Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Narcis-Adrian Petriman"'
Publikováno v:
Microbial Cell, Vol 7, Iss 11, Pp 289-299 (2020)
Cilia and flagella are slender projections found on most eukaryotic cells including unicellular organisms such as Chlamydomonas, Trypanosoma and Tetrahymena, where they serve motility and signaling functions. The cilium is a large molecular machine c
Externí odkaz:
https://doaj.org/article/4283ccd1e8114032bfd145412f241dee
Publikováno v:
eLife, Vol 9 (2020)
The structures of the bovine and human BBSome reveal that a conformational change is required to recruit the complex to the ciliary membrane.
Externí odkaz:
https://doaj.org/article/15e3ee3815874f56be0d3aa62d1b4c65
Autor:
Lara Knüpffer, Clara Fehrenbach, Kärt Denks, Veronika Erichsen, Narcis-Adrian Petriman, Hans-Georg Koch
Publikováno v:
mBio, Vol 10, Iss 4 (2019)
ABSTRACT Bacteria execute a variety of protein transport systems for maintaining the proper composition of their different cellular compartments. The SecYEG translocon serves as primary transport channel and is engaged in transporting two different s
Externí odkaz:
https://doaj.org/article/dfb2cb01a5c94f7481d09e63f0d90395
Autor:
Narcis Adrian Petriman, Pleasantine Mill, Margaret A. Keighren, Petra Kiesel, Tooba Quidwai, Jonathan N. Wells, Jiaolong Wang, Laura C. Murphy, Weihua Leng, Esben Lorentzen, Gaia Pigino, Joseph A. Marsh, Emma Hall
Publikováno v:
Quidwai, T, Wang, J, Hall, E A, Petriman, N A, Leng, W, Kiesel, P, Wells, J N, Murphy, L C, Keighren, M A, A Marsh, J, Lorentzen, E, Pigino, G & Mill, P 2021, ' A WDR35-dependent coat protein complex transports ciliary membrane cargo vesicles to cilia ', eLife, vol. 10, e69786 . https://doi.org/10.7554/eLife.69786
eLife
eLife, Vol 10 (2021)
Quidwai, T, Wang, J, Hall, E A, Petriman, N A, Leng, W, Kiesel, P, Wells, J N, Murphy, L C, Keighren, M A, A Marsh, J, Lorentzen, E, Pigino, G & Mill, P 2021, ' A WDR35-dependent coat protein complex transports ciliary membrane cargo vesicles to cilia ', eLIFE, vol. 10 . https://doi.org/10.7554/eLife.69786
eLife
eLife, Vol 10 (2021)
Quidwai, T, Wang, J, Hall, E A, Petriman, N A, Leng, W, Kiesel, P, Wells, J N, Murphy, L C, Keighren, M A, A Marsh, J, Lorentzen, E, Pigino, G & Mill, P 2021, ' A WDR35-dependent coat protein complex transports ciliary membrane cargo vesicles to cilia ', eLIFE, vol. 10 . https://doi.org/10.7554/eLife.69786
Intraflagellar transport (IFT) is a highly conserved mechanism for motor-driven transport of cargo within cilia, but how this cargo is selectively transported to cilia is unclear. WDR35/IFT121 is a component of the IFT-A complex best known for its ro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66f64150e8e37334c7485a5f3df509bf
https://pure.au.dk/portal/da/publications/a-wdr35dependent-coat-protein-complex-transports-ciliary-membrane-cargo-vesicles-to-cilia(26b12d5e-fddf-47db-b664-49374d435eed).html
https://pure.au.dk/portal/da/publications/a-wdr35dependent-coat-protein-complex-transports-ciliary-membrane-cargo-vesicles-to-cilia(26b12d5e-fddf-47db-b664-49374d435eed).html
Autor:
Ruth Steinberg, Ilie Sachelaru, Hans-Georg Koch, Bettina Warscheid, Benjamin Jauss, Friedel Drepper, Narcis-Adrian Petriman, Lisa Franz, Thomas Welte
Publikováno v:
J Biol Chem
The SecYEG translocon constitutes the major protein transport channel in bacteria and transfers an enormous variety of different secretory and inner-membrane proteins. The minimal core of the SecYEG translocon consists of three inner-membrane protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a209b231ab1d343530ecb49f8122576
https://doi.org/10.1074/jbc.ra119.010686
https://doi.org/10.1074/jbc.ra119.010686
Autor:
Benjamin Jauß, Lisa Franz, Friedel Drepper, Antonia Hufnagel, Narcis-Adrian Petriman, Bettina Warscheid, Hans-Georg Koch, Ilie Sachelaru
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-16 (2018)
Scientific Reports
Scientific Reports
YidC/Oxa1/Alb3 are essential proteins that operate independently or cooperatively with the Sec machinery during membrane protein insertion in bacteria, archaea and eukaryotic organelles. Although the interaction between the bacterial SecYEG transloco
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9af4074281446a229d96b8c23f03f54
http://link.springer.com/article/10.1038/s41598-017-19019-w
http://link.springer.com/article/10.1038/s41598-017-19019-w
Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon
Autor:
Andreas Vogt, Albena Draycheva, Patrick Kuhn, Narcis-Adrian Petriman, Friedel Drepper, Wolfgang Wintermeyer, Hans-Georg Koch, Lukas Sturm, Bettina Warscheid
Publikováno v:
Journal of Cell Biology
The Journal of Cell Biology
The Journal of Cell Biology
The cotranslational transfer of nascent membrane proteins to the SecYEG translocon is facilitated by a reorientation of the SecY-bound signal recognition particle (SRP) receptor, FtsY, which accompanies the formation of a quaternary targeting complex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1c7e87a1d371858eb8503a31f2c7921
https://doi.org/10.1083/jcb.201502103
https://doi.org/10.1083/jcb.201502103
Publikováno v:
Journal of Biological Chemistry. 289:21706-21715
The Sec translocon constitutes a ubiquitous protein transport channel that consists in bacteria of the three core components: SecY, SecE, and SecG. Additional proteins interact with SecYEG during different stages of protein transport. During targetin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fda2bb953470f1be41c024fbdffdf17a
https://doi.org/10.1074/jbc.m114.577916
https://doi.org/10.1074/jbc.m114.577916
Autor:
Kärt Denks, Hans-Georg Koch, Narcis-Adrian Petriman, Ilie Sachelaru, Renuka Kudva, Andreas Vogt
Publikováno v:
Molecular Membrane Biology. 31:58-84
Protein transport via the Sec translocon represents an evolutionary conserved mechanism for delivering cytosolically-synthesized proteins to extra-cytosolic compartments. The Sec translocon has a three-subunit core, termed Sec61 in Eukaryotes and Sec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62b13fb7211ed423a95a6a23f3500d4f
https://doi.org/10.3109/09687688.2014.907455
https://doi.org/10.3109/09687688.2014.907455
Publikováno v:
BIOspektrum. 21:696-698
Compartmentalization is a unifying principle of eukaryotic and prokaryotic cells and necessitates specific protein delivery systems that transport proteins from their site of synthesis in the cytosol to their sites of function. Bacteria use a large v
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c9be2fc5f7600499b05778df163002cd
https://doi.org/10.1007/s12268-015-0631-6
https://doi.org/10.1007/s12268-015-0631-6