(Q39021695)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27890920%20AND%20SRC:MED&resulttype=core&format=json

28 March 2020

review article

1 reference

title

Protein export through the bacterial Sec pathway (English)

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27890920%20AND%20SRC:MED&resulttype=core&format=json

28 March 2020

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27890920%20AND%20SRC:MED&resulttype=core&format=json

28 March 2020

Nikolina Sostaric

3

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27890920%20AND%20SRC:MED&resulttype=core&format=json

28 March 2020

Anastassios Economou

4

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27890920%20AND%20SRC:MED&resulttype=core&format=json

28 March 2020

Spyridoula Karamanou

5

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27890920%20AND%20SRC:MED&resulttype=core&format=json

28 March 2020

author name string

Alexandra Tsirigotaki

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27890920%20AND%20SRC:MED&resulttype=core&format=json

28 March 2020

language of work or name

English

0 references

publication date

28 November 2016

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27890920%20AND%20SRC:MED&resulttype=core&format=json

Nature Reviews Microbiology

28 March 2020

published in

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27890920%20AND%20SRC:MED&resulttype=core&format=json

28 March 2020

volume

15

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27890920%20AND%20SRC:MED&resulttype=core&format=json

28 March 2020

issue

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27890920%20AND%20SRC:MED&resulttype=core&format=json

28 March 2020

page(s)

21-36

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27890920%20AND%20SRC:MED&resulttype=core&format=json

https://scigraph.springernature.com/pub.10.1038/nrmicro.2016.161

28 March 2020

exact match

0 references

cites work

Breaking on through to the other side: protein export through the bacterial Sec system.

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Protein folding in the cell envelope of Escherichia coli.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

X-ray structure of a protein-conducting channel

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

The Canonical and Accessory Sec System of Gram-positive Bacteria.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Membrane protein insertion and proton-motive-force-dependent secretion through the bacterial holo-translocon SecYEG-SecDF-YajC-YidC.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

YidC occupies the lateral gate of the SecYEG translocon and is sequentially displaced by a nascent membrane protein.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Membrane protein insertion and assembly by the bacterial holo-translocon SecYEG-SecDF-YajC-YidC.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Signal recognition particle: an essential protein-targeting machine

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

SecA-mediated targeting and translocation of secretory proteins.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

SecA interacts with ribosomes in order to facilitate posttranslational translocation in bacteria.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Cryo-electron microscopic structure of SecA protein bound to the 70S ribosome

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

ΔμH+ and ATP function at different steps of the catalytic cycle of preprotein translocase

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Charge-driven dynamics of nascent-chain movement through the SecYEG translocon

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

The membrane insertase YidC.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Signal peptidase I: cleaving the way to mature proteins

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Selective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivo

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Signal peptides are allosteric activators of the protein translocase

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Information encoded in non-native states drives substrate-chaperone pairing

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Signal-sequence induced conformational changes in the signal recognition particle

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Activated GTPase movement on an RNA scaffold drives co-translational protein targeting

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Sequential checkpoints govern substrate selection during cotranslational protein targeting

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Interplay between trigger factor and other protein biogenesis factors on the ribosome

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Signal sequences activate the catalytic switch of SRP RNA.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Quaternary Structure of SecA in Solution and Bound to SecYEG Probed at the Single Molecule Level

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Unlocking the Bacterial SecY Translocon

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Lateral opening of the bacterial translocon on ribosome binding and signal peptide insertion

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Membrane protein TM segments are retained at the translocon during integration until the nascent chain cues FRET-detected release into bulk lipid

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Structure of the Sec61 channel opened by a signal sequence

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Structure of a complex of the ATPase SecA and the protein-translocation channel

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

A gating motif in the translocation channel sets the hydrophobicity threshold for signal sequence function

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Monitoring the activity of single translocons.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Structures of the Sec61 complex engaged in nascent peptide translocation or membrane insertion

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Quaternary dynamics of the SecA motor drive translocase catalysis.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Structural Basis for Signal-Sequence Recognition by the Translocase Motor SecA as Determined by NMR

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Preprotein-controlled catalysis in the helicase motor of SecA

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Disorder-order folding transitions underlie catalysis in the helicase motor of SecA

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

A "push and slide" mechanism allows sequence-insensitive translocation of secretory proteins by the SecA ATPase

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Crystal structure of a substrate-engaged SecY protein-translocation channel

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Escherichia coli signal recognition particle receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

FtsY, the bacterial signal-recognition particle receptor, interacts functionally and physically with the SecYEG translocon

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Regulation of cargo recognition, commitment, and unloading drives cotranslational protein targeting

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Real-time observation of trigger factor function on translating ribosomes.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Chaperone networking facilitates protein targeting to the bacterial cytoplasmic membrane.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Multitasking SecB chaperones in bacteria

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Direct observation of chaperone-induced changes in a protein folding pathway

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Molecular chaperones in protein folding and proteostasis

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Defining the role of the Escherichia coli chaperone SecB using comparative proteomics.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Trigger Factor can antagonize both SecB and DnaK/DnaJ chaperone functions in Escherichia coli.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Trigger factor retards protein export in Escherichia coli.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Effect of signal peptide on the stability and folding kinetics of maltose binding protein

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

The presence of a helix breaker in the hydrophobic core of signal sequences of secretory proteins prevents recognition by the signal-recognition particle in Escherichia coli

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Structural basis of signal-sequence recognition by the signal recognition particle

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Regulation by a chaperone improves substrate selectivity during cotranslational protein targeting

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Real-time observation of signal recognition particle binding to actively translating ribosomes.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

mRNA-programmed translation pauses in the targeting of E. coli membrane proteins

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Local slowdown of translation by nonoptimal codons promotes nascent-chain recognition by SRP in vivo

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Whole genome analysis reveals a high incidence of non-optimal codons in secretory signal sequences of Escherichia coli.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Accurate prediction of cellular co-translational folding indicates proteins can switch from post- to co-translational folding

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Directed evolution of efficient secretion in the SRP-dependent export of TolB.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Molecular mechanism and structure of Trigger Factor bound to the translating ribosome

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Use of thioredoxin as a reporter to identify a subset of Escherichia coli signal sequences that promote signal recognition particle-dependent translocation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

An unusual signal peptide extension inhibits the binding of bacterial presecretory proteins to the signal recognition particle, trigger factor, and the SecYEG complex

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Defining the specificity of cotranslationally acting chaperones by systematic analysis of mRNAs associated with ribosome-nascent chain complexes

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Signal recognition particle and SecA cooperate during export of secretory proteins with highly hydrophobic signal sequences

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Cotranslational protein folding on the ribosome monitored in real time.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

A signal sequence is not required for protein export in prlA mutants of Escherichia coli

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Co-translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Lipid activation of the signal recognition particle receptor provides spatial coordination of protein targeting

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Trigger factor depletion or overproduction causes defective cell division but does not block protein export

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Structure and function of the molecular chaperone Trigger Factor.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Binding specificity of Escherichia coli trigger factor

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Concerted action of the ribosome and the associated chaperone trigger factor confines nascent polypeptide folding

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Crystal structure of SecB from Escherichia coli

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Crystal structure of the bacterial protein export chaperone secB

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Tight hydrophobic contacts with the SecB chaperone prevent folding of substrate proteins.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Structural basis for the antifolding activity of a molecular chaperone

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Substrate specificity of the SecB chaperone

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

High-affinity binding of Escherichia coli SecB to the signal sequence region of a presecretory protein

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

The basis of asymmetry in the SecA:SecB complex

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Structural determinants of SecB recognition by SecA in bacterial protein translocation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Orientation of SecA and SecB in complex, derived from disulfide cross-linking

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Dimeric SecA couples the preprotein translocation in an asymmetric manner

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Conformational Flexibility and Peptide Interaction of the Translocation ATPase SecA

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Identification of the preprotein binding domain of SecA.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

A molecular switch in SecA protein couples ATP hydrolysis to protein translocation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Mapping polypeptide interactions of the SecA ATPase during translocation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Preserving the membrane barrier for small molecules during bacterial protein translocation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Investigating the SecY plug movement at the SecYEG translocation channel.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Crystal Structures of SecYEG in Lipidic Cubic Phase Elucidate a Precise Resting and a Peptide-Bound State

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Structure of the SecY complex unlocked by a preprotein mimic.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Three-dimensional structure of the bacterial protein-translocation complex SecYEG

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Structure of the E. coli protein-conducting channel bound to a translating ribosome

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Bacterial protein translocation requires only one copy of the SecY complex in vivo

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

The oligomeric state and arrangement of the active bacterial translocon

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Two copies of the SecY channel and acidic lipids are necessary to activate the SecA translocation ATPase

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

A single copy of SecYEG is sufficient for preprotein translocation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Protein translocation is mediated by oligomers of the SecY complex with one SecY copy forming the channel.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Conformational transition of Sec machinery inferred from bacterial SecYE structures

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Hydrophobically stabilized open state for the lateral gate of the Sec translocon

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Dynamic structure of the translocon SecYEG in membrane: direct single molecule observations.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Structure of the Mammalian Ribosome-Sec61 Complex to 3.4 Å Resolution

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Regulation of the Protein-Conducting Channel by a Bound Ribosome

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

The sec and prl genes of Escherichia coli

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Modeling the effects of prl mutations on the Escherichia coli SecY complex

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

The PrlA and PrlG phenotypes are caused by a loosened association among the translocase SecYEG subunits

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Structure of the SecY channel during initiation of protein translocation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Mutations in the Sec61p Channel Affecting Signal Sequence Recognition and Membrane Protein Topology

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

ATPase Active-Site Electrostatic Interactions Control the Global Conformation of the 100 kDa SecA Translocase

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

The dynamic action of SecA during the initiation of protein translocation.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Conformational Changes of the Clamp of the Protein Translocation ATPase SecA

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Helicase Motif III in SecA is essential for coupling preprotein binding to translocation ATPase.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

A large conformational change couples the ATP binding site of SecA to the SecY protein channel.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Cross-talk between catalytic and regulatory elements in a DEAD motor domain is essential for SecA function

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

SecA: a tale of two protomers

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Conformational dynamics of the plug domain of the SecYEG protein-conducting channel.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Two-way communication between SecY and SecA suggests a Brownian ratchet mechanism for protein translocation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

The Sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Molecular code for transmembrane-helix recognition by the Sec61 translocon

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

How translocons select transmembrane helices

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Size, motion, and function of the SecY translocon revealed by molecular dynamics simulations with virtual probes

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

A biphasic pulling force acts on transmembrane helices during translocon-mediated membrane integration

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Orientational preferences of neighboring helices can drive ER insertion of a marginally hydrophobic transmembrane helix

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

A dual function for SecA in the assembly of single spanning membrane proteins in Escherichia coli

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Lipids and topological rules governing membrane protein assembly.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

A role for the two-helix finger of the SecA ATPase in protein translocation.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Mobility of the SecA 2-helix-finger is not essential for polypeptide translocation via the SecYEG complex

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Structure and function of a membrane component SecDF that enhances protein export

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

The catalytic cycle of the escherichia coli SecA ATPase comprises two distinct preprotein translocation events

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Bacterial Sec protein transport is rate-limited by precursor length: a single turnover study

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Peptide binding to a bacterial signal peptidase visualized by peptide tethering and carrier-driven crystallization

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Dynamic interaction of the sec translocon with the chaperone PpiD

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

The periplasmic chaperone PpiD interacts with secretory proteins exiting from the SecYEG translocon.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Protein transport by the bacterial Tat pathway

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Secretion systems in Gram-negative bacteria: structural and mechanistic insights.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Type III Secretion: Building and Operating a Remarkable Nanomachine.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Protein secretion and surface display in Gram-positive bacteria

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Outer membrane protein biogenesis in Gram-negative bacteria

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Lipoprotein sorting in bacteria.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

A protein export pathway involving Escherichia coli porins

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Global proteomic profiling of native outer membrane vesicles derived from Escherichia coli.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Visualization of a polytopic membrane protein during SecY-mediated membrane insertion

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO.2016.161

Proteome-wide subcellular topologies of E. coli polypeptides database (STEPdb).

31 March 2020

1 reference

12 December 2020

Inserting proteins into the bacterial cytoplasmic membrane using the Sec and YidC translocases

1 reference

12 December 2020

ProOmpA spontaneously folds in a membrane assembly competent state which trigger factor stabilizes

1 reference

12 December 2020

The methionine-rich domain of the 54 kd protein subunit of the signal recognition particle contains an RNA binding site and can be crosslinked to a signal sequence

1 reference

12 December 2020

Identifiers

DOI

10.1038/NRMICRO.2016.161

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:27890920%20AND%20SRC:MED&resulttype=core&format=json

release_lbrjsifsinab5cjb5lnt3cwaou

28 March 2020

Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/lbrjsifsinab5cjb5lnt3cwaou

24 November 2022

mapped directly with Wikidata item

1 reference