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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 protein is SbCASP1, annotated in UniProt as Casparian strip membrane protein 1 from Sorghum bicolor (UniProt accession C5YAP3; locus Sb06g033470) and belonging to the CASP/CASPL (Casparian strip membrane domain protein) family (user-supplied UniProt context). In the retrievable literature corpus for this run, I did not obtain a primary publication that explicitly mentions C5YAP3 or Sb06g033470; thus, SbCASP1 functional statements below are primarily inferred from conserved CASP-family mechanisms, and are supported by direct experimental evidence from closely related cereal CASP homologs (notably sorghum SbCASP4 and sorghum SbCASP‑LP1C1) and from Arabidopsis/rice CASP research (direct evidence for family function). This approach avoids a common ambiguity where “CASP1” could refer to unrelated genes in other kingdoms; here it is clearly plant Casparian strip membrane domain protein literature. (xue2024comparativeanalysisof pages 18-19, wei2021sbcasp4improvessalt pages 1-2)
| Claim/Topic | Key takeaway | Species/context | Evidence type (direct vs inference) | Publication (authors, year) | URL/DOI | Citation ID(s) |
|---|---|---|---|---|---|---|
| Target identity & limitations | The target is Sorghum bicolor CASP-family protein CASP1 from UniProt C5YAP3 / Sb06g033470, but no direct primary literature for SbCASP1/C5YAP3 was retrieved in the available corpus. Functional annotation therefore should be restricted to CASP-family inference plus cereal/sorghum homolog evidence, avoiding unrelated non-plant “CASP1” genes. | Sorghum bicolor; family-level annotation constrained by missing direct paper on C5YAP3 | Direct for limitation; inference for function | Xue et al., 2024; Wei et al., 2021 | https://doi.org/10.3390/ijms25189858 ; https://doi.org/10.1007/s00425-021-03731-z | (xue2024comparativeanalysisof pages 18-19, wei2021sbcasp4improvessalt pages 1-2) |
| CASP/CASPL definitions and domains | CASPs are Casparian strip membrane domain proteins; CASPLs are the broader related family. Family identification in recent plant comparative work uses DUF588 / PF04535; evolutionary analyses link CASPLs to MARVEL-like proteins/domains. | Arabidopsis, rice, plant-wide evolutionary context | Inference for SbCASP1 from conserved family/domain membership | Roppolo et al., 2014; Xue et al., 2024 | https://doi.org/10.1104/pp.114.239137 ; https://doi.org/10.3390/ijms25189858 | (roppolo2014functionalandevolutionary pages 1-2, roppolo2014functionalandevolutionary pages 14-17, xue2024comparativeanalysisof pages 1-2) |
| Topology and localization | CASPs are four-transmembrane-span proteins with cytosolic N- and C-termini. They accumulate in the Casparian strip membrane domain (CSD), a specialized plasma-membrane domain of root endodermal cells; sorghum SbCASP4 is likewise plasma-membrane localized and expressed in endodermis/Casparian-strip region. | Arabidopsis foundational mechanism; sorghum homolog support | Inference for SbCASP1 from family; direct for sorghum homolog SbCASP4 | Roppolo et al., 2014; Wei et al., 2021 | https://doi.org/10.1104/pp.114.239137 ; https://doi.org/10.1007/s00425-021-03731-z | (roppolo2014functionalandevolutionary pages 1-2, roppolo2014functionalandevolutionary pages 1-1, wei2021sbcasp4improvessalt pages 3-6, wei2021sbcasp4improvessalt pages 6-9, wei2021sbcasp4improvessalt pages 12-13) |
| Mechanistic role | CASPs function as a stable membrane scaffold/fence that helps define the CSD and recruits lignin polymerization machinery for Casparian strip formation. Recent synthesis notes recruitment/organization of RBOHF, ESB1, PER64, UCC1 and related enzymes required for endodermal lignification and diffusion-barrier formation. | Root endodermis / Casparian strip | Inference for SbCASP1 from conserved mechanism | Roppolo et al., 2014; Xue et al., 2024; Wang et al., 2020 | https://doi.org/10.1104/pp.114.239137 ; https://doi.org/10.3390/ijms25189858 ; https://doi.org/10.1186/s12864-020-6723-9 | (roppolo2014functionalandevolutionary pages 1-2, roppolo2014functionalandevolutionary pages 1-1, xue2024comparativeanalysisof pages 1-2, wang2020casparianstripmembrane pages 1-2) |
| Regulation/signaling | CASP-mediated barrier assembly is regulated by MYB36 and monitored by the CIF1/2–SGN3–SGN1 (SCHENGEN) pathway. MYB36 activates CASP1, ESB1, PER64 and related genes; SGN signaling senses barrier defects and promotes compensatory lignification/suberization. | Mainly Arabidopsis; broadly conserved endodermal barrier pathway | Inference for SbCASP1 from conserved pathway; direct support from sorghum homolog response signatures | Manzano et al., 2025; Xue et al., 2024; Wei et al., 2021 | https://doi.org/10.1101/2022.10.20.513117 ; https://doi.org/10.3390/ijms25189858 ; https://doi.org/10.1007/s00425-021-03731-z | (manzano2025regulationandfunction pages 1-3, xue2024comparativeanalysisof pages 1-2, wei2021sbcasp4improvessalt pages 9-12) |
| Cereal/sorghum functional evidence | SbCASP4 from sweet sorghum improved salt exclusion by strengthening the root apoplastic barrier; transgenic lines had higher salinity threshold (125 mM NaCl) than WT (115 mM) and casp5 mutant (94 mM). A 2023 sorghum study reported SbCASP-LP1C1 similarly improves salt exclusion/barrier function. In rice, OsCASP1 is implicated in Casparian strip formation, selective mineral uptake, and nutrient-stress responses. | Sorghum and rice cereals | Direct for SbCASP4 and SbCASP-LP1C1/OsCASP evidence; inference to SbCASP1 orthologous function | Wei et al., 2021; Liu et al., 2023; Xue et al., 2024 | https://doi.org/10.1007/s00425-021-03731-z ; https://doi.org/10.1007/s11103-022-01312-6 ; https://doi.org/10.3390/ijms25189858 | (wei2021sbcasp4improvessalt pages 6-9, liu2023sbcasplp1c1improvessalt pages 1-2, xue2024comparativeanalysisof pages 13-15, xue2024comparativeanalysisof pages 17-18) |
| Application/statistics | CASP-family genes are plausible targets for engineering root diffusion barriers to improve salt tolerance and ion homeostasis in crops. Quantitative support includes sorghum-homolog transgenics with improved salinity thresholds and a global estimate of ~1.125 billion hectares of salinized land, underscoring agricultural relevance. | Crop improvement / abiotic stress adaptation | Application inference supported by direct transgenic and review-style comparative evidence | Liu et al., 2023; Wei et al., 2021; Xue et al., 2024 | https://doi.org/10.1007/s11103-022-01312-6 ; https://doi.org/10.1007/s00425-021-03731-z ; https://doi.org/10.3390/ijms25189858 | (liu2023sbcasplp1c1improvessalt pages 1-2, wei2021sbcasp4improvessalt pages 6-9, xue2024comparativeanalysisof pages 13-15) |
Table: This table summarizes the strongest available evidence for annotating Sorghum bicolor CASP1 (UniProt C5YAP3) while clearly separating direct sorghum evidence from family-based inference. It highlights domain identity, topology, localization, mechanism, regulatory pathways, and cereal application relevance with citation IDs for traceability.
The Casparian strip (CS) is a localized cell-wall lignin barrier in the root endodermis that restricts apoplastic diffusion into the stele; at the plasma membrane adjacent to the CS, plants form a specialized membrane region termed the Casparian strip membrane domain (CSD). CASP proteins accumulate in this domain and are a defining molecular feature of CSD organization. (roppolo2014functionalandevolutionary pages 1-2)
CASPARIAN STRIP MEMBRANE DOMAIN PROTEINS (CASPs) are described as four-transmembrane (4TM) proteins that mediate CS deposition by recruiting lignin polymerization machinery, and their membrane domain is unusually stable, consistent with a membrane scaffold/fence that defines a restricted domain (CSD). CASPs have cytosolic N- and C-termini, with a short intracellular loop, and show very low turnover once localized to the CSD; they are initially present more broadly but become restricted to the CSD. (roppolo2014functionalandevolutionary pages 1-2, roppolo2014functionalandevolutionary pages 12-13)
Given that SbCASP1 (C5YAP3) is annotated as a CASP-family member (UniProt context) and CASPs share conserved 4TM architecture, the most parsimonious functional definition for SbCASP1 is that it is a CSD-localizing 4TM scaffold protein involved in endodermal barrier formation (inference supported by family mechanism). (roppolo2014functionalandevolutionary pages 1-2)
Recent gene-family identification work in rice and Arabidopsis uses a hidden Markov model for DUF588 (PF04535) to define CASP family members, consistent with the CASP/CASPL domain assignment in UniProt/InterPro for SbCASP1. (xue2024comparativeanalysisof pages 1-2)
Evolutionary analysis indicates that CASP-like proteins (CASPLs) occur across land plants and green algae, and homologs outside plants map to the MARVEL protein family; some sequences are annotated as MARVEL-like (InterPro) and comparative analyses explicitly connect plant CASPLs with MARVEL domains (Pfam PF01284). (roppolo2014functionalandevolutionary pages 1-2, roppolo2014functionalandevolutionary pages 14-17)
The best-supported primary molecular role for CASP-family proteins is organizational rather than enzymatic: CASPs are described as a membrane scaffold/fence at the CSD that recruits/coordinates the lignin polymerization machinery for CS formation. (roppolo2014functionalandevolutionary pages 1-2, roppolo2014functionalandevolutionary pages 1-1)
A recent 2024 synthesis further describes CASPs as localizing to the CS membrane domain and recruiting enzymes implicated in lignin polymerization and strip assembly, including RBOHF, ESB1, PER64, and UCC1. (xue2024comparativeanalysisof pages 1-2)
Implication for SbCASP1: SbCASP1 is therefore most likely a plasma membrane structural organizer that helps establish a localized lignin impregnation in the endodermal anticlinal wall (Casparian strip), shaping solute flow into the stele (inference from family mechanism). (roppolo2014functionalandevolutionary pages 1-2, xue2024comparativeanalysisof pages 1-2)
CASP-family proteins are membrane proteins; sorghum homolog evidence supports plasma membrane/Casparian strip association. In sweet sorghum, SbCASP4 (a sorghum CASP homolog) was experimentally localized to the plasma membrane and expressed in root endodermal/Casparian-strip regions via in situ hybridization and reporter constructs; in Arabidopsis, SbCASP4-GFP showed enrichment in endodermal cells, especially the Casparian strip. (wei2021sbcasp4improvessalt pages 3-6, wei2021sbcasp4improvessalt pages 6-9, wei2021sbcasp4improvessalt pages 9-12)
Implication for SbCASP1: given shared CASP family topology and CSD targeting behavior, SbCASP1 is most likely a plasma membrane protein enriched at the CSD in root endodermal cells (inference supported by foundational CASP localization behavior and sorghum homolog experiments). (roppolo2014functionalandevolutionary pages 1-2, wei2021sbcasp4improvessalt pages 9-12)
A key transcriptional regulator of endodermal barrier formation is MYB36, which activates CASP-related genes (including CASP1) and other CS polymerization components (e.g., PER64, ESB1). (manzano2025regulationandfunction pages 1-3)
CASP-mediated barrier formation is monitored by the CIF peptide–SGN receptor/kinase pathway (“SCHENGEN” surveillance): comparative and mechanistic syntheses emphasize CIF1/2 peptide signaling through SGN3 and SGN1 to ensure barrier integrity and to trigger compensatory lignification/suberization when defects are detected. (manzano2025regulationandfunction pages 1-3, xue2024comparativeanalysisof pages 1-2)
In a sorghum-homolog transgenic context, SbCASP4 expression correlated with elevated expression of AtMYB36 and barrier-related genes including AtSGN1 under salt stress, consistent with CASP proteins functioning within/alongside this regulatory network rather than as classic ion transporters. (wei2021sbcasp4improvessalt pages 9-12)
A 2024 comparative analysis in rice (Oryza sativa) and Arabidopsis expanded CASP family catalogs using the PF04535 (DUF588) model and reported that most CASP genes are highly expressed in roots/endodermis and respond to abiotic stresses. The study highlights crop-relevant phenotypes previously reported for OsCASP1, including roles in CS formation and mineral/nutrient homeostasis (e.g., altered tolerance to ion deficiencies), and it presents nutrient-deficiency responsive expression patterns with statistical testing (Student’s t-test; p < 0.01, ***p < 0.001). (xue2024comparativeanalysisof pages 13-15, xue2024comparativeanalysisof pages 17-18)
This supports a current view that CASP-family proteins are not only developmental barrier components but also participate in adaptive remodeling of root diffusion barriers under nutrient and stress conditions—an important framing for crop functional annotation. (xue2024comparativeanalysisof pages 13-15)
A 2023 study reported that a sweet sorghum CASP-like protein (SbCASP‑LP1C1) can improve salt exclusion by enhancing the root apoplastic barrier when expressed in Arabidopsis, reducing Na+ accumulation and decreasing stele permeability to propidium iodide under salinity. The same study framed these results in an application context for crop salt tolerance improvement and cited global salinization pressure (~1.125 billion hectares of salinized land). (liu2023sbcasplp1c1improvessalt pages 1-2)
Although this is not SbCASP1 (C5YAP3), it provides direct, recent (2023) sorghum CASP-family functional evidence supporting the inference that sorghum CASP proteins can be leveraged to strengthen endodermal/apoplastic barriers. (liu2023sbcasplp1c1improvessalt pages 1-2)
A clear real-world implementation pattern in this literature is engineering/expressing CASP-family genes to modulate the root apoplastic barrier and thereby improve salt tolerance.
In sorghum-derived gene experiments, SbCASP4 expressed in Arabidopsis increased salt tolerance and salt exclusion phenotypes under 50 mM NaCl, with multiple physiological readouts including ion accumulation, reactive oxygen species (ROS) measures, and propidium iodide exclusion from the stele (barrier integrity). (wei2021sbcasp4improvessalt pages 9-12)
In addition, SbCASP4 overexpression yielded a higher computed salinity threshold (external NaCl concentration reducing fresh weight to 50%) of 125 mM NaCl compared with 115 mM for wild type and 94 mM for a casp5 mutant, providing a quantitative metric for barrier-mediated salt tolerance improvement. (wei2021sbcasp4improvessalt pages 6-9)
The agricultural rationale is that the endodermal diffusion barrier influences Na+ exclusion (salt tolerance) and selective nutrient uptake/homeostasis. The 2024 rice/Arabidopsis CASP family analysis explicitly connects CASP genes (including OsCASP1 evidence cited therein) to selective mineral uptake and nutrient stress phenotypes, supporting the notion that tuning CASP-mediated barriers can shape ion homeostasis in crops. (xue2024comparativeanalysisof pages 17-18, xue2024comparativeanalysisof pages 13-15)
Authoritative mechanistic interpretation from Roppolo et al. (Plant Physiology, 2014) is that CASPs form a high-stability membrane scaffold and mediate Casparian strip deposition by recruiting lignin polymerization machinery, a framing that remains central to the field’s current understanding and underpins functional annotation of CASP1 orthologs in non-model plants. (roppolo2014functionalandevolutionary pages 1-2, roppolo2014functionalandevolutionary pages 1-1)
A 2024 comparative analysis (IJMS) synthesizes this model into a broader crop context, emphasizing that CASPs are pivotal for CS formation and are implicated in environmental stress responses and nutrient-related phenotypes, motivating continued functional investigation in cereals. (xue2024comparativeanalysisof pages 1-2, xue2024comparativeanalysisof pages 13-15)
In SbCASP4 heterologous-expression experiments in Arabidopsis under salt stress, reported quantitative outcomes include:
- Salinity threshold: WT 115 mM, casp5 mutant 94 mM, SbCASP4-OE 125 mM NaCl (threshold defined as the NaCl concentration that reduces fresh weight to 50% of control). (wei2021sbcasp4improvessalt pages 6-9)
- Experimental and statistical context: NaCl treatment at 50 mM for 5 days, ion assays reported as means ± SD with n=3, and significance evaluated by Duncan’s multiple range test at P=0.05. (wei2021sbcasp4improvessalt pages 9-12)
A 2023 sorghum CASP-like study contextualized the application by citing ~1.125 billion hectares of salinized land globally, underscoring the importance of salt-exclusion strategies and root-barrier engineering. (liu2023sbcasplp1c1improvessalt pages 1-2)
Most defensible primary function (inference from conserved CASP mechanism):
SbCASP1 (C5YAP3) is most likely a 4TM plasma membrane scaffold protein that localizes to the Casparian strip membrane domain (CSD) in root endodermal cells, where it helps organize a membrane microdomain and recruits/positions lignin polymerization machinery to build the Casparian strip, thereby contributing to the endodermal apoplastic diffusion barrier and influencing ion/water movement into the stele. (roppolo2014functionalandevolutionary pages 1-2, xue2024comparativeanalysisof pages 1-2)
Localization (inference supported by sorghum homolog direct evidence):
SbCASP1 is predicted/expected to be plasma-membrane localized and enriched at the endodermal CSD, consistent with sorghum SbCASP4 plasma-membrane localization and Casparian-strip region expression. (wei2021sbcasp4improvessalt pages 3-6, wei2021sbcasp4improvessalt pages 6-9)
Pathway/regulation (inference from conserved endodermal programs):
SbCASP1 likely acts downstream of endodermal differentiation regulators such as MYB36 and within barrier integrity/surveillance signaling involving CIF peptides and SGN kinases, which coordinate lignification/suberization responses to barrier defects. (manzano2025regulationandfunction pages 1-3, xue2024comparativeanalysisof pages 1-2)
Because no retrieved primary paper directly assays SbCASP1 (C5YAP3; Sb06g033470), the following would be most decisive for upgrading inference to direct evidence:
- Root cell-type expression (endodermis specificity) and developmental timing in sorghum.
- Subcellular localization (SbCASP1-GFP) to confirm CSD targeting.
- Genetic perturbation (CRISPR knockout/knockdown) and assays of Casparian strip integrity (e.g., PI exclusion), lignin deposition, and ion homeostasis.
References
(xue2024comparativeanalysisof pages 18-19): Baoping Xue, Zicong Liang, Yue Liu, Dongyang Li, Peng Cao, and Chang Liu. Comparative analysis of casparian strip membrane domain protein family in oryza sativa (l.) and arabidopsis thaliana (l.). International Journal of Molecular Sciences, 25:9858, Sep 2024. URL: https://doi.org/10.3390/ijms25189858, doi:10.3390/ijms25189858. This article has 5 citations.
(wei2021sbcasp4improvessalt pages 1-2): Xiaocen Wei, Lili Liu, Chaoxia Lu, Fang Yuan, Guoliang Han, and Baoshan Wang. Sbcasp4 improves salt exclusion by enhancing the root apoplastic barrier. Planta, Sep 2021. URL: https://doi.org/10.1007/s00425-021-03731-z, doi:10.1007/s00425-021-03731-z. This article has 24 citations and is from a peer-reviewed journal.
(roppolo2014functionalandevolutionary pages 1-2): Daniele Roppolo, Brigitte Boeckmann, Alexandre Pfister, Emmanuel Boutet, Maria C. Rubio, Valérie Dénervaud-Tendon, Joop E.M. Vermeer, Jacqueline Gheyselinck, Ioannis Xenarios, and Niko Geldner. Functional and evolutionary analysis of the casparian strip membrane domain protein family. Plant Physiology, 165:1709-1722, Jun 2014. URL: https://doi.org/10.1104/pp.114.239137, doi:10.1104/pp.114.239137. This article has 134 citations and is from a highest quality peer-reviewed journal.
(roppolo2014functionalandevolutionary pages 14-17): Daniele Roppolo, Brigitte Boeckmann, Alexandre Pfister, Emmanuel Boutet, Maria C. Rubio, Valérie Dénervaud-Tendon, Joop E.M. Vermeer, Jacqueline Gheyselinck, Ioannis Xenarios, and Niko Geldner. Functional and evolutionary analysis of the casparian strip membrane domain protein family. Plant Physiology, 165:1709-1722, Jun 2014. URL: https://doi.org/10.1104/pp.114.239137, doi:10.1104/pp.114.239137. This article has 134 citations and is from a highest quality peer-reviewed journal.
(xue2024comparativeanalysisof pages 1-2): Baoping Xue, Zicong Liang, Yue Liu, Dongyang Li, Peng Cao, and Chang Liu. Comparative analysis of casparian strip membrane domain protein family in oryza sativa (l.) and arabidopsis thaliana (l.). International Journal of Molecular Sciences, 25:9858, Sep 2024. URL: https://doi.org/10.3390/ijms25189858, doi:10.3390/ijms25189858. This article has 5 citations.
(roppolo2014functionalandevolutionary pages 1-1): Daniele Roppolo, Brigitte Boeckmann, Alexandre Pfister, Emmanuel Boutet, Maria C. Rubio, Valérie Dénervaud-Tendon, Joop E.M. Vermeer, Jacqueline Gheyselinck, Ioannis Xenarios, and Niko Geldner. Functional and evolutionary analysis of the casparian strip membrane domain protein family. Plant Physiology, 165:1709-1722, Jun 2014. URL: https://doi.org/10.1104/pp.114.239137, doi:10.1104/pp.114.239137. This article has 134 citations and is from a highest quality peer-reviewed journal.
(wei2021sbcasp4improvessalt pages 3-6): Xiaocen Wei, Lili Liu, Chaoxia Lu, Fang Yuan, Guoliang Han, and Baoshan Wang. Sbcasp4 improves salt exclusion by enhancing the root apoplastic barrier. Planta, Sep 2021. URL: https://doi.org/10.1007/s00425-021-03731-z, doi:10.1007/s00425-021-03731-z. This article has 24 citations and is from a peer-reviewed journal.
(wei2021sbcasp4improvessalt pages 6-9): Xiaocen Wei, Lili Liu, Chaoxia Lu, Fang Yuan, Guoliang Han, and Baoshan Wang. Sbcasp4 improves salt exclusion by enhancing the root apoplastic barrier. Planta, Sep 2021. URL: https://doi.org/10.1007/s00425-021-03731-z, doi:10.1007/s00425-021-03731-z. This article has 24 citations and is from a peer-reviewed journal.
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(wei2021sbcasp4improvessalt pages 9-12): Xiaocen Wei, Lili Liu, Chaoxia Lu, Fang Yuan, Guoliang Han, and Baoshan Wang. Sbcasp4 improves salt exclusion by enhancing the root apoplastic barrier. Planta, Sep 2021. URL: https://doi.org/10.1007/s00425-021-03731-z, doi:10.1007/s00425-021-03731-z. This article has 24 citations and is from a peer-reviewed journal.
(liu2023sbcasplp1c1improvessalt pages 1-2): Lili Liu, Xiaocen Wei, Zhen Yang, Fang Yuan, Guoliang Han, Jianrong Guo, and Baoshan Wang. Sbcasp-lp1c1 improves salt exclusion by enhancing the root apoplastic barrier. Plant Molecular Biology, 111:73-88, Nov 2023. URL: https://doi.org/10.1007/s11103-022-01312-6, doi:10.1007/s11103-022-01312-6. This article has 9 citations and is from a peer-reviewed journal.
(xue2024comparativeanalysisof pages 13-15): Baoping Xue, Zicong Liang, Yue Liu, Dongyang Li, Peng Cao, and Chang Liu. Comparative analysis of casparian strip membrane domain protein family in oryza sativa (l.) and arabidopsis thaliana (l.). International Journal of Molecular Sciences, 25:9858, Sep 2024. URL: https://doi.org/10.3390/ijms25189858, doi:10.3390/ijms25189858. This article has 5 citations.
(xue2024comparativeanalysisof pages 17-18): Baoping Xue, Zicong Liang, Yue Liu, Dongyang Li, Peng Cao, and Chang Liu. Comparative analysis of casparian strip membrane domain protein family in oryza sativa (l.) and arabidopsis thaliana (l.). International Journal of Molecular Sciences, 25:9858, Sep 2024. URL: https://doi.org/10.3390/ijms25189858, doi:10.3390/ijms25189858. This article has 5 citations.
(roppolo2014functionalandevolutionary pages 12-13): Daniele Roppolo, Brigitte Boeckmann, Alexandre Pfister, Emmanuel Boutet, Maria C. Rubio, Valérie Dénervaud-Tendon, Joop E.M. Vermeer, Jacqueline Gheyselinck, Ioannis Xenarios, and Niko Geldner. Functional and evolutionary analysis of the casparian strip membrane domain protein family. Plant Physiology, 165:1709-1722, Jun 2014. URL: https://doi.org/10.1104/pp.114.239137, doi:10.1104/pp.114.239137. This article has 134 citations and is from a highest quality peer-reviewed journal.