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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 UniProt target Q88F17 is annotated as Aquaporin Z (AqpZ) from Pseudomonas putida strain KT2440 (ordered locus PP_4282), belonging to the MIP/aquaporin (TC 1.A.8) family. Within the literature retrieved using the provided tools, no primary experimental study was found that directly characterizes PP_4282/Q88F17 (e.g., deletion phenotype, permeability measurements, localization assays, or structure) in P. putida KT2440. Therefore, the most defensible functional annotation for Q88F17 must be framed as orthology- and mechanism-based inference from canonical bacterial AqpZ work (especially E. coli AqpZ), with explicit separation of direct KT2440 evidence vs inference. (fan2024improvementinsalt pages 2-3, savage2003architectureandselectivity pages 2-3, tong2019prokaryoticaquaporins pages 1-3)
Aquaporins are integral membrane proteins of the Major Intrinsic Protein (MIP) superfamily that facilitate diffusion of water and (in some family members) other small uncharged solutes across biological membranes. Prokaryotic aquaporins are commonly grouped into water-selective aquaporins (AQPs), aquaglyceroporins (GLPs) (glycerol-permeable), and more divergent/unorthodox types with alternative substrate profiles. (tong2019prokaryoticaquaporins pages 1-3)
AqpZ is the name historically used for a bacterial water-selective aquaporin best characterized in Escherichia coli. The defining mechanistic features of AqpZ-like water channels include:
- Tetrameric assembly in the membrane, with each monomer forming an independent pore. (savage2003architectureandselectivity pages 2-3, savage2003architectureandselectivity pages 3-4)
- A conserved aquaporin fold: six transmembrane helices plus two half-helices, and signature conserved motifs including two NPA motifs that form a central constriction important for selectivity and proton exclusion. (savage2003architectureandselectivity pages 2-3, tong2019prokaryoticaquaporins pages 1-3, savage2003architectureandselectivity pages 3-4)
- A second constriction—the aromatic/arginine (ar/R) selectivity filter—that strongly influences substrate specificity (water vs glycerol). (tong2019prokaryoticaquaporins pages 1-3, tong2019prokaryoticaquaporins pages 7-9)
Because PP_4282 is annotated as Aquaporin Z and belongs to aquaporin/MIP families, and because bacterial AqpZ has been repeatedly shown to be a water-selective channel in canonical systems, the most conservative functional claim for P. putida KT2440 Q88F17 is:
AqpZ (Q88F17) is likely an inner-membrane aquaporin that facilitates rapid, selective transmembrane water flux (osmotic water permeability).
Mechanistic support from the canonical AqpZ structure indicates strong water selectivity driven by a narrow, hydrophilic filter region and single-file water transport; functional data summarized in authoritative prokaryotic aquaporin reviews indicate that AqpZ behaves as an “exclusive water facilitator” (water transport detectable; glycerol/urea transport not detected in standard assays). (savage2003architectureandselectivity pages 3-4, tong2019prokaryoticaquaporins pages 7-9, tong2019prokaryoticaquaporins pages 9-11)
Important limitation: the above statement is inferred; no direct permeability assay for P. putida KT2440 Q88F17 was present in retrieved evidence. (fan2024improvementinsalt pages 2-3)
The E. coli AqpZ 2.5 Å X-ray structure provides direct structural rationale for discrimination between water and glycerol: the pore is narrow (filter ~2 Å) and lined by residues that stabilize water but sterically/chemically disfavor glycerol; in contrast, the bacterial aquaglyceroporin GlpF has substitutions that enlarge/hydrophobize the filter to accommodate glycerol. (savage2003architectureandselectivity pages 3-4)
A prokaryotic aquaporin review further summarizes that AqpZ shows high water permeability with low activation energy and that heterologous/reconstituted assays did not detect transport of nonionic solutes such as glycerol or urea for AqpZ. (tong2019prokaryoticaquaporins pages 7-9, tong2019prokaryoticaquaporins pages 9-11)
Inference for Q88F17: by family assignment (Aquaporin Z) and the conserved AqpZ mechanism, Q88F17 is expected to be water-selective rather than glycerol-permeable. (tong2019prokaryoticaquaporins pages 7-9, tong2019prokaryoticaquaporins pages 9-11)
A key aquaporin concept is that high water permeability must not collapse proton gradients. The AqpZ structure supports a proton exclusion mechanism in which pore electrostatics and the NPA region orient a central water such that it cannot support continuous proton hopping along a water wire. (savage2003architectureandselectivity pages 3-4)
Inference for Q88F17: proton exclusion is expected to be conserved in AqpZ-like water channels because it is tightly coupled to the canonical aquaporin fold and the NPA/ar/R architecture. (tong2019prokaryoticaquaporins pages 1-3, savage2003architectureandselectivity pages 3-4)
Structural evidence indicates AqpZ is an integral membrane protein with a canonical six-transmembrane helix fold, assembling as a homotetramer, with the N-terminus on the cytoplasmic side (as shown for E. coli AqpZ). (savage2003architectureandselectivity pages 2-3)
Inference for Q88F17: consistent with the MIP/aquaporin family and AqpZ orthology, PP_4282 is expected to localize to the cytoplasmic (inner) membrane of this Gram-negative bacterium and form tetramers, with one functional water pore per monomer. (savage2003architectureandselectivity pages 2-3, tong2019prokaryoticaquaporins pages 1-3)
An authoritative review of prokaryotic aquaporins summarizes that AqpZ in canonical bacterial contexts supports rapid water influx/efflux during sudden osmotic shifts (hypo-osmotic induction noted; role in osmoregulation and competitive viability). (tong2019prokaryoticaquaporins pages 9-11)
Inference for P. putida KT2440: Q88F17 AqpZ likely contributes to water homeostasis during osmotic transitions (e.g., sudden changes in external osmolarity), complementing other osmotic systems (compatible solute metabolism/transport; mechanosensitive channels). (tong2019prokaryoticaquaporins pages 9-11)
A recent KT2440 salt-tolerance study used RNA-seq under 5% w/v NaCl and identified key salt response processes (membrane components, redox processes, chemotaxis, catabolic processes) and prioritized genes such as betB and an exogenous Na+/H+ antiporter for engineering; however, aqpZ/aquaporin was not explicitly highlighted among validated targets in the retrieved excerpt. (fan2024improvementinsalt pages 2-3)
This absence does not falsify an aqpZ role in KT2440, but it does mean that, in the retrieved evidence, aqpZ is not currently a leading experimentally validated KT2440 salt-tolerance determinant.
A key recent advance is an in situ/near-native structural determination of AqpZ by solid-state NMR directly in E. coli inner membranes. The authors report complete chemical shift assignments and extraction of extensive restraints (reported as 1017 distance restraints in the summary excerpt) enabling a ~1.7 Å ssNMR structure in cellular membranes, supported by specialized labeling/sample preparation to suppress background signals. (xie2023solidstatenmrstructure pages 1-2, xie2023solidstatenmrstructure pages 3-5)
Relevance to Q88F17 annotation: this strengthens confidence that the canonical AqpZ fold and tetramer organization observed in purified/detergent environments is representative of native bacterial membranes, supporting transfer of mechanistic inference to bacterial AqpZ orthologs such as P. putida PP_4282. (xie2023solidstatenmrstructure pages 1-2, xie2023solidstatenmrstructure pages 3-5)
A 2023 biophysical study observed that AqpZ preparations can show higher-order assemblies in detergent and nanodiscs (mass photometry peaks including ~183 kDa for tetramer+detergent and up to ~604 kDa species interpreted as stacked tetramers with additional detergent). It also reports AqpZ-containing nanodiscs with major mass ~198 kDa and evidence for nanodisc filament/stack formation that is AqpZ-dependent and disrupted by adding sub-CMC octyl glucoside. (surya2023anomalousoligomerizationbehavior pages 4-7, surya2023anomalousoligomerizationbehavior pages 2-4)
Expert interpretation: AqpZ’s charge asymmetry (cytoplasmic face more positive; extracellular more negative) may favor head-to-tail stacking, implying that sample environment can create non-physiological oligomerization that should be controlled for in structural/functional studies. (surya2023anomalousoligomerizationbehavior pages 1-2, surya2023anomalousoligomerizationbehavior pages 4-7)
A 2024 Analytical Chemistry paper applied native MS (with charge-reducing additives such as spermine and TMAO) to quantify AqpZ–lipid binding in different detergents. Key quantitative findings include:
- Stoichiometry shifts: AqpZ binds up to ~17 POPE in LDAO versus ~10 in DM/C8E4, illustrating strong environment dependence. (kumar2024nativemassspectrometry pages 5-7)
- Affinity for cardiolipin analog (TOCDL): highest affinity in LDAO with Kd1 ≈ 0.3–1.4 μM; AqpZ–TOCDL interactions were reported as >20-fold enhanced relative to DM. (kumar2024nativemassspectrometry pages 5-7, kumar2024nativemassspectrometry pages 8-9)
Expert interpretation: reported Kd values reflect both intrinsic lipid affinity and competition with detergents at binding sites, meaning detergent selection is part of the “measurement model,” not just a technicality. (kumar2024nativemassspectrometry pages 8-9)
AqpZ has been incorporated into block-copolymer vesicle membranes to create highly water-permeable, solute-rejecting membranes. In a widely cited PNAS study:
- Osmotic shrinkage kinetics differed dramatically: 5–20 ms for AqpZ-containing polymer vesicles versus ~10 s for polymer-only vesicles. (kumar2007highlypermeablepolymeric pages 1-3)
- Activation energy for water transport decreased to ~3.4 kcal/mol for AqpZ-polymer vesicles, consistent with channel-mediated water transport. (kumar2007highlypermeablepolymeric pages 1-1, kumar2007highlypermeablepolymeric pages 3-4)
- Reported productivity gains included ~800-fold improvement and performance exceeding benchmark salt-rejecting membranes in their comparisons. (kumar2007highlypermeablepolymeric pages 4-4)
Although these implementations use recombinant AqpZ (historically E. coli AqpZ), they demonstrate how AqpZ-family channels can be deployed as functional nanofluidic elements in engineered membranes. (kumar2007highlypermeablepolymeric pages 4-4, kumar2007highlypermeablepolymeric pages 1-3)
The 2024 native-MS work positions AqpZ as a model for developing conditions (detergent + charge reducer) that preserve oligomeric state and allow quantification of lipid binding, with stated relevance to biochemical/structural investigations and potential drug discovery workflows. (kumar2024nativemassspectrometry pages 1-2, kumar2024nativemassspectrometry pages 8-9)
The following table separates direct KT2440 evidence from cross-organism inference, and provides URLs/DOIs and quantitative data.
| Claim/annotation | Evidence type (structure/biophysics/genetics/transcriptomics/method) | Organism/system | Key quantitative data | Key mechanistic details (motifs/ar/R/NPA/tetramer) | Year | Source URL/DOI | Citation ID |
|---|---|---|---|---|---|---|---|
| Direct evidence in P. putida KT2440 is limited: no organism-specific experimental characterization of PP_4282/AqpZ was identified in the retrieved literature; annotation therefore relies mainly on orthology/family assignment plus general bacterial AqpZ evidence. | Literature gap / annotation status | Pseudomonas putida KT2440 (Q88F17/PP_4282) | No direct permeability, knockout, or structural data found for PP_4282 in retrieved sources | UniProt/domain context is consistent with MIP/aquaporin family, but retrieved papers did not experimentally test PP_4282 | 2024 | https://doi.org/10.3390/biology13060404 | (fan2024improvementinsalt pages 2-3) |
| No explicit aqpZ signal in retrieved KT2440 salt-stress transcriptomics: a recent KT2440 salt-tolerance RNA-seq study highlighted osmolyte and ion-homeostasis genes, but did not report aqpZ/aquaporin among validated salt-response hits. | Transcriptomics | P. putida KT2440 under 5% w/v NaCl | RNA-seq thresholds included log2FC >= 1 and p <= 0.05; engineered strains reached 5-6% w/v NaCl tolerance, but aqpZ was not highlighted | Suggests aqpZ was not a prominent validated salt-response determinant in this dataset; absence of evidence is not evidence of absence | 2024 | https://doi.org/10.3390/biology13060404 | (fan2024improvementinsalt pages 2-3) |
| Likely primary function (inferred): water-selective channel rather than glycerol channel. | Orthology-based functional inference from biophysics/structure | Canonical bacterial AqpZ, primarily Escherichia coli | Heterologous or reconstitution assays reported high water permeability with low activation energy; nonionic solutes such as glycerol and urea were not detected as AqpZ substrates | Orthodox aquaporin architecture; distinct from GlpF aquaglyceroporin | 2019 | https://doi.org/10.3390/cells8111316 | (tong2019prokaryoticaquaporins pages 7-9, tong2019prokaryoticaquaporins pages 9-11) |
| Membrane localization and topology (inferred for PP_4282): inner-membrane integral protein with six transmembrane helices, two half-helices, cytoplasmic N-terminus, and one pore per monomer. | Structure | E. coli AqpZ X-ray structure, used for inference to bacterial AqpZ orthologs | Channel length about 28 A; selectivity filter about 2 A diameter; pore width less than 4 A | Canonical MIP fold with 6 TM helices plus 2 half-helices; homotetrameric assembly | 2003 | https://doi.org/10.1371/journal.pbio.0000072 | (savage2003architectureandselectivity pages 2-3, savage2003architectureandselectivity pages 3-4) |
| Tetrameric organization is a conserved hallmark of AqpZ and likely applies to PP_4282. | Structure / biophysics | E. coli AqpZ in nanodiscs, detergent, and native membranes | Mass photometry detected about 198 kDa AqpZ-containing nanodiscs; detergent-associated AqpZ tetramer peak about 183 kDa; native-membrane ssNMR used intermonomer restraints to define tetramer | Tetramer stable in membranes; each monomer forms an individual water pore | 2003, 2023 | https://doi.org/10.1371/journal.pbio.0000072 ; https://doi.org/10.3390/ijms24098098 ; https://doi.org/10.1126/sciadv.adh4168 | (savage2003architectureandselectivity pages 2-3, xie2023solidstatenmrstructure pages 3-5, surya2023anomalousoligomerizationbehavior pages 4-7, surya2023anomalousoligomerizationbehavior pages 2-4) |
| Selectivity filter residues define water specificity. | Structure / mechanism | E. coli AqpZ | Selectivity filter contains a bound water; constriction about 2 A | ar/R region residues include Phe43, His174, Thr183, and Arg189; pore is narrow and relatively hydrophilic, favoring water and excluding glycerol | 2003 | https://doi.org/10.1371/journal.pbio.0000072 | (savage2003architectureandselectivity pages 3-4, tong2019prokaryoticaquaporins pages 7-9) |
| NPA motifs are central to channel architecture and proton exclusion. | Structure / mechanism | Canonical bacterial AqpZ | Five waters resolved in single file in pore | Two conserved NPA motifs form the central constriction; asparagines orient pore waters and disrupt proton-wire formation | 2003, 2019 | https://doi.org/10.1371/journal.pbio.0000072 ; https://doi.org/10.3390/cells8111316 | (savage2003architectureandselectivity pages 2-3, tong2019prokaryoticaquaporins pages 1-3, savage2003architectureandselectivity pages 3-4) |
| Proton exclusion mechanism: AqpZ conducts water but blocks proton leakage. | Structure / mechanism | E. coli AqpZ | Structural model based on resolved waters and hydrogen-bond geometry | Central waters are forced into orientations that prevent continuous proton hopping; electrostatics at the NPA region contribute | 2003 | https://doi.org/10.1371/journal.pbio.0000072 | (savage2003architectureandselectivity pages 3-4) |
| Physiological role in osmoregulation (inferred for PP_4282): AqpZ facilitates rapid water influx and efflux during sudden osmotic shifts. | Genetics / physiology | E. coli AqpZ | AqpZ loss reduces competitive viability at low osmolarity; aqpZ is induced by hypo-osmotic conditions in reviewed studies | Supports rapid cell-volume adjustment rather than osmolyte transport | 2019 | https://doi.org/10.3390/cells8111316 | (tong2019prokaryoticaquaporins pages 9-11) |
| Gating remains debated, but current view disfavors strong physiological gating by R189. | Mechanism / regulatory interpretation | E. coli AqpZ | Earlier gating proposals focused on Arg189; later work in bilayers and native membranes argued channel is constitutively open | R189 in the selectivity filter was proposed as gate, but later solid-state NMR and native-membrane work suggested prior gating observations reflected detergent effects | 2019, 2023 | https://doi.org/10.3390/cells8111316 ; https://doi.org/10.1126/sciadv.adh4168 | (tong2019prokaryoticaquaporins pages 11-12, xie2023solidstatenmrstructure pages 1-2) |
| Recent structural advance: AqpZ structure was determined directly in native bacterial inner membranes by ssNMR, strengthening confidence in native-state annotation. | Method / structure | E. coli inner membrane | 1017 distance restraints; 1007 C13-C13 restraints in one summary; 1.7 A ssNMR structure; background labeling reduced to within about 7 percent of AqpZ level; about 48 percent decrease in AqpZ expression under suppression protocol | Confirms native-membrane tetrameric architecture and close similarity to prior synthetic-membrane structures | 2023 | https://doi.org/10.1126/sciadv.adh4168 | (xie2023solidstatenmrstructure pages 3-5, xie2023solidstatenmrstructure pages 1-2, xie2023solidstatenmrstructure pages 8-9) |
| Recent oligomerization finding: AqpZ can form higher-order head-to-tail stacks in nanodiscs or detergent, an important caution for structural interpretation. | Biophysics / method | E. coli AqpZ in nanodiscs and LMNG detergent | Species at about 183, 327, 464, and 604 kDa; mass increments about 137-144 kDa; dominant nanodisc species about 198 kDa; AUC peak about 6.5 S with additional species at 9.5, 12.5, and 15.5 S | Electrostatic asymmetry between cytoplasmic and extracellular faces may promote head-to-tail stacking; empty nanodiscs lacked filaments | 2023 | https://doi.org/10.3390/ijms24098098 | (surya2023anomalousoligomerizationbehavior pages 4-7, surya2023anomalousoligomerizationbehavior pages 1-2, surya2023anomalousoligomerizationbehavior pages 2-4) |
| Recent lipid-interaction advance: AqpZ-lipid binding is strongly detergent-dependent, with LDAO enhancing detectable cardiolipin and phospholipid association. | Biophysics / native MS | Purified AqpZ in detergents | Up to about 10 POPE bound in DM or C8E4, up to 17 in LDAO; NG showed up to 8 POPG-associated states in one condition; TOCDL Kd1 about 0.3-1.4 uM in LDAO; more than 20-fold enhancement of AqpZ-TOCDL interaction relative to DM | Charge-reducing additives SPM and TMAO preserve tetramer and shift charge states; detergent competition complicates apparent Kd values | 2024 | https://doi.org/10.1021/acs.analchem.4c03312 | (kumar2024nativemassspectrometry pages 8-9, kumar2024nativemassspectrometry pages 7-8, kumar2024nativemassspectrometry pages 5-7, kumar2024nativemassspectrometry pages 2-3, kumar2024nativemassspectrometry pages 3-5, kumar2024nativemassspectrometry pages 1-2) |
| Biomimetic application: AqpZ has been implemented in polymeric membranes to create highly water-permeable yet solute-rejecting membranes. | Application / biophysics | AqpZ reconstituted into PMOXA-PDMS-PMOXA polymer vesicles | Initial osmotic shrinkage time 5-20 ms for AqpZ-ABA vesicles versus about 10 s for polymer-only vesicles; permeability increased about 38-94 times in reported experiments and up to about 3000 times at an optimal ratio in one condition; overall productivity improved about 800-fold; activation energy 3.4 kcal/mol versus 8.7 kcal/mol for polymer alone | Demonstrates that AqpZ can retain water selectivity in synthetic membranes; supports real-world membrane-engineering relevance of the AqpZ family | 2007 | https://doi.org/10.1073/pnas.0708762104 | (kumar2007highlypermeablepolymeric pages 4-4, kumar2007highlypermeablepolymeric pages 1-1, kumar2007highlypermeablepolymeric pages 4-5, kumar2007highlypermeablepolymeric pages 3-4, kumar2007highlypermeablepolymeric pages 1-3, kumar2007highlypermeablepolymeric pages 5-6) |
| Most defensible functional annotation for UniProt Q88F17 and PP_4282: probable inner-membrane homotetrameric orthodox aquaporin that mediates selective water flux for osmoadaptation; direct KT2440-specific evidence remains lacking in retrieved literature. | Integrated annotation | P. putida KT2440 PP_4282 inferred from bacterial AqpZ orthology | Quantitative data currently come from homologous bacterial AqpZ systems rather than PP_4282 itself | Supported by MIP family membership, aquaporin domains, and conserved AqpZ structural principles including 6 TM helices, dual NPA motifs, ar/R filter, and tetrameric assembly | 2003-2024 | https://doi.org/10.1371/journal.pbio.0000072 ; https://doi.org/10.3390/cells8111316 ; https://doi.org/10.1126/sciadv.adh4168 | (savage2003architectureandselectivity pages 2-3, tong2019prokaryoticaquaporins pages 1-3, tong2019prokaryoticaquaporins pages 9-11, xie2023solidstatenmrstructure pages 3-5, fan2024improvementinsalt pages 2-3) |
Table: This table separates direct evidence for Pseudomonas putida KT2440 PP_4282 from inference based on canonical bacterial AqpZ studies, especially E. coli. It is useful for tracing which functional claims are experimentally supported for the target organism versus transferred by orthology and conserved aquaporin mechanism.
References
(fan2024improvementinsalt pages 2-3): Min Fan, Shuyu Tan, Wei Wang, and Xuehong Zhang. Improvement in salt tolerance ability of pseudomonas putida kt2440. Biology, 13:404, Jun 2024. URL: https://doi.org/10.3390/biology13060404, doi:10.3390/biology13060404. This article has 25 citations.
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(kumar2007highlypermeablepolymeric pages 1-3): Manish Kumar, Mariusz Grzelakowski, Julie Zilles, Mark Clark, and Wolfgang Meier. Highly permeable polymeric membranes based on the incorporation of the functional water channel protein aquaporin z. Proceedings of the National Academy of Sciences, 104:20719-20724, Dec 2007. URL: https://doi.org/10.1073/pnas.0708762104, doi:10.1073/pnas.0708762104. This article has 870 citations and is from a highest quality peer-reviewed journal.
(kumar2007highlypermeablepolymeric pages 1-1): Manish Kumar, Mariusz Grzelakowski, Julie Zilles, Mark Clark, and Wolfgang Meier. Highly permeable polymeric membranes based on the incorporation of the functional water channel protein aquaporin z. Proceedings of the National Academy of Sciences, 104:20719-20724, Dec 2007. URL: https://doi.org/10.1073/pnas.0708762104, doi:10.1073/pnas.0708762104. This article has 870 citations and is from a highest quality peer-reviewed journal.
(kumar2007highlypermeablepolymeric pages 3-4): Manish Kumar, Mariusz Grzelakowski, Julie Zilles, Mark Clark, and Wolfgang Meier. Highly permeable polymeric membranes based on the incorporation of the functional water channel protein aquaporin z. Proceedings of the National Academy of Sciences, 104:20719-20724, Dec 2007. URL: https://doi.org/10.1073/pnas.0708762104, doi:10.1073/pnas.0708762104. This article has 870 citations and is from a highest quality peer-reviewed journal.
(kumar2007highlypermeablepolymeric pages 4-4): Manish Kumar, Mariusz Grzelakowski, Julie Zilles, Mark Clark, and Wolfgang Meier. Highly permeable polymeric membranes based on the incorporation of the functional water channel protein aquaporin z. Proceedings of the National Academy of Sciences, 104:20719-20724, Dec 2007. URL: https://doi.org/10.1073/pnas.0708762104, doi:10.1073/pnas.0708762104. This article has 870 citations and is from a highest quality peer-reviewed journal.
(kumar2024nativemassspectrometry pages 1-2): Smriti Kumar, Lauren Stover, Lie Wang, Hanieh Bahramimoghaddam, Ming Zhou, David H. Russell, and Arthur Laganowsky. Native mass spectrometry of membrane protein–lipid interactions in different detergent environments. Analytical Chemistry, 96:16768-16776, Oct 2024. URL: https://doi.org/10.1021/acs.analchem.4c03312, doi:10.1021/acs.analchem.4c03312. This article has 15 citations and is from a highest quality peer-reviewed journal.
(tong2019prokaryoticaquaporins pages 11-12): Huichun Tong, Qingqing Hu, Lin Zhu, and Xiuzhu Dong. Prokaryotic aquaporins. Cells, 8:1316, Oct 2019. URL: https://doi.org/10.3390/cells8111316, doi:10.3390/cells8111316. This article has 34 citations.
(xie2023solidstatenmrstructure pages 8-9): Huayong Xie, Yongxiang Zhao, Weijing Zhao, Yanke Chen, Maili Liu, and Jun Yang. Solid-state nmr structure determination of a membrane protein in e. coli cellular inner membrane. Nov 2023. URL: https://doi.org/10.1126/sciadv.adh4168, doi:10.1126/sciadv.adh4168. This article has 35 citations and is from a highest quality peer-reviewed journal.
(kumar2024nativemassspectrometry pages 7-8): Smriti Kumar, Lauren Stover, Lie Wang, Hanieh Bahramimoghaddam, Ming Zhou, David H. Russell, and Arthur Laganowsky. Native mass spectrometry of membrane protein–lipid interactions in different detergent environments. Analytical Chemistry, 96:16768-16776, Oct 2024. URL: https://doi.org/10.1021/acs.analchem.4c03312, doi:10.1021/acs.analchem.4c03312. This article has 15 citations and is from a highest quality peer-reviewed journal.
(kumar2024nativemassspectrometry pages 2-3): Smriti Kumar, Lauren Stover, Lie Wang, Hanieh Bahramimoghaddam, Ming Zhou, David H. Russell, and Arthur Laganowsky. Native mass spectrometry of membrane protein–lipid interactions in different detergent environments. Analytical Chemistry, 96:16768-16776, Oct 2024. URL: https://doi.org/10.1021/acs.analchem.4c03312, doi:10.1021/acs.analchem.4c03312. This article has 15 citations and is from a highest quality peer-reviewed journal.
(kumar2024nativemassspectrometry pages 3-5): Smriti Kumar, Lauren Stover, Lie Wang, Hanieh Bahramimoghaddam, Ming Zhou, David H. Russell, and Arthur Laganowsky. Native mass spectrometry of membrane protein–lipid interactions in different detergent environments. Analytical Chemistry, 96:16768-16776, Oct 2024. URL: https://doi.org/10.1021/acs.analchem.4c03312, doi:10.1021/acs.analchem.4c03312. This article has 15 citations and is from a highest quality peer-reviewed journal.
(kumar2007highlypermeablepolymeric pages 4-5): Manish Kumar, Mariusz Grzelakowski, Julie Zilles, Mark Clark, and Wolfgang Meier. Highly permeable polymeric membranes based on the incorporation of the functional water channel protein aquaporin z. Proceedings of the National Academy of Sciences, 104:20719-20724, Dec 2007. URL: https://doi.org/10.1073/pnas.0708762104, doi:10.1073/pnas.0708762104. This article has 870 citations and is from a highest quality peer-reviewed journal.
(kumar2007highlypermeablepolymeric pages 5-6): Manish Kumar, Mariusz Grzelakowski, Julie Zilles, Mark Clark, and Wolfgang Meier. Highly permeable polymeric membranes based on the incorporation of the functional water channel protein aquaporin z. Proceedings of the National Academy of Sciences, 104:20719-20724, Dec 2007. URL: https://doi.org/10.1073/pnas.0708762104, doi:10.1073/pnas.0708762104. This article has 870 citations and is from a highest quality peer-reviewed journal.