuberger, Zoltán Nyiri. Eggshell Biliverdin and Protoporphyrin Pigments in a Songbird: Are They Derived from Erythrocytes, Blood Plasma, or the Shell Gland?. Physiological and biochemical zoology : PBZ. 2017 Nov; 90(6):613-626. doi: 10.1086/694297. [PMID: 28937855]
  • Ricardo Ernesto Bianchetti, Aline Bertinatto Cruz, Bruna Soares Oliveira, Diego Demarco, Eduardo Purgatto, Lázaro Eustáquio Pereira Peres, Magdalena Rossi, Luciano Freschi. Phytochromobilin deficiency impairs sugar metabolism through the regulation of cytokinin and auxin signaling in tomato fruits. Scientific reports. 2017 08; 7(1):7822. doi: 10.1038/s41598-017-08448-2. [PMID: 28798491]
  • Raphael A Seidel, Thierry Claudel, Franziska A Schleser, Navin K Ojha, Matthias Westerhausen, Sandor Nietzsche, Christoph Sponholz, Frans Cuperus, Sina M Coldewey, Stefan H Heinemann, Georg Pohnert, Michael Trauner, Michael Bauer. Impact of higher-order heme degradation products on hepatic function and hemodynamics. Journal of hepatology. 2017 08; 67(2):272-281. doi: 10.1016/j.jhep.2017.03.037. [PMID: 28412296]
  • Lu Lu, Bao-Qing Zhao, Dan Miao, Wen-Long Ding, Ming Zhou, Hugo Scheer, Kai-Hong Zhao. A Simple Preparation Method for Phytochromobilin. Photochemistry and photobiology. 2017 05; 93(3):675-680. doi: 10.1111/php.12710. [PMID: 28500696]
  • Andrea W U Busch, Zachary WareJoncas, Beronda L Montgomery. Tryptophan-Rich Sensory Protein/Translocator Protein (TSPO) from Cyanobacterium Fremyella diplosiphon Binds a Broad Range of Functionally Relevant Tetrapyrroles. Biochemistry. 2017 Jan; 56(1):73-84. doi: 10.1021/acs.biochem.6b01019. [PMID: 27990801]
  • Di Yan, Christian Domes, Robert Domes, Timea Frosch, Jürgen Popp, Mathias W Pletz, Torsten Frosch. Fiber enhanced Raman spectroscopic analysis as a novel method for diagnosis and monitoring of diseases related to hyperbilirubinemia and hyperbiliverdinemia. The Analyst. 2016 Oct; 141(21):6104-6115. doi: 10.1039/c6an01670g. [PMID: 27704083]
  • W Clark, E Leclercq, H Migaud, J Nairn, A Davie. Isolation, identification and characterisation of ballan wrasse Labrus bergylta plasma pigment. Journal of fish biology. 2016 Oct; 89(4):2070-2084. doi: 10.1111/jfb.13106. [PMID: 27501866]
  • Paul A Sigala, Koldo Morante, Kouhei Tsumoto, Jose M M Caaveiro, Daniel E Goldberg. In-Cell Enzymology To Probe His-Heme Ligation in Heme Oxygenase Catalysis. Biochemistry. 2016 08; 55(34):4836-49. doi: 10.1021/acs.biochem.6b00562. [PMID: 27490825]
  • Chin-Kai Tseng, Chun-Kuang Lin, Yu-Hsuan Wu, Yen-Hsu Chen, Wei-Chun Chen, Kung-Chia Young, Jin-Ching Lee. Human heme oxygenase 1 is a potential host cell factor against dengue virus replication. Scientific reports. 2016 08; 6(?):32176. doi: 10.1038/srep32176. [PMID: 27553177]
  • Mitja Martelanc, Lovro Žiberna, Sabina Passamonti, Mladen Franko. Application of high-performance liquid chromatography combined with ultra-sensitive thermal lens spectrometric detection for simultaneous biliverdin and bilirubin assessment at trace levels in human serum. Talanta. 2016 07; 154(?):92-8. doi: 10.1016/j.talanta.2016.03.053. [PMID: 27154653]
  • Andrii A Kaberniuk, Anton A Shemetov, Vladislav V Verkhusha. A bacterial phytochrome-based optogenetic system controllable with near-infrared light. Nature methods. 2016 07; 13(7):591-7. doi: 10.1038/nmeth.3864. [PMID: 27159085]
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