The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The target is correctly identified as the SPI-1 type III secretion-system ATPase InvC, standardized as SctN1, from Salmonella enterica serovar Typhimurium strain LT2 (ordered locus STM2894). The literature protein is a 432-residue, approximately 47.4-kDa F1-like/AAA+-related P-loop ATPase associated specifically with the SPI-1 injectisome. This matches the supplied UniProt family and domain annotations. The retrieved primary papers did not themselves print the modern P0A1B9–STM2894–sctN1 cross-reference, so that exact mapping rests on the supplied UniProt record; nevertheless, organism, synonym InvC, system, size, motifs, and biochemical function all agree, and no similarly named protein from another organism was substituted. Importantly, InvC must not be confused with SsaN, the paralogous ATPase of the Salmonella SPI-2 system. (eichelberg1994molecularandfunctional pages 6-7, eichelberg1994molecularandfunctional pages 1-2)
InvC’s primary function is to hydrolyze ATP at the cytoplasmic base of the SPI-1 injectisome and couple nucleotide-dependent conformational changes to secretion-substrate handling. The best-supported model is that it helps recruit chaperone-bound substrates, remove or reorganize their chaperones, and prepare secretion proteins for entry into the narrow export channel. ATP hydrolysis is directly demonstrated; universal chaperone dissociation and substrate unfolding by purified InvC remain less directly established and should be described as a strongly supported T3SS-family mechanism rather than a demonstrated reaction for every SPI-1 cargo. (eichelberg1994molecularandfunctional pages 8-9, allison2014identificationofthe pages 8-9, bernal2019structuralanalysisof pages 1-2)
| Annotation dimension | Best-supported conclusion | Direct evidence / quantitative result | Evidence type | Key source with publication date and DOI URL | Confidence / limitation |
|---|---|---|---|---|---|
| Identity | sctN1/InvC (P0A1B9; STM2894) is the SPI-1 type III secretion-system ATPase of Salmonella enterica serovar Typhimurium LT2; it is distinct from the SPI-2 ATPase SsaN. | Experimental literature identifies InvC as a 432-aa, predicted 47,393-Da S. Typhimurium invasion protein and SPI-1 ATPase. (eichelberg1994molecularandfunctional pages 6-7, eichelberg1994molecularandfunctional pages 1-2) | Sequence analysis; biochemical characterization | Eichelberg et al., 1994-08, DOI | High for organism, protein and system; P0A1B9, STM2894 and the standardized symbol sctN1 derive from the supplied UniProt record and were not printed in the retrieved primary-paper excerpts. |
| ATPase reaction | InvC catalyzes ATP hydrolysis: ATP + H₂O → ADP + inorganic phosphate; ATP is the demonstrated nucleotide substrate. | Purified, nondenatured InvC released approximately 250 pmol Pi·min⁻¹·µg protein⁻¹ under the reported assay conditions. (eichelberg1994molecularandfunctional pages 8-9, eichelberg1994molecularandfunctional pages 5-5) | Purified-protein biochemical assay | Eichelberg et al., 1994-08, DOI | High for ATP hydrolysis; no full kinetic characterization, Mg²⁺ dependence profile, Km, kcat or broad nucleotide panel was recovered. |
| Catalytic Lys165 | Lys165 in the Walker-A/P-loop is essential for ATPase activity and biological function. | K165E eliminated significant ATPase activity and failed to complement an invC mutant: invasion was 0.08 ± 0.04%, versus 30 ± 2.1% or 21 ± 1.6% with functional invC constructs. (eichelberg1994molecularandfunctional pages 5-5, eichelberg1994molecularandfunctional pages 6-7) | Site-directed mutagenesis; enzymology; genetic complementation | Eichelberg et al., 1994-08, DOI | High; substitution may affect nucleotide binding and local structure, but concordant biochemical and cellular defects strongly support catalytic necessity. |
| Domain architecture | InvC is an F₁/V₁/A₁-like, AAA+-related P-loop ATPase with an N-terminal assembly/regulatory region, central ATPase core and C-terminal substrate/chaperone-recognition region. | InvCΔ79 comprises an ATPase core at approximately Arg81–Thr355 and C-terminal domain at Thr356–Asn431; its P-loop is GCGKT, residues 162–166. Apo, ATPγS-bound and ADP-bound structures were solved at 2.05, 2.65 and 2.80 Å, respectively. (bernal2019structuralanalysisof pages 1-2, bernal2019structuralanalysisof pages 2-3) | X-ray crystallography; sequence/structure comparison | Bernal et al., 2019-08, DOI | High for structural boundaries and nucleotide site; “AAA+” describes mechanistic/structural relatedness, while the closest family annotation is the T3SS ATPase/F₁-like α/β-chain family. |
| Oligomerization | Functional InvC is positioned as a predicted/assembled hexameric ring, but isolated N-terminally truncated InvC is predominantly monomeric or dimeric. | SEC-MALS measured InvCΔ79 species of approximately 40 kDa and 80 kDa; native MS confirmed monomers and dimers. The N-terminal 1–79 residues promote stable higher-order assembly. (bernal2019structuralanalysisof pages 2-3) | SEC-MALS; native mass spectrometry; structural modeling | Bernal et al., 2019-08, DOI | Moderate–high; monomer/dimer measurements concern a truncated soluble construct, whereas hexamerization is favored in the intact sorting platform and is not reproduced robustly in isolation. |
| Sorting-platform localization | InvC acts on the cytoplasmic face of the bacterial inner membrane, in the central hub directly beneath the export apparatus—not in the periplasm, extracellular space or host cell. | Cryo-electron tomography resolved a six-pod platform approximately 23 nm high × 36 nm wide, with a central nave approximately 12 nm across. InvC occupies the hexameric nave; its C terminus faces InvA, with InvI/SctO between them. (hu2017insitumolecular pages 5-6) | In situ cryo-electron tomography; subtomogram averaging; chromosomal protein tagging | Hu et al., 2017-03, DOI | High for cellular position and orientation; deletion of InvC reduced rather than erased nave density, showing that the hub also contains other components. |
| Sorting-platform interactions | InvC is connected to SpaO/SpaOC pods through OrgB spokes and contacts the central stalk InvI/SctO, which links toward InvA and the export gate. | Co-expression/co-purification supported the chain SpaO/SpaOC–OrgB–InvC–InvI. A soluble complex reached 207 ± 1 kDa; native MS detected a 215-kDa 2(SpaO–2SpaOC)–2OrgB–InvC assembly. (bornicke2020invitroreconstitution pages 71-74, bornicke2020invitroreconstitution pages 68-71) | Complex reconstitution; SEC-MALS; native MS; SAXS | Bernal et al., 2019-09, DOI | High for the interaction topology; soluble complexes are heterogeneous and do not by themselves reproduce the complete sixfold membrane-associated machine. |
| Cargo/chaperone interaction | InvC’s C-terminal region participates in recognition of chaperone–effector cargo, but direct evidence for ATP-driven release or unfolding by purified InvC remains incomplete. | InvC-L376P reportedly failed to bind the SicP–SptP complex. Direct mapping in the paralog SsaN placed chaperone docking in the C-terminal helix-10 region; however, reconstituted InvC-platform complexes showed no validated SicP/SptP binding by native MS or SEC-MALS. (allison2014identificationofthe pages 8-9, bornicke2020invitroreconstitutiona pages 62-68, bornicke2020invitroreconstitution pages 62-68) | Mutagenesis and binding assays; paralog-supported structural inference; negative biophysical results | Allison et al., 2014-08, DOI; Bernal et al., 2019-08, DOI | Moderate; cargo recognition is supported, but claims that InvC directly dissociates and unfolds every SPI-1 substrate should be labeled mechanistic inference rather than fully demonstrated substrate-by-substrate biochemistry. |
| Biological phenotype | InvC ATPase activity is required for SPI-1-mediated host-cell entry and associated cytoskeletal remodeling, rather than bacterial attachment alone. | Wild-type invasion was reported as 88 ± 4%, versus 0.10 ± 0.03% for an invC mutant; functional invC plasmids restored 30 ± 2.1% or 21 ± 1.6% invasion. The mutant attached but failed to induce normal cytoskeletal rearrangements. (eichelberg1994molecularandfunctional pages 6-7) | Gentamicin-protection invasion assay; complementation; cell biology | Eichelberg et al., 1994-08, DOI | High for cultured epithelial-cell invasion; direct InvC-specific animal virulence statistics were not recovered. |
| Substrate specificity | The chemically established substrate is ATP; physiological protein clients are multiple SPI-1 secretion substrates presented with cognate chaperones, not one uniquely specific effector. | ATPγS and ADP occupy the conserved nucleotide site and induce remodeling of two pore-facing loops. No comparative ATP/GTP/CTP/UTP kinetic panel or definitive InvC substrate repertoire was reported. (bernal2019structuralanalysisof pages 1-2) | Ligand-bound crystallography; functional inference | Bernal et al., 2019-08, DOI | Moderate: ATP specificity is directly supported, but nucleotide selectivity and protein-cargo specificity remain incompletely quantified. |
| Recent 2024 context | Recent work expands Salmonella pathogenicity-island and structural-genomics context but does not materially revise the InvC mechanism established by earlier biochemical and structural studies. | A 2024 pangenome study examined 79,758 strains, 13,147 proteins and 17,238 domains; among 272 proteins from 14 SPIs, 90 were secretion-machinery proteins and 41% of SPI-protein domains lacked prior sequence annotation. (medvedev2024structureclassificationof pages 1-2) | Large-scale pangenome and structure classification | Medvedev et al., 2024-05, DOI | High for broad quantitative context, low for InvC-specific inference: the study did not add direct InvC ATPase, localization, interaction or substrate evidence. |
Table: Evidence matrix distinguishing direct experimental support from structural inference and unresolved questions for the Salmonella Typhimurium SPI-1 ATPase sctN1/InvC (P0A1B9).
The experimentally characterized S. Typhimurium InvC is 432 amino acids long with a predicted mass of 47,393 Da. It belongs to the conserved secretion-associated ATPases homologous to FliI, Shigella Spa47, and Yersinia YscN. These characteristics align with UniProt P0A1B9, STM2894, and the standardized injectisome nomenclature SctN1, where “1” distinguishes the SPI-1 system from the SPI-2 ATPase. (eichelberg1994molecularandfunctional pages 6-7, eichelberg1994molecularandfunctional pages 7-8)
The supplied domain assignments—AAA+ ATPase, ATPase α/β-chain family, and F1/V1/A1 α/β-subunit-like nucleotide-binding domains—are consistent with crystallography and sequence analysis. InvC is not a membrane transporter subunit and is not itself secreted. Rather, it is a soluble, peripheral cytoplasmic component recruited to the membrane-associated injectisome sorting platform. (bernal2019structuralanalysisof pages 1-2, bernal2019structuralanalysisof pages 2-3, hu2017insitumolecular pages 5-6)
The directly supported reaction is:
ATP + H₂O → ADP + Pi
Purified InvC hydrolyzed ATP at approximately 250 pmol inorganic phosphate min⁻¹ µg⁻¹ protein under the original assay conditions. This establishes ATP as a biochemical substrate and supports EC 7.4.2.8 in the functional sense that ATP hydrolysis is coupled to protein export, although InvC is not by itself a membrane-spanning transporter. (eichelberg1994molecularandfunctional pages 8-9, eichelberg1994molecularandfunctional pages 5-5)
Catalytic necessity was demonstrated by replacing Lys165 in the Walker-A/P-loop with glutamate. K165E InvC lacked significant ATPase activity and failed to complement an invC mutant, directly linking ATP utilization to SPI-1 biological function. The conserved nucleotide-binding sequence is GCGKT at residues 162–166. (eichelberg1994molecularandfunctional pages 5-5, bernal2019structuralanalysisof pages 2-3)
ATP, ATPγS, and ADP have been visualized or tested in InvC studies. ATPγS- and ADP-bound structures validate the nucleotide pocket, but ATPγS is an analogue rather than a physiological hydrolysis substrate. The retrieved literature did not provide a comparative ATP/GTP/CTP/UTP panel, Km, kcat, catalytic efficiency, or a definitive metal-ion specificity profile. Therefore, annotation as an ATPase is secure, whereas claims of absolute nucleotide exclusivity are not. (bernal2019structuralanalysisof pages 1-2, bernal2019structuralanalysisof pages 2-3)
InvC’s physiological protein “substrates” are not a single species. It acts within a sorting platform that processes multiple SPI-1 secretion cargos, including chaperone-associated translocators and effectors. Evidence implicates the C-terminal region in binding the SicP–SptP chaperone-effector pair: InvC-L376P failed to bind that complex. However, later reconstitution experiments did not obtain reliable quantitative binding of SicP/SptP to InvC-containing complexes, and apparent nanomolar signals were attributed to dissociation or aggregation artifacts. Thus, cargo recognition is supported, but the full client repertoire and binding constants remain unresolved. (bornicke2020invitroreconstitutiona pages 62-68, allison2014identificationofthe pages 8-9, bornicke2020invitroreconstitution pages 62-68)
InvC comprises three functional regions:
Structures of InvC lacking residues 1–79 were solved at 2.05 Å without nucleotide, 2.65 Å with ATPγS, and 2.80 Å with ADP. Nucleotide binding remodels the active site and two pore-facing loops. Because these loops face the central channel of the modeled InvC ring and are required for function, they provide a plausible coupling mechanism between ATP-state changes and cargo processing. (bernal2019structuralanalysisof pages 1-2)
Isolated InvCΔ79 formed approximately 40-kDa monomers and 80-kDa dimers by SEC-MALS and native mass spectrometry. This does not contradict the hexameric cellular model: removal of the N terminus eliminates a region important for oligomer stabilization, and intact InvC is organized by OrgB and the rest of the sorting platform. Accordingly, the functional state is best annotated as a platform-assembled hexameric ATPase ring, while free or truncated protein can be monomeric/dimeric. (bernal2019structuralanalysisof pages 2-3, bornicke2020invitroreconstitution pages 74-77)
InvC functions on the cytoplasmic side of the inner membrane, directly beneath the membrane export apparatus. It is neither an integral membrane protein nor an extracellular needle component. In situ cryo-electron tomography placed InvC in the central nave of a six-pod SPI-1 sorting platform approximately 23 nm high and 36 nm wide, with a central nave approximately 12 nm across. Its C terminus is oriented toward the cytoplasmic domain of the export-gate component InvA. (hu2017insitumolecular pages 5-6)
The interaction chain is approximately:
PrgH/basal body → OrgA → SpaO/SpaOC pods → OrgB spokes → InvC ATPase → InvI/SctO stalk → InvA/export gate.
OrgB connects peripheral SpaO-containing pods to the central ATPase. InvI/SctO occupies or contacts InvC’s central pore and links toward InvA. Deleting InvC reduces sorting-platform density but does not remove the entire nave, demonstrating that the central density is not exclusively InvC. (bornicke2020invitroreconstitution pages 20-24, hu2017insitumolecular pages 5-6, bornicke2020invitroreconstitution pages 68-71)
Biochemical reconstitution supports this topology. A major soluble species measured 207 ± 1 kDa, while native mass spectrometry detected a 215-kDa 2(SpaO–2SpaOC)–2OrgB–InvC complex. SAXS showed an extended L-shaped building block, with SpaO/SpaOC in the outer arm, OrgB forming the connection, and InvC at the hub. Assembly of six such units predicts approximately 6 InvC molecules in the completed ring, although SpaO copy-number estimates remain model-dependent. (bornicke2020invitroreconstitution pages 71-74, bornicke2020invitroreconstitution pages 74-77, bornicke2020invitroreconstitution pages 58-62)
SPI-1 encodes an injectisome that exports needle, tip, translocon, and effector proteins in a regulated sequence. InvC is part of the cytoplasmic sorting/energizing machinery. Its mechanistic role can be divided into:
The proton motive force also contributes substantially to T3SS export; InvC should therefore not be described as the sole force that physically propels proteins through the complete needle. A more defensible interpretation is that it is an ATP-powered substrate-processing and export-coupling factor. Its alignment beneath the export gate and ATP-sensitive pore loops fit this role. (bernal2019structuralanalysisof pages 1-2, bornicke2020invitroreconstitution pages 20-24)
Direct evidence for the broader cargo-processing model varies. InvC-specific mutagenesis supports chaperone-complex docking, while detailed mapping in the SPI-2 paralog SsaN places the docking interface in C-terminal helix 10 and identifies critical residues. That paralog evidence is mechanistically informative but cannot substitute for direct InvC assays. No reliable InvC-specific release kinetics or direct unfolding rate was recovered. (allison2014identificationofthe pages 7-8, allison2014identificationofthe pages 8-9)
InvC is essential for efficient SPI-1-mediated epithelial-cell entry. In one gentamicin-protection experiment, wild-type S. Typhimurium showed 88 ± 4% invasion, compared with 0.10 ± 0.03% for an invC mutant. Plasmids carrying functional invC restored invasion to 30 ± 2.1% or 21 ± 1.6%, whereas K165E InvC gave only 0.08 ± 0.04%. The mutant remained capable of attachment but failed to induce normal host-cell cytoskeletal rearrangements, placing InvC upstream of effector-dependent uptake signaling rather than general bacterial adhesion. (eichelberg1994molecularandfunctional pages 6-7)
Earlier measurements under a different presentation of the assay reported wild-type invasion of 58 ± 2% and mutant invasion of 0.11 ± 0.01%, again showing an approximately orders-of-magnitude defect. Differences between reported wild-type percentages likely reflect assay normalization or table context, but both datasets support the same conclusion. (eichelberg1994molecularandfunctional pages 4-5)
These phenotypes are consistent with failure to export the SPI-1 proteins that trigger actin remodeling and bacterial internalization. They do not establish that InvC independently controls transcription, metabolism, or host signaling; those effects are downstream consequences of a disabled secretion machine.
The 2023–2024 literature found in this search updates broader T3SS, Salmonella infection, and structural-genomics knowledge but adds little direct InvC-specific enzymology. A December 2024 authoritative review emphasizes the genetic diversity of S. enterica, its pathogenicity islands, and the variability of infection biology; it reports infectious-dose estimates ranging from approximately 30 to more than 10⁹ organisms, depending on strain, host, food matrix, and microbiota. This provides disease context but does not revise InvC’s molecular mechanism. (han2024infectionbiologyof pages 2-5)
A 2024 Salmonella pangenome study analyzed 79,758 strains, 13,147 proteins, and 17,238 domains. Among 272 proteins from 14 characterized pathogenicity islands, 90 were secretion-machinery proteins, and 41% of SPI-protein domains lacked prior sequence annotation. It also found 3,682 proteins enriched in clinical isolates. These results show that even well-known pathogenicity islands retain considerable annotation gaps, but the study did not add direct evidence on InvC ATP hydrolysis, localization, or cargo specificity. (medvedev2024structureclassificationof pages 1-2)
Thus, the most decisive InvC-specific advances remain the foundational 1994 biochemical/genetic study, 2017 in situ architecture, and 2019 ligand-bound structures and sorting-platform reconstitution. The absence of a 2023–2024 InvC-specific breakthrough should be reported rather than filling the gap with evidence from other SctN-family proteins.
InvC is an attractive research-stage antivirulence target because inhibiting it should disable SPI-1 secretion and epithelial invasion without necessarily blocking bacterial growth. Its conserved nucleotide pocket, oligomerization surfaces, and chaperone-docking region offer possible intervention sites. However, conservation with other bacterial secretion ATPases—and structural kinship with F1/V1/A1-type ATPases—creates selectivity challenges.
Target validation is essential. A 2022 study found that 100 μM C24H17ClN4O2S reduced epithelial-cell invasion by approximately 50% and inhibited SipA/SipC secretion without inhibiting bacterial growth, yet purified-InvC assays showed no inhibition at 10–100 μM. The compound instead affected SPI-1 regulation, illustrating why reduced secretion alone cannot establish InvC as the molecular target. (boonyom2022asmallmolecule pages 5-7)
No approved drug, clinical implementation, or human trial specifically targeting InvC was identified. Current applications are therefore preclinical: biochemical inhibitor screening, structure-guided design, reconstitution of secretion complexes, and use of invC mutants as T3SS-deficient controls.
InvC and its catalytic mutants provide tools for separating apparatus assembly from active secretion, testing cargo-selection models, and mapping sorting-platform organization. Because T3SSs can be repurposed for protein delivery, mechanistic knowledge of InvC may eventually help engineer secretion platforms, but the retrieved evidence does not establish a deployed InvC-based biotechnology.
High-confidence annotation: InvC/SctN1 is the SPI-1-associated cytoplasmic ATPase; it hydrolyzes ATP, occupies the central sorting-platform hub, and is required for secretion-dependent epithelial invasion. Its catalytic P-loop, Lys165, ATPase-core structure, and platform position are supported by complementary biochemistry, mutagenesis, crystallography, mass spectrometry, and in situ cryo-ET. (eichelberg1994molecularandfunctional pages 5-5, hu2017insitumolecular pages 5-6)
Moderate-confidence mechanistic extension: InvC recognizes chaperone-effector complexes and helps release/unfold cargo. This is consistent with InvC mutagenesis, ligand-induced pore-loop movements, and stronger direct experiments on SctN paralogs, but complete substrate-by-substrate InvC biochemistry remains unavailable. (allison2014identificationofthe pages 8-9, bernal2019structuralanalysisof pages 1-2)
Not presently justified: assigning one exclusive protein substrate; claiming broad nucleotide specificity measurements; describing InvC as an integral membrane transporter; claiming ATP hydrolysis alone powers translocation through the entire needle; or asserting a clinically validated InvC inhibitor.
References
(eichelberg1994molecularandfunctional pages 6-7): Katrin Eichelberg, C. Ginocchio, and J. Galán. Molecular and functional characterization of the salmonella typhimurium invasion genes invb and invc: homology of invc to the f0f1 atpase family of proteins. Journal of Bacteriology, 176:4501-4510, Aug 1994. URL: https://doi.org/10.1128/jb.176.15.4501-4510.1994, doi:10.1128/jb.176.15.4501-4510.1994. This article has 241 citations and is from a peer-reviewed journal.
(eichelberg1994molecularandfunctional pages 1-2): Katrin Eichelberg, C. Ginocchio, and J. Galán. Molecular and functional characterization of the salmonella typhimurium invasion genes invb and invc: homology of invc to the f0f1 atpase family of proteins. Journal of Bacteriology, 176:4501-4510, Aug 1994. URL: https://doi.org/10.1128/jb.176.15.4501-4510.1994, doi:10.1128/jb.176.15.4501-4510.1994. This article has 241 citations and is from a peer-reviewed journal.
(eichelberg1994molecularandfunctional pages 8-9): Katrin Eichelberg, C. Ginocchio, and J. Galán. Molecular and functional characterization of the salmonella typhimurium invasion genes invb and invc: homology of invc to the f0f1 atpase family of proteins. Journal of Bacteriology, 176:4501-4510, Aug 1994. URL: https://doi.org/10.1128/jb.176.15.4501-4510.1994, doi:10.1128/jb.176.15.4501-4510.1994. This article has 241 citations and is from a peer-reviewed journal.
(allison2014identificationofthe pages 8-9): Sarah E. Allison, Brian R. Tuinema, Ellen S. Everson, Seiji Sugiman-Marangos, Kun Zhang, Murray S. Junop, and Brian K. Coombes. Identification of the docking site between a type iii secretion system atpase and a chaperone for effector cargo. Journal of Biological Chemistry, 289:23734-23744, Aug 2014. URL: https://doi.org/10.1074/jbc.m114.578476, doi:10.1074/jbc.m114.578476. This article has 47 citations and is from a domain leading peer-reviewed journal.
(bernal2019structuralanalysisof pages 1-2): Ivonne Bernal, Jonas Römermann, Lara Flacht, Michele Lunelli, Charlotte Uetrecht, and Michael Kolbe. Structural analysis of ligand‐bound states of the salmonella type iii secretion system atpase invc. Protein Science, 28:1888-1901, Aug 2019. URL: https://doi.org/10.1002/pro.3704, doi:10.1002/pro.3704. This article has 13 citations and is from a peer-reviewed journal.
(eichelberg1994molecularandfunctional pages 5-5): Katrin Eichelberg, C. Ginocchio, and J. Galán. Molecular and functional characterization of the salmonella typhimurium invasion genes invb and invc: homology of invc to the f0f1 atpase family of proteins. Journal of Bacteriology, 176:4501-4510, Aug 1994. URL: https://doi.org/10.1128/jb.176.15.4501-4510.1994, doi:10.1128/jb.176.15.4501-4510.1994. This article has 241 citations and is from a peer-reviewed journal.
(bernal2019structuralanalysisof pages 2-3): Ivonne Bernal, Jonas Römermann, Lara Flacht, Michele Lunelli, Charlotte Uetrecht, and Michael Kolbe. Structural analysis of ligand‐bound states of the salmonella type iii secretion system atpase invc. Protein Science, 28:1888-1901, Aug 2019. URL: https://doi.org/10.1002/pro.3704, doi:10.1002/pro.3704. This article has 13 citations and is from a peer-reviewed journal.
(hu2017insitumolecular pages 5-6): Bo Hu, Maria Lara-Tejero, Qingke Kong, Jorge E. Galán, and Jun Liu. In situ molecular architecture of the salmonella type iii secretion machine. Cell, 168:1065-1074.e10, Mar 2017. URL: https://doi.org/10.1016/j.cell.2017.02.022, doi:10.1016/j.cell.2017.02.022. This article has 264 citations and is from a highest quality peer-reviewed journal.
(bornicke2020invitroreconstitution pages 71-74): CJ Börnicke. In vitro reconstitution and characterization of soluble complexes of the salmonella type iii secretion system sorting platform. Unknown journal, 2020.
(bornicke2020invitroreconstitution pages 68-71): CJ Börnicke. In vitro reconstitution and characterization of soluble complexes of the salmonella type iii secretion system sorting platform. Unknown journal, 2020.
(bornicke2020invitroreconstitutiona pages 62-68): CJ Börnicke. In vitro reconstitution and characterization of soluble complexes of the salmonella type iii secretion system sorting platform. Unknown journal, 2020.
(bornicke2020invitroreconstitution pages 62-68): CJ Börnicke. In vitro reconstitution and characterization of soluble complexes of the salmonella type iii secretion system sorting platform. Unknown journal, 2020.
(medvedev2024structureclassificationof pages 1-2): Kirill E. Medvedev, Jing Zhang, R. Dustin Schaeffer, Lisa N. Kinch, Qian Cong, and Nick V. Grishin. Structure classification of the proteins from salmonella enterica pangenome revealed novel potential pathogenicity islands. May 2024. URL: https://doi.org/10.1038/s41598-024-60991-x, doi:10.1038/s41598-024-60991-x. This article has 12 citations and is from a peer-reviewed journal.
(eichelberg1994molecularandfunctional pages 7-8): Katrin Eichelberg, C. Ginocchio, and J. Galán. Molecular and functional characterization of the salmonella typhimurium invasion genes invb and invc: homology of invc to the f0f1 atpase family of proteins. Journal of Bacteriology, 176:4501-4510, Aug 1994. URL: https://doi.org/10.1128/jb.176.15.4501-4510.1994, doi:10.1128/jb.176.15.4501-4510.1994. This article has 241 citations and is from a peer-reviewed journal.
(bornicke2020invitroreconstitution pages 74-77): CJ Börnicke. In vitro reconstitution and characterization of soluble complexes of the salmonella type iii secretion system sorting platform. Unknown journal, 2020.
(bornicke2020invitroreconstitution pages 20-24): CJ Börnicke. In vitro reconstitution and characterization of soluble complexes of the salmonella type iii secretion system sorting platform. Unknown journal, 2020.
(bornicke2020invitroreconstitution pages 58-62): CJ Börnicke. In vitro reconstitution and characterization of soluble complexes of the salmonella type iii secretion system sorting platform. Unknown journal, 2020.
(allison2014identificationofthe pages 7-8): Sarah E. Allison, Brian R. Tuinema, Ellen S. Everson, Seiji Sugiman-Marangos, Kun Zhang, Murray S. Junop, and Brian K. Coombes. Identification of the docking site between a type iii secretion system atpase and a chaperone for effector cargo. Journal of Biological Chemistry, 289:23734-23744, Aug 2014. URL: https://doi.org/10.1074/jbc.m114.578476, doi:10.1074/jbc.m114.578476. This article has 47 citations and is from a domain leading peer-reviewed journal.
(eichelberg1994molecularandfunctional pages 4-5): Katrin Eichelberg, C. Ginocchio, and J. Galán. Molecular and functional characterization of the salmonella typhimurium invasion genes invb and invc: homology of invc to the f0f1 atpase family of proteins. Journal of Bacteriology, 176:4501-4510, Aug 1994. URL: https://doi.org/10.1128/jb.176.15.4501-4510.1994, doi:10.1128/jb.176.15.4501-4510.1994. This article has 241 citations and is from a peer-reviewed journal.
(han2024infectionbiologyof pages 2-5): Jing Han, Nesreen Aljahdali, Shaohua Zhao, Hailin Tang, Heather Harbottle, Maria Hoffmann, Jonathan G. Frye, and Steven L. Foley. Infection biology of salmonella enterica. EcoSal Plus, Dec 2024. URL: https://doi.org/10.1128/ecosalplus.esp-0001-2023, doi:10.1128/ecosalplus.esp-0001-2023. This article has 129 citations.
(boonyom2022asmallmolecule pages 5-7): Rerngwit Boonyom, Sittiruk Roytrakul, and Patipat Thinwang. A small molecule, c24h17cln4o2s, inhibits the function of the type iii secretion system in salmonella typhimurium. Journal of Genetic Engineering and Biotechnology, 20:54, Dec 2022. URL: https://doi.org/10.1186/s43141-022-00336-1, doi:10.1186/s43141-022-00336-1. This article has 7 citations.