Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Deanna L. Mendez"'
Autor:
Jiao Li, Wan Zheng, Ming Gu, Long Han, Yanmei Luo, Koukou Yu, Mengxin Sun, Yuliang Zong, Xiuxiu Ma, Bing Liu, Ethan P. Lowder, Deanna L. Mendez, Robert G. Kranz, Kai Zhang, Jiapeng Zhu
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-13 (2022)
Bacterial ABC transporter complex CcmABCD, a part of cytochrome c maturation system, transfers heme from one binding partner (CcmC) to another (CcmE). Here authors describe high resolution cryo-EM structures of CcmABCD in multiple states and propose
Externí odkaz:
https://doaj.org/article/e104efcb27cf4836910eeadd14d685ba
Autor:
Deanna L. Mendez, Ethan P. Lowder, Dustin E. Tillman, Molly C. Sutherland, Andrea L. Collier, Michael J. Rau, James A. J. Fitzpatrick, Robert G. Kranz
Publikováno v:
Nature chemical biology. 18(1)
Although the individual structures and respiratory functions of cytochromes are well studied, the structural basis for their assembly, including transport of heme for attachment, are unknown. We describe cryo-electron microscopy (cryo-EM) structures
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d590d2cf4026ac0ebb248d0f5d246c76
https://pubmed.ncbi.nlm.nih.gov/34931065
https://pubmed.ncbi.nlm.nih.gov/34931065
In vitro reconstitution reveals major differences between human and bacterial cytochrome c synthases
Autor:
Dustin E Tillman, Noah T Prizant, Olga Melnikov, Robert G. Kranz, Molly C. Sutherland, Deanna L. Mendez, Shalon E. Babbitt, Nathan L. Tran, Andrea L Collier
Publikováno v:
eLife, Vol 10 (2021)
eLife
eLife
Cytochromes c are ubiquitous heme proteins in mitochondria and bacteria, all possessing a CXXCH (CysXxxXxxCysHis) motif with covalently attached heme. We describe the first in vitro reconstitution of cytochrome c biogenesis using purified mitochondri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61b938b93993465243a7e1bd87685190
https://doi.org/10.7554/elife.64891
https://doi.org/10.7554/elife.64891
Autor:
Deanna L. Mendez, Olga Melnikov, Nathan L. Tran, Robert G. Kranz, Shalon E. Babbitt, Andrea L Collier, Molly C. Sutherland, Dustin E Tillman, Noah T Prizant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e71716c6c108812f66f26138c935e07c
https://doi.org/10.7554/elife.64891.sa2
https://doi.org/10.7554/elife.64891.sa2
Publikováno v:
Biochemistry. 56:2766-2769
Cytochrome c (cyt c) has two important roles in vertebrates: mitochondrial electron transport and activating the intrinsic cell death pathway (apoptosis). To initiate cell death, cyt c dissociates from the inner mitochondrial membrane and migrates to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3cc20fed5acfe906041876b8d58029d
https://doi.org/10.1021/acs.biochem.7b00309
https://doi.org/10.1021/acs.biochem.7b00309
C-type cytochromes (cyts c) are generally characterized by the presence of two thioether attachments between heme and two cysteine residues within a highly conserved CXXCH motif. Most eukaryotes use the System III cyt c biogenesis pathway composed of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ced24f20a8947ca2aee8912f8a0e8f83
https://europepmc.org/articles/PMC5551481/
https://europepmc.org/articles/PMC5551481/
Autor:
John M. D’Alessandro, Robert G. Kranz, Jeremy D. King, Deanna L. Mendez, Shalon E. Babbitt, Liviu M. Mirica, Michael B. Watson, Robert E. Blankenship
Cytochrome c (cyt c), required for electron transport in mitochondria, possesses a covalently attached heme cofactor. Attachment is catalyzed by holocytochrome c synthase (HCCS), leading to two thioether bonds between heme and a conserved CXXCH motif
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dabc222ddff0b5f372bac9f5d31b8c87
https://europepmc.org/articles/PMC5338485/
https://europepmc.org/articles/PMC5338485/
Autor:
Brian San Francisco, Gudrun S. Lukat-Rodgers, Eric C. Bretsnyder, Kenton R. Rodgers, Shalon E. Babbitt, Robert G. Kranz, Deanna L. Mendez
Publikováno v:
Journal of Biological Chemistry. 289:28795-28807
Mitochondrial cytochrome c assembly requires the covalent attachment of heme by thioether bonds between heme vinyl groups and a conserved CXXCH motif of cytochrome c/c1. The enzyme holocytochrome c synthase (HCCS) binds heme and apocytochrome c subst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d65e37a9330703437c890b86ca27fb6
https://doi.org/10.1074/jbc.m114.593509
https://doi.org/10.1074/jbc.m114.593509
Publikováno v:
Journal of Biological Chemistry. 288:22315-22323
Drosophila melanogaster Heterochromatin Protein 1a (HP1a) is an essential protein critical for heterochromatin assembly and regulation. Its chromo shadow domain (CSD) homodimerizes, a requirement for binding protein partners that contain a PXVXL moti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3384a6ec203eb4e029b8be5a350939c6
https://doi.org/10.1074/jbc.m113.468413
https://doi.org/10.1074/jbc.m113.468413
Autor:
Sarah C. R. Elgin, Gena E. Stephens, Daesung Kim, Wladek Minor, Maksymilian Chruszcz, Sepideh Khorasanizadeh, Deanna L. Mendez
Publikováno v:
ChemBioChem. 12:1084-1096
Drosophila melanogaster heterochromatin protein 1a (HP1a) is essential for compacted heterochromatin structure and the associated gene silencing. Its chromo shadow domain (CSD) is well known for binding to peptides that contain a PXVXL motif. Heteroc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80ca712cd957a3b20f9d1315e82d5771
https://doi.org/10.1002/cbic.201000598
https://doi.org/10.1002/cbic.201000598