ArticleMolecular biology of the cell2026
Twin-arginine transport complex plays an essential role in
Trisha N Chong, Klara Christensen, Damion L Whitfield, Mayura Panjalingam, Nima Pendar, Phway Phway Myat, Joseph C Chen
Abstract read
In one paragraphArticle in Molecular biology of the cell, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
2 · The registryThe trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
3 · Its place in the literatureWho cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
4 · The recordCorrections and comments
5 · Who and what moneyAuthors and funding
7 authors.
Trisha N ChongDepartment of Pathology, Stanford University, Stanford, CA 94306.
Klara ChristensenDepartment of Biology, San Francisco State University, San Francisco, CA 94132.
Damion L WhitfieldDepartment of Biology, San Francisco State University, San Francisco, CA 94132.
Mayura PanjalingamDepartment of Chemistry, New York University, New York, NY 10003.
Nima PendarDepartment of Biology, San Francisco State University, San Francisco, CA 94132.
Phway Phway MyatDepartment of Biology, San Francisco State University, San Francisco, CA 94132.
Joseph C ChenDepartment of Biology, San Francisco State University, San Francisco, CA 94132.
Funding
SFSU MA-MS/PHD BRIDGE TO THE FUTURER25GM048972 · NIGMS · SAN FRANCISCO STATE UNIVERSITY · PI BAYLISS, FRANK T, FUSE, MEGUMI M. · 1992 to 2020
$5.6MU-RISE at San Francisco State UniversityT34GM145400 · NIGMS · SAN FRANCISCO STATE UNIVERSITY · PI Raymond M. Esquerra, MEGUMI M. FUSE · 2022 to 2026
$4.6MSinorhizobium meliloti factors that affect biofilm formation and symbiosis efficiencySC3GM096943 · NIGMS · SAN FRANCISCO STATE UNIVERSITY · PI CHEN, JOSEPH CHIUNG-CHU · 2012 to 2023
$1.4MRegulated Assembly of Subcellular Structures in alpha-ProteobacteriaSC2GM082318 · NIGMS · SAN FRANCISCO STATE UNIVERSITY · PI CHEN, JOSEPH CHIUNG-CHU · 2008 to 2010
$380kNecessity of RNA degradosome assembly in Sinorhizobium meliloti for effective symbiosisR16GM153570 · NIGMS · SAN FRANCISCO STATE UNIVERSITY · PI Joseph Chiung-Chu Chen · 2025 to 2026
$310kRegulated proteolysis in Caulobacter cell cycleF32GM067472 · NIGMS · STANFORD UNIVERSITY · PI CHEN, JOSEPH C · 2003 to 2005
$139kNIGMS NIH HHS F32 GM067472NIGMS NIH HHS R16 GM153570NIGMS NIH HHS R25 GM048972NIGMS NIH HHS SC2 GM082318NIGMS NIH HHS SC3 GM096943NIGMS NIH HHS T34 GM145400
6 · The paper itselfAbstract
Two main pathways are responsible for protein secretion across the cytoplasmic membrane in prokaryotes. While the general secretory (Sec) pathway transports proteins across the membrane in an unfolded state, the twin-arginine translocation (Tat) pathway exports proteins primarily in their folded conformation. Although the Tat system appears dispensable in multiple model bacteria, some species require it for viability, and the reason for the distinction is nebulous. Here we show that all three subunits of the Tat complex-TatA, TatB, and TatC-are essential in the alpha-proteobacterium
Indexed as
Bacterial ProteinsCaulobacter crescentusMembrane Transport ProteinsTwin-Arginine-Translocation SystemCell ShapeMicrobial ViabilityPenicillin-Binding ProteinsProtein TransportBacterial ProteinsMembrane Transport ProteinsPenicillin-Binding ProteinsTwin-Arginine-Translocation System
Identifiers
PMID41537744
PMCPMC12911857
What Socratic holds
Textmetadata
LicenceCC BY
Read underepoch 390