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A unifying mechanism for protein transport through the core bacterial Sec machinery
WJ Allen, I Collinson - Open Biology, 2023 - royalsocietypublishing.org
Encapsulation and compartmentalization are fundamental to the evolution of cellular life, but
they also pose a challenge: how to partition the molecules that perform biological functions …
they also pose a challenge: how to partition the molecules that perform biological functions …
How quality control systems AID Sec-dependent protein translocation
The evolutionarily conserved Sec machinery is responsible for transporting proteins across
the cytoplasmic membrane. Protein substrates of the Sec machinery must be in an unfolded …
the cytoplasmic membrane. Protein substrates of the Sec machinery must be in an unfolded …
Vestiges of the bacterial signal recognition particle-based protein targeting in mitochondria
J Pyrih, T Pánek, IM Durante, V Rašková… - Molecular biology …, 2021 - academic.oup.com
The main bacterial pathway for inserting proteins into the plasma membrane relies on the
signal recognition particle (SRP), composed of the Ffh protein and an associated RNA …
signal recognition particle (SRP), composed of the Ffh protein and an associated RNA …
Cotranslational folding of alkaline phosphatase in the periplasm of Escherichia coli
Cotranslational protein folding studies using Force Profile Analysis, a method where the
SecM translational arrest peptide is used to detect folding‐induced forces acting on the …
SecM translational arrest peptide is used to detect folding‐induced forces acting on the …
Plastid molecular chaperone HSP90C interacts with the SecA1 subunit of Sec Translocase for thylakoid protein transport
AM Nair, T Jiang, B Mu, R Zhao - Plants, 2024 - mdpi.com
The plastid stroma-localized chaperone HSP90C plays a crucial role in maintaining optimal
proteostasis within chloroplasts and participates in protein translocation processes. While …
proteostasis within chloroplasts and participates in protein translocation processes. While …
Iron is a ligand of SecA-like metal-binding domains in vivo
T Cranford-Smith, M Jamshad, M Jeeves… - Journal of Biological …, 2020 - jbc.org
The ATPase SecA is an essential component of the bacterial Sec machinery, which
transports proteins across the cytoplasmic membrane. Most SecA proteins contain a long C …
transports proteins across the cytoplasmic membrane. Most SecA proteins contain a long C …
[PDF][PDF] SecA–a multidomain and multitask bacterial export protein
P Ambroziak, I Rzepka… - Acta Biochimica …, 2021 - frontierspartnerships.org
Most bacterial secretory proteins destined to the extracytoplasmic space are secreted
posttranslationally by the Sec translocase. SecA, a key component of the Sec system, is the …
posttranslationally by the Sec translocase. SecA, a key component of the Sec system, is the …
[HTML][HTML] The Structure of Clostridioides difficile SecA2 ATPase Exposes Regions Responsible for Differential Target Recognition of the SecA1 and SecA2-Dependent …
N Lindič, J Loboda, A Usenik, R Vidmar… - International journal of …, 2020 - mdpi.com
SecA protein is a major component of the general bacterial secretory system. It is an ATPase
that couples nucleotide hydrolysis to protein translocation. In some Gram-positive …
that couples nucleotide hydrolysis to protein translocation. In some Gram-positive …
Investigation of the structure and function of SecH, a novel component of the Sec machinery in Escherichia coli
MA Wynne - 2023 - etheses.bham.ac.uk
The Sec machinery translocates proteins across, or inserts proteins into, the cytoplasmic
membrane and is responsible for translocation of approximately 20% of all proteins …
membrane and is responsible for translocation of approximately 20% of all proteins …
AscA (YecA) is a molecular chaperone involved in Sec-dependent protein translocation in Escherichia coli
TC Smith, M Wynne, C Carter, C Jiang, M Jamshad… - bioRxiv, 2020 - biorxiv.org
Proteins that are translocated across the cytoplasmic membrane by Sec machinery must be
in an unfolded conformation in order to pass through the protein-conducting channel during …
in an unfolded conformation in order to pass through the protein-conducting channel during …