Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Therese Eneqvist"'
Publikováno v:
FEBS Letters. 583:2727-2733
AtPreP (Arabidopsis thaliana Presequence Protease) is a zink metallooligopeptidase that is dually targeted to both mitochondria and chloroplasts. In these organelles it functions as a peptidasome that degrades the N-terminal targeting peptides that a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d7585265d267235535af6b2371a5717
https://doi.org/10.1016/j.febslet.2009.07.040
https://doi.org/10.1016/j.febslet.2009.07.040
Autor:
Annelie Ståhl, Shashi Bhushan, Anne Frohn, B. Martin Hallberg, Kenneth A. Johnson, Elzbieta Glaser, Therese Eneqvist
Publikováno v:
The EMBO Journal. 25:1977-1986
Presequence protease PreP is a novel protease that degrades targeting peptides as well as other unstructured peptides in both mitochondria and chloroplasts. The first structure of PreP from Arabidopsis thaliana refined at 2.1 Angstroms resolution sho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6092bc03ad22b40100b47c50520fc8be
https://doi.org/10.1038/sj.emboj.7601080
https://doi.org/10.1038/sj.emboj.7601080
Publikováno v:
Biochemistry. 44:13063-13070
The Tyr114Cys substitution in the human plasma protein transthyretin leads to a particularly aggressive form of familial amyloidotic polyneuropathy. In a previous study we demonstrated that ATTR Tyr114Cys forms intermolecular disulfide bonds, which p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::43f85633dd95a2af47ede5cdf4a700a1
https://doi.org/10.1021/bi050795s
https://doi.org/10.1021/bi050795s
Autor:
Erik Lundberg, Deborah M. Power, Anders Karlsson, Shenghua Huang, A. Elisabeth Sauer-Eriksson, Therese Eneqvist, Cecília R.A. Santos
Publikováno v:
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Transthyretin (TTR) is an extracellular transport protein involved in the distribution of thyroid hormones and vitamin A. So far, TTR has only been found in vertebrates, of which piscine TTR displays the lowest sequence identity with human TTR (47%).
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14370c8a156a515b4a3bf0c082cd81bf
https://doi.org/10.1074/jbc.m313553200
https://doi.org/10.1074/jbc.m313553200
Publikováno v:
European Journal of Biochemistry. 270:518-532
A number of proteins related to the homotetrameric transport protein transthyretin (TTR) forms a highly conserved protein family, which we present in an integrated analysis of data from different sources combined with an initial biochemical character
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c21d5ff6dcd953ff399165a0331b3ad2
https://doi.org/10.1046/j.1432-1033.2003.03408.x
https://doi.org/10.1046/j.1432-1033.2003.03408.x
Autor:
Karin Andersson, A. Elisabeth Sauer-Eriksson, Therese Eneqvist, Anders Olofsson, Erik Lundgren
Publikováno v:
Molecular Cell. 6:1207-1218
Transthyretin is a tetrameric plasma protein associated with two forms of amyloid disease. The structure of the highly amyloidogenic transthyretin triple mutant TTRG53S/E54D/L55S determined at 2.3 A resolution reveals a novel conformation: the beta-s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac40c2b20d5eb4458386fd38a9eac10b
https://doi.org/10.1016/s1097-2765(00)00117-9
https://doi.org/10.1016/s1097-2765(00)00117-9
Autor:
Nyosha Alikhani, Catarina Moreira Pinho, Elzbieta Glaser, Caroline Graff, Laura Fratiglioni, Therese Eneqvist, Hans G. Bäckman, Behnosh F. Björk
Publikováno v:
Neuroscience letters. 469(2)
Several studies suggest mitochondrial dysfunction as a possible mechanism underlying the development of Alzheimer disease (AD). There is data showing that amyloid-beta (A beta) peptide is present in AD brain mitochondria. The human presequence protea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d969e755f7f96b947e9e7098d8ebd861
https://pubmed.ncbi.nlm.nih.gov/19962426
https://pubmed.ncbi.nlm.nih.gov/19962426
Publikováno v:
Biological chemistry. 387(8)
The 2.1-A-resolution crystal structure of the novel mitochondrial and chloroplastic metalloendopeptidase, AtPreP1, revealed a unique peptidasome structure, in which the two halves of the enzyme completely enfold a huge proteolytic cavity. Based on th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f318057ad863661b866d339a3bc806e
https://pubmed.ncbi.nlm.nih.gov/16895479
https://pubmed.ncbi.nlm.nih.gov/16895479
Autor:
Erik Lundgren, Therese Eneqvist, Andreas Hörnberg, Anders Olofsson, A. Elisabeth Sauer-Eriksson
Publikováno v:
Biochimica et biophysica acta. 1700(1)
Conformational changes in native and variant forms of the human plasma protein transthyretin (TTR) induce several types of amyloid diseases. Biochemical and structural studies have mapped the initiation site of amyloid formation onto residues at the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d1a55482407950c42bfa65ead07f05f
https://pubmed.ncbi.nlm.nih.gov/15210129
https://pubmed.ncbi.nlm.nih.gov/15210129
Autor:
Therese Eneqvist, Erik Lundgren, A. Elisabeth Sauer-Eriksson, Jana Jass, Yukio Ando, Taihei Miyakawa, Anders Olofsson, Shoichi Katsuragi
Publikováno v:
Biochemistry. 41(44)
The Y114C mutation in human transthyretin (TTR) is associated with a particular form of familial amyloidotic polyneuropathy. We show that vitreous aggregates ex vivo consist of either regular amyloid fibrils or disordered disulfide-linked precipitate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::37f1565b741146d26a2850cd45afca19
https://pubmed.ncbi.nlm.nih.gov/12403615
https://pubmed.ncbi.nlm.nih.gov/12403615