Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Lukas, Stiburek"'
Autor:
Jiri Zeman, Tomas Honzik, Marketa Tesarova, Václav Martínek, Jana Sladkova, Daniela Burska, Marie Vanisova, Josef Zamecnik, Lukas Stiburek, Hana Hansikova, Jana Krizova
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1867:166147
The mitochondrial respiratory chain (MRC) complex III (CIII) associates with complexes I and IV (CI and CIV) into supercomplexes. We identified a novel homozygous missense mutation (c.665G>C; p.Gly222Ala) in UQCRC2 coding for structural subunit Core
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96a234b800c6de63faa669af2a4b4728
https://doi.org/10.1016/j.bbadis.2021.166147
https://doi.org/10.1016/j.bbadis.2021.166147
Autor:
Jiri Zeman, Daniela Fornuskova, Kamila Vinsova, Lukas Stiburek, Laszlo Wenchich, Olga Kostkova, Josef Houstek, Jana Cesnekova
Publikováno v:
Molecular Biology of the Cell
Loss-of-function studies show that the human mitochondrial YME1L protease ensures cell proliferation, maintains normal cristae morphology and complex I activity, acts in an antiapoptotic manner, protects mitochondria from accumulation of oxidatively
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50fd59161f0245227f0a9e480c0e8c0f
https://doi.org/10.1091/mbc.e11-08-0674
https://doi.org/10.1091/mbc.e11-08-0674
Autor:
Hana Hansikova, Tomas Honzik, Lukas Stiburek, Marketa Tesarova, Laszlo Wenchich, Evzenie Tietzeova, Olga Brantova, Daniela Fornuskova, Jiri Zeman
Publikováno v:
Biochimica et Biophysica Acta-Molecular Basis of Disease
Biochimica et Biophysica Acta-Molecular Basis of Disease, Elsevier, 2008, 1782 (5), pp.317. ⟨10.1016/j.bbadis.2008.02.001⟩
Biochimica et Biophysica Acta-Molecular Basis of Disease, Elsevier, 2008, 1782 (5), pp.317. ⟨10.1016/j.bbadis.2008.02.001⟩
The impact of point mutations in mitochondrial tRNA genes on the amount and stability of respiratory chain complexes and ATP synthase (OXPHOS) has been broadly characterized in cultured skin fibroblasts, skeletal muscle samples, and mitochondrial cyb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ec4c604c6a1bb653f920be1b23217b5
https://doi.org/10.1016/j.bbadis.2008.02.001
https://doi.org/10.1016/j.bbadis.2008.02.001
Publikováno v:
The Biochemical journal. 473(6)
Mitochondrial protein homeostasis is crucial for cellular function and integrity and is therefore maintained by several classes of proteins possessing chaperone and/or proteolytic activities. In the present study, we focused on characterization of LA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b34aa988550da5b1dd2b48b0108931d
https://pubmed.ncbi.nlm.nih.gov/26759378
https://pubmed.ncbi.nlm.nih.gov/26759378
Autor:
Jana, Cesnekova, Jana, Spacilova, Hana, Hansikova, Josef, Houstek, Jiri, Zeman, Lukas, Stiburek
Publikováno v:
Oncotarget
p53 is a major cellular tumor suppressor that in addition to its nuclear, transcription-dependent activity is also known to function extranuclearly. Cellular stressors such as reactive oxygen species can promote translocation of p53 into mitochondria
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::23150ef0f8e1c920a7e2a85192105d62
https://pubmed.ncbi.nlm.nih.gov/27323408
https://pubmed.ncbi.nlm.nih.gov/27323408
Autor:
Josef Houstek, L Cerna, Jiri Zeman, Katerina Vesela, Petr Pecina, Lukas Stiburek, Marketa Tesarova, Hana Hansikova
Publikováno v:
Biochemical Journal. 392:625-632
The biogenesis of eukaryotic COX (cytochrome c oxidase) requires several accessory proteins in addition to structural subunits and prosthetic groups. We have analysed the assembly state of COX and SCO2 protein levels in various tissues of six patient
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6886dc14a333cc15567dc30af7f6d156
https://doi.org/10.1042/bj20050807
https://doi.org/10.1042/bj20050807
Publikováno v:
The FASEB Journal. 28
Lace1 (Lactation elevated 1) is a human homolog of yeast Afg1 (ATPase family gene 1) ATPase with sequence identity ranging from 41,5 % H. sapiens vs. S. cerevisiae to 88,9 % H. sapiens vs. M. muscu...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cc7a6ef1f14fbbe9185eefc79ec80975
https://doi.org/10.1096/fasebj.28.1_supplement.lb168
https://doi.org/10.1096/fasebj.28.1_supplement.lb168
Autor:
Hana Hansikova, Daniela Fornuskova, Jiri Zeman, Kamila Vinsova, Lukas Stiburek, Laszlo Wenchich
Publikováno v:
Biochemical Journal
Biochemical Journal, Portland Press, 2010, 428 (3), pp.363-374. ⟨10.1042/BJ20091714⟩
Biochemical Journal, Portland Press, 2010, 428 (3), pp.363-374. ⟨10.1042/BJ20091714⟩
Mammalian CcO (cytochrome c oxidase) is a hetero-oligomeric protein complex composed of 13 structural subunits encoded by both the mitochondrial and nuclear genomes. To study the role of nuclear-encoded CcO subunits in the assembly and function of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9adbfa84988f478f2403a8d1030658f
https://hal.archives-ouvertes.fr/hal-00486858
https://hal.archives-ouvertes.fr/hal-00486858
Autor:
Lukas Stiburek, Jiri Zeman
Publikováno v:
Biochimica et biophysica acta. 1797(6-7)
Eukaryotic cytochrome c oxidase (CcO), the terminal enzyme of the energy-transducing mitochondrial electron transport chain is a hetero-oligomeric, heme–copper oxidase complex composed of both mitochondrially and nuclear-encoded subunits. It is emb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b91561ed1b38d3e10485f6f3fca05145
https://pubmed.ncbi.nlm.nih.gov/20398622
https://pubmed.ncbi.nlm.nih.gov/20398622
Publikováno v:
American journal of physiology. Cell physiology. 296(5)
Sco1 and Sco2 are mitochondrial copper-binding proteins involved in the biogenesis of the CuAsite in the cytochrome c oxidase (CcO) subunit Cox2 and in the maintenance of cellular copper homeostasis. Human Surf1 is a CcO assembly factor with an impor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a912693b1413f5ebb557f5a0c9b94036
https://pubmed.ncbi.nlm.nih.gov/19295170
https://pubmed.ncbi.nlm.nih.gov/19295170