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Involvement of PpiD in Sec-dependent protein translocation
Biochimica Et Biophysica Acta - Molecular Cell Research, 2018 The periplasmic space in between the inner and outer membrane of Gram-negative bacteria contains numerous chaperones that are involved in the biogenesis and rescue of extra-cytosolic proteins. In contrast to most of those periplasmic chaperones, PpiD is anchored by an N-terminal transmembrane domain within the inner membrane of Escherichia coli.
Yufan Zhou, Matthias Müller
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Dynamic Interaction of the Sec Translocon with the Chaperone PpiD [PDF]
Journal of Biological Chemistry, 2014 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 targeting, SecYEG interacts with SecA, the SRP receptor, or the ribosome.
Renuka Kudva, Hans-Georg Koch
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The Role of Communication of PPID in the Pandemic Situation
Advances in social science, education and humanities research, 2022 Anasta Novi Hidayati +2 more
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Analisis Program Peningkatan Nilai PPID
Bandung Conference Series: Public Relations, 2023Abstract. This research was made as a report on the author's internship at PT Semen Indonesia regarding any work that the author has done, especially regarding company information disclosure and the PPID (Information and Documentation Management Officer) value improvement program.
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UP-SSO: Enhancing the User Privacy of SSO by Integrating PPID and SGX
2021 International Conference on Advanced Computing and Endogenous Security, 2022Qiongxiao Wang, Jingqiang Lin
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PPIDS: Privacy Preserving Intrusion Detection System
2007The goal of intrusion detection systems(IDS) is to protect from the signs of security problems. However, since an IDS usually depends on the monitored data and has to identify an intruder, the running of IDS comes to threaten users' privacy.
Hyun-A Park +3 more
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The Periplasmic Chaperone PpiD Interacts with Secretory Proteins Exiting from the SecYEG Translocon
Biochemistry, 2008The Sec translocon of Escherichia coli mediates the export of numerous secretory and membrane proteins. To dissect the passage of an exported protein across the Sec translocon into consecutive steps, we generated in vitro translocation intermediates of a polypeptide chain, which by its N-terminus is anchored in the membrane and by its C-terminus ...
Ken-Ichi Nishiyama, Matthias Müller
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