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Molecular machines that facilitate bacterial outer membrane protein biogenesis
Almost all outer membrane proteins (OMPs) in Gram-negative bacteria contain a β-barrel
domain that spans the outer membrane (OM). To reach the OM, OMPs must be translocated …
domain that spans the outer membrane (OM). To reach the OM, OMPs must be translocated …
Periplasmic chaperones: outer membrane biogenesis and envelope stress
Envelope biogenesis and homeostasis in gram-negative bacteria are exceptionally intricate
processes that require a multitude of periplasmic chaperones to ensure cellular survival …
processes that require a multitude of periplasmic chaperones to ensure cellular survival …
Regulation of α-synuclein by chaperones in mammalian cells
Neurodegeneration in patients with Parkinson's disease is correlated with the occurrence of
Lewy bodies—intracellular inclusions that contain aggregates of the intrinsically disordered …
Lewy bodies—intracellular inclusions that contain aggregates of the intrinsically disordered …
NMR spectroscopy captures the essential role of dynamics in regulating biomolecular function
Biomolecules are in constant motion. To understand how they function, and why
malfunctions can cause disease, it is necessary to describe their three-dimensional …
malfunctions can cause disease, it is necessary to describe their three-dimensional …
Outer membrane protein biogenesis in Gram-negative bacteria
SE Rollauer, MA Sooreshjani… - … Transactions of the …, 2015 - royalsocietypublishing.org
Gram-negative bacteria contain a double membrane which serves for both protection and for
providing nutrients for viability. The outermost of these membranes is called the outer …
providing nutrients for viability. The outermost of these membranes is called the outer …
Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM
The β-barrel assembly machinery (BAM) is a∼ 203 kDa complex of five proteins (BamA–E),
which is essential for viability in E. coli. BAM promotes the folding and insertion of β-barrel …
which is essential for viability in E. coli. BAM promotes the folding and insertion of β-barrel …
Structural basis for protein antiaggregation activity of the trigger factor chaperone
T Saio, X Guan, P Rossi, A Economou, CG Kalodimos - Science, 2014 - science.org
Introduction Molecular chaperones prevent aggregation and misfolding of proteins in the
cellular environment and are thus central to maintaining protein homeostasis. Molecular …
cellular environment and are thus central to maintaining protein homeostasis. Molecular …
Structural basis for client recognition and activity of Hsp40 chaperones
Y Jiang, P Rossi, CG Kalodimos - Science, 2019 - science.org
Hsp70 and Hsp40 chaperones work synergistically in a wide range of biological processes
including protein synthesis, membrane translocation, and folding. We used nuclear …
including protein synthesis, membrane translocation, and folding. We used nuclear …
Structural insights into the mechanism of protein transport by the Type 9 Secretion System translocon
Secretion systems are protein export machines that enable bacteria to exploit their
environment through the release of protein effectors. The Type 9 Secretion System (T9SS) is …
environment through the release of protein effectors. The Type 9 Secretion System (T9SS) is …
Structural basis for the antifolding activity of a molecular chaperone
C Huang, P Rossi, T Saio, CG Kalodimos - Nature, 2016 - nature.com
Molecular chaperones act on non-native proteins in the cell to prevent their aggregation,
premature folding or misfolding. Different chaperones often exert distinct effects, such as …
premature folding or misfolding. Different chaperones often exert distinct effects, such as …