(Q38065265)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23216251%20AND%20SRC:MED&resulttype=core&format=json

19 February 2020

review article

1 reference

title

Breaking on through to the other side: protein export through the bacterial Sec system (English)

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23216251%20AND%20SRC:MED&resulttype=core&format=json

19 February 2020

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23216251%20AND%20SRC:MED&resulttype=core&format=json

Marios Frantzeskos Sardis

19 February 2020

series ordinal

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23216251%20AND%20SRC:MED&resulttype=core&format=json

19 February 2020

Anastassios Economou

series ordinal

4

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23216251%20AND%20SRC:MED&resulttype=core&format=json

19 February 2020

author name string

Spyridoula Karamanou

series ordinal

3

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23216251%20AND%20SRC:MED&resulttype=core&format=json

19 February 2020

language of work or name

English

0 references

publication date

1 January 2013

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23216251%20AND%20SRC:MED&resulttype=core&format=json

19 February 2020

number of pages

13

1 reference

based on heuristic

inferred from page(s)

published in

Biochemical Journal

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23216251%20AND%20SRC:MED&resulttype=core&format=json

19 February 2020

volume

449

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23216251%20AND%20SRC:MED&resulttype=core&format=json

19 February 2020

issue

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23216251%20AND%20SRC:MED&resulttype=core&format=json

19 February 2020

page(s)

25-37

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23216251%20AND%20SRC:MED&resulttype=core&format=json

Toward a protein profile of Escherichia coli: comparison to its transcription profile

19 February 2020

cites work

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Bacterial protein secretion through the translocase nanomachine

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Subterfuge and manipulation: type III effector proteins of phytopathogenic bacteria

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

The bacterial injection kit: type III secretion systems

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Twin-arginine-specific protein export in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Transport and proofreading of proteins by the twin-arginine translocation (Tat) system in bacteria

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Structural and dynamic properties of bacterial type IV secretion systems (review).

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

SecA, a remarkable nanomachine

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

X-ray structure of a protein-conducting channel

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

The surprising complexity of signal sequences

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Signal peptides are allosteric activators of the protein translocase

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Chaperone release and unfolding of substrates in type III secretion

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Secretion by numbers: Protein traffic in prokaryotes

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Signal sequences. The limits of variation

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

The Escherichia coli SRP and SecB targeting pathways converge at the translocon

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

The E. coli ffh gene is necessary for viability and efficient protein export.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

A conserved function of YidC in the biogenesis of respiratory chain complexes.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Cotranslational and posttranslational protein translocation in prokaryotic systems

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Binding of SecB to ribosome-bound polypeptides has the same characteristics as binding to full-length, denatured proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Asymmetric binding between SecA and SecB two symmetric proteins: implications for function in export.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Signal peptidase I: cleaving the way to mature proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Structural biology of periplasmic chaperones.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

β-Barrel membrane protein assembly by the Bam complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Lipoprotein sorting in bacteria.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Crystal structure of the signal sequence binding subunit of the signal recognition particle

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Crystal structure of the NG domain from the signal-recognition particle receptor FtsY

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Structure of the conserved GTPase domain of the signal recognition particle

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

The guanine nucleotide-binding switch in three dimensions

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

The Crystal Structure of the Signal Recognition Particle in Complex with Its Receptor

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

The 54-kD protein of signal recognition particle contains a methionine-rich RNA binding domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Domain interactions in E. coli SRP: stabilization of M domain by RNA is required for effective signal sequence modulation of NG domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Crystal structure of the ribonucleoprotein core of the signal recognition particle

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Interaction of signal-recognition particle 54 GTPase domain and signal-recognition particle RNA in the free signal-recognition particle

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Recognition of a signal peptide by the signal recognition particle

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Following the signal sequence from ribosomal tunnel exit to signal recognition particle

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Membrane targeting of ribosomes and their release require distinct and separable functions of FtsY.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Role of SRP RNA in the GTPase cycles of Ffh and FtsY.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Signal sequences activate the catalytic switch of SRP RNA.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Concentrations of 4.5S RNA and Ffh protein in Escherichia coli: the stability of Ffh protein is dependent on the concentration of 4.5S RNA.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

L23 protein functions as a chaperone docking site on the ribosome

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Chaperone binding at the ribosomal exit tunnel

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

In vivo analysis of the overlapping functions of DnaK and trigger factor

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Effect of C-terminal truncation on the molecular chaperone function and dimerization of Escherichia coli trigger factor

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Structure and function of the molecular chaperone Trigger Factor.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Autogenous translation regulation by Escherichia coli ATPase SecA may be mediated by an intrinsic RNA helicase activity of this protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Structure and function of SecA, the preprotein translocase nanomotor

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

ATP- and ADP-dependent modulation of RNA unwinding and strand annealing activities by the DEAD-box protein DED1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

The DEAD-box protein family of RNA helicases

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Identification of the preprotein binding domain of SecA.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Selective photoaffinity labeling identifies the signal peptide binding domain on SecA

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Preprotein-controlled catalysis in the helicase motor of SecA

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Global co-ordination of protein translocation by the SecA IRA1 switch

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

The long alpha-helix of SecA is important for the ATPase coupling of translocation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Structural biology: Clamour for a kiss

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

SecA: a tale of two protomers

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Energetics of SecA dimerization

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

SecA, an essential component of the secretory machinery of Escherichia coli, exists as homodimer.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Nucleotide binding induces changes in the oligomeric state and conformation of Sec A in a lipid environment: a small-angle neutron-scattering study

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Ring-like pore structures of SecA: implication for bacterial protein-conducting channels

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Crystal structure of the translocation ATPase SecA from Thermus thermophilus reveals a parallel, head-to-head dimer.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Full-length Escherichia coli SecA dimerizes in a closed conformation in solution as determined by cryo-electron microscopy.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

The active ring-like structure of SecA revealed by electron crystallography: conformational change upon interaction with SecB.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Structure of dimeric SecA, the Escherichia coli preprotein translocase motor

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Escherichia coli SecA truncated at its termini is functional and dimeric.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

SecA dimer cross-linked at its subunit interface is functional for protein translocation

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Translocation of proteins across the cell envelope of Gram-positive bacteria

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

SecB is a bona fide generalized chaperone in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Crystal structure of the bacterial protein export chaperone secB

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Structural determinants of SecB recognition by SecA in bacterial protein translocation

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Crystal structure of SecB from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

SecB, one small chaperone in the complex milieu of the cell

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Molecular dynamics studies of the archaeal translocon

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Residues essential for the function of SecE, a membrane component of the Escherichia coli secretion apparatus, are located in a conserved cytoplasmic region

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Conformational transition of Sec machinery inferred from bacterial SecYE structures

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

prlA suppressors in Escherichia coli relieve the proton electrochemical gradient dependency of translocation of wild-type precursors

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Deregulation of the SecYEG translocation channel upon removal of the plug domain.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

The plug domain of the SecY protein stabilizes the closed state of the translocation channel and maintains a membrane seal

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Dynamics of SecY translocons with translocation-defective mutations

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Synthetic peptides identify a second periplasmic site for the plug of the SecYEG protein translocation complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Signal sequence recognition in posttranslational protein transport across the yeast ER membrane.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

SecDF of Bacillus subtilis, a molecular Siamese twin required for the efficient secretion of proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Genetic and molecular characterization of the Escherichia coli secD operon and its products

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

SecDFyajC forms a heterotetrameric complex with YidC.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Proteolytic processing of Escherichia coli twin-arginine signal peptides by LepB.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Complete genome sequence and comparative genomic analysis of an emerging human pathogen, serotype V Streptococcus agalactiae

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Families of serine peptidases.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Evolutionary families of peptidases

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

The chemistry and enzymology of the type I signal peptidases

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Signal recognition particle binds to ribosome-bound signal sequences with fluorescence-detected subnanomolar affinity that does not diminish as the nascent chain lengthens.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Structure of the E. coli signal recognition particle bound to a translating ribosome.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Signal sequence-independent membrane targeting of ribosomes containing short nascent peptides within the exit tunnel

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Signal recognition particle receptor exposes the ribosomal translocon binding site.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Accumulation of endoplasmic membranes and novel membrane-bound ribosome-signal recognition particle receptor complexes in Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Dual recognition of the ribosome and the signal recognition particle by the SRP receptor during protein targeting to the endoplasmic reticulum

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Single Copies of Sec61 and TRAP Associate with a Nontranslating Mammalian Ribosome

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Ribosome binding of a single copy of the SecY complex: implications for protein translocation

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Sequential checkpoints govern substrate selection during cotranslational protein targeting

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Assisted folding of D-glyceraldehyde-3-phosphate dehydrogenase by trigger factor

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Trigger factor and DnaK cooperate in folding of newly synthesized proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Identification of nascent chain interaction sites on trigger factor

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

SecB--a chaperone dedicated to protein translocation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Substrate specificity of the SecB chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

The C terminus of SecA is involved in both lipid binding and SecB binding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Sites of interaction between SecA and the chaperone SecB, two proteins involved in export

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

SecYEG and SecA are the stoichiometric components of preprotein translocase

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

A single copy of SecYEG is sufficient for preprotein translocation

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Zinc stabilizes the SecB binding site of SecA.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Conformational Flexibility and Peptide Interaction of the Translocation ATPase SecA

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

The oligomeric state and arrangement of the active bacterial translocon

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Structure of the SecY complex unlocked by a preprotein mimic.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

SecA supports a constant rate of preprotein translocation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

In and Out of the ER: Protein Folding, Quality Control, Degradation, and Related Human Diseases

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

EchoLOCATION: an in silico analysis of the subcellular locations of Escherichia coli proteins and comparison with experimentally derived locations

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

The Universal Protein Resource (UniProt) in 2010

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Improved prediction of signal peptides: SignalP 3.0

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Protein-translocating trimeric autotransporters of gram-negative bacteria

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Cryo-EM structure of the ribosome–SecYE complex in the membrane environment

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Targeting, insertion, and localization of Escherichia coli YidC.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Determination of the binding frame within a physiological ligand for the chaperone SecB.

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Escherichia coli SecA shape and dimensions

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

Structural determinants of lateral gate opening in the protein translocon

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1042%2FBJ20121227