Deep Research
Falcon
(PR1B1-deep-research-falcon.md)
Falcon
(PR1B1-deep-research-falcon.md)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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
Research report: Functional annotation of tomato PR1B1 (UniProt P04284) — Pathogenesis-related leaf protein 6 / PR-1-type CAP protein
0) Target verification (critical disambiguation)
The literature on tomato PR-1 proteins uses multiple overlapping names (PR-1, PR1b1, P1/P14, “leaf protein” designations). The core gene-level identifier PR1b1 was cloned and deposited as accession Y08804 (with an acidic paralog PR1a2 = Y08844), establishing an unambiguous molecular handle for tomato PR1b1-family annotation. (tornero1997twopr1genes pages 1-2)
Important limitation: in the retrieved evidence, the classic tomato PR protein called P1(P14) is clearly a PR-1-type protein but is not explicitly sequence-mapped to Y08804/P04284 in the quoted text; therefore, claims about P1(P14) are used as family-/isoform-level contextual evidence, not as definitive isoform-specific claims for P04284. (vera1989‘pathogenesisrelated’p1(p14)protein. pages 8-9)
1) Key concepts and definitions (current understanding)
1.1 PR-1 proteins and the CAP superfamily
PR-1 proteins belong to the broader CAP (CRISP/Antigen 5/PR-1) superfamily. Modern mechanistic syntheses frame plant PR-1 proteins as secreted defense proteins whose biochemical activity has been historically unclear but is increasingly linked to lipid binding and processing into immune signaling peptides. (han2023thefunctionof pages 9-10, han2023thefunctionof pages 1-2)
A 2017 biochemical/structural study on CAP proteins includes “tomato PR1B1 (P04284)” explicitly in a table of CAP-family members (by UniProt identifier), supporting that the target (P04284) is recognized in the CAP protein literature as a bona fide CAP-family representative. (bai2023mopce1acappr pages 15-16)
1.2 Apoplast, vacuole, and secretory precursors
Classical PR proteins are frequently found in the apoplast (extracellular space). Some PR-1 isoforms, particularly basic members, are often described as vacuolar and/or extracellular; these compartment assignments are important because they determine whether PR-1 acts as a direct antimicrobial effector in the apoplast, a stored defense factor in vacuoles, or both. (loon1999thefamiliesof pages 3-5)
2) Gene/protein overview for PR1B1 (P04284): function, regulation, and localization
2.1 Molecular identity and inducible expression programs
In tomato, Tornero et al. cloned and characterized two PR-1 genes and identified PR1b1 (basic) as pathogen-responsive; PR1b1 is strongly activated locally around tissues undergoing the hypersensitive response after TMV inoculation and is inducible by salicylic acid (SA) and ethylene precursors (ACC and ethephon). (tornero1997twopr1genes pages 8-9, tornero1997twopr1genes pages 1-2)
A key regulatory element in PR1b1 transcriptional control is a conserved promoter GCCGCCTC motif; deletion of the region containing this motif drastically reduces TMV-induced expression, and the motif is tied to ethylene-dependent activation in the promoter assays. (tornero1997twopr1genes pages 8-9)
2.2 Pathogen-induced PR1B1 expression can be ethylene-perception independent in compatible infection
In a high-impact Plant Cell study, tomato leaves inoculated with Xanthomonas campestris pv. vesicatoria (1 × 10^6 CFU/mL) showed pathogen-induced accumulation of PR-1B1 mRNA in both wild-type and the ethylene-insensitive Never ripe (Nr/Nr) genotype. Quantification indicated the peak PR-1B1 induction reached ~20-fold above mock at 10 days after inoculation, and ethylene insensitivity did not reduce PR-1B1 induction in this compatible interaction. (lund1998ethyleneregulatesthe pages 5-6, lund1998ethyleneregulatesthe pages 9-10)
Interpretation: PR1B1 is embedded in defense signaling networks that can be triggered by pathogen challenge even when canonical ethylene perception is impaired, consistent with PR1B1 being an integrated output of broader immune and stress signaling rather than a strictly ethylene-dependent marker in all contexts. (lund1998ethyleneregulatesthe pages 9-10)
2.3 Secretory pathway processing and extracellular/vacuolar localization (tomato PR-1 family evidence)
A classical tomato PR-1-type protein called P1(P14) was shown by immunogold labeling to accumulate in intercellular spaces (apoplast) and in vacuolar inclusion bodies in viroid-stressed leaves, with corrected gold-label densities of about 137 particles/µm² in intercellular spaces and 120 particles/µm² in vacuolar inclusions. (vera1989‘pathogenesisrelated’p1(p14)protein. pages 5-8)
The same study also provided direct biochemical evidence for precursor processing: in vitro translation produced a larger precursor that was processed to the mature ~14 kDa form in the presence of microsomes, consistent with entry into the ER and cleavage of an N-terminal signal peptide during secretory trafficking. (vera1989‘pathogenesisrelated’p1(p14)protein. pages 5-8)
Independently, a tomato fruit study characterized PR1b1 as a small basic protein and explicitly reports a PR1b1 sequence with an N-terminal signal peptide (24 aa), consistent with secretion. (goyal2016pathogenesisrelatedprotein1b1 pages 4-6)
3) Primary functional roles: what PR1B1 likely does
3.1 Direct antimicrobial/anti-oomycete activity (family-level functional evidence)
A highly cited comparative review summarizes experimental evidence that tomato PR-1 proteins can show direct antifungal activity, including inhibition of Phytophthora infestans zoospore germination in vitro and reduction of lesion area on infected leaf discs in vivo; the review also notes that basic tomato PR-1 proteins show higher antifungal activity than acidic counterparts. (loon1999thefamiliesof pages 3-5)
While these assays are not reproduced in the retrieved excerpts for P04284 specifically, they strongly support the working functional model that tomato PR1B1-like proteins contribute to defense as extracellular antimicrobial proteins, especially against oomycetes. (loon1999thefamiliesof pages 3-5)
3.2 PR1 as a precursor of immune signaling peptide CAPE1 (major modern mechanism)
A major 2023 synthesis describes a tomato-specific mechanism: PR1 proteins are proteolytically processed to release a conserved 11-amino-acid C-terminal peptide, CAPE1, which is sufficient to activate immune responses. CAPE1 induces ROS and defense/stress-response gene expression and can confer resistance to Pseudomonas syringae without triggering a hypersensitive response. (han2023thefunctionof pages 6-8)
The site of CAPE1 processing is inferred to be extracellular/apoplastic: treatment of apoplastic fluid with serine-protease inhibitors blocks accumulation of the peptide, implicating extracellular serine proteases in PR1 maturation. (han2023thefunctionof pages 6-8)
Mechanistic significance: this places PR1 proteins (including PR1B1-family proteins) in a dual role—(i) potential direct antimicrobial activity and (ii) functioning as pro-proteins for extracellular damage-associated molecular pattern (DAMP)-like signals that amplify immunity. (han2023thefunctionof pages 6-8)
4) Recent developments (prioritizing 2023–2024)
4.1 PR1/CAP proteins as targets of pathogen effectors and relocalization mechanisms
The 2023 review compiles evidence that multiple pathogen effectors target PR1 proteins to suppress immunity. A tomato-relevant example is the Fusarium oxysporum effector FolSvp1, which interacts with PR1 and relocalizes it from the apoplast to the nucleus, thereby abolishing CAPE1 generation and facilitating infection. (han2023thefunctionof pages 8-9)
This positions apoplastic PR1/CAPE processing as a contested node in plant–pathogen interactions and suggests that maintaining PR1 in the apoplast (and enabling its cleavage) is functionally important for defense. (han2023thefunctionof pages 8-9)
4.2 Lipid-binding pockets, CAPE release models, and structural framing
A core conceptual development emphasized in 2023–2024 reviews is that CAP-family proteins contain hydrophobic ligand-binding pockets (fatty acids/oxylipins and related hydrophobic molecules) and that lipid binding may influence the C-terminal conformation and thus CAPE1 release. (han2023thefunctionof pages 9-10)
The retrieved figures from Han et al. visually summarize CAP-domain architecture (including the CAPE1 motif and a binding-pocket model) and propose how lipid binding and pathogen effectors can regulate CAPE1 release; these models are shown in the cited figure panels. (han2023thefunctionof media a5725da9, han2023thefunctionof media 95b772ed)
4.3 2024 perspective: PR abundance, multigene families, and pathogen “PR-like” proteins
A 2024 review highlights that PR1 can be extremely abundant (noted as 1–2% of leaf protein) and that PR1 belongs to large multigene families (example counts: 22 PR1 homologs in Arabidopsis and 39 in rice). It also emphasizes that pathogens (fungi/oomycetes/nematodes) encode PR1-like CAP proteins that can function as virulence factors, and suggests pathogen-derived PR-like proteins may form complexes with host PR proteins to interfere with host defense. (han2024dualfunctionalityof pages 1-2)
5) Regulation by abiotic stress and cross-protection: real-world physiological contexts
5.1 Chilling stress in fruit and polyamine-associated accumulation
In tomato fruit, PR1b1 is induced strongly by chilling/rewarming. In an experiment chilling mature-green fruit 14 days at 2°C followed by rewarming to 20°C, putrescine increased 10–12-fold during chilling. A ~14 kDa protein band identified as PR1b1 peaked at 6 days after rewarming in control fruit and then declined to near-undetectable by 15 days, whereas in high-polyamine transgenic lines PR1b1 continued to accumulate and remained high through 15 days after rewarming. (goyal2016pathogenesisrelatedprotein1b1 pages 4-6)
Transcripts in the polyamine-accumulating lines were reported as “several-fold higher” than controls at 2 and 6 days after rewarming, while control fruit showed negligible PR1b1 expression until late timepoints. (goyal2016pathogenesisrelatedprotein1b1 pages 6-7, goyal2016pathogenesisrelatedprotein1b1 pages 4-6)
The same study reported that blocking ethylene action (1-MCP) reduced ethylene but did not affect PR1b1 protein induction, and that SA levels were higher in transgenic fruit after rewarming, supporting a model where PR1b1 induction in this context is ethylene-independent and possibly linked to SA-associated stress signaling. (goyal2016pathogenesisrelatedprotein1b1 pages 6-7)
6) Current applications and implementations
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Immune status marker (research and breeding): PR1/PR1b1 is widely used as a transcriptional marker of defense activation, especially in SA-associated responses, and tomato PR1b1 promoter elements have been studied for inducible expression designs in plant biotechnology (e.g., promoter motif analyses in TMV/ethylene/SA contexts). (tornero1997twopr1genes pages 8-9, tornero1997twopr1genes pages 1-2)
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Engineering broad-spectrum disease resistance: Transgenic strategies that enhance systemic acquired resistance pathways (e.g., NPR1 pathway engineering) have been tested in tomato and include monitoring PR1-family transcripts (including PR1b1 and PR1p6). Such approaches can reduce disease severity against multiple pathogens, although isoform-specific PR1b1 quantitative induction was not extractable from the retrieved excerpt. (lin2004transgenictomatoplants pages 6-8)
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Peptide-based immunity elicitation (emerging application): The CAPE1 concept supports development of endogenous peptide elicitors (or their stabilized analogs) to enhance disease resistance. In tomato, CAPE1 is sufficient to induce ROS and defense genes and to reduce Pseudomonas colonization, motivating translational work in crop protection. (han2023thefunctionof pages 6-8)
7) Expert synthesis and interpretation (authoritative analysis)
Working functional annotation for PR1B1 (P04284) in tomato:
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Primary cellular site of action: predominantly the secretory pathway and apoplast, with evidence that related PR-1 proteins can also accumulate in vacuolar inclusions under stress; PR1 proteins can be processed from a precursor in an ER/microsome-dependent manner, supporting secretion. (vera1989‘pathogenesisrelated’p1(p14)protein. pages 5-8, goyal2016pathogenesisrelatedprotein1b1 pages 4-6)
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Primary biological role: defense-associated secreted protein induced by pathogens and by immune hormones (SA and, depending on context, ethylene-related signaling) and by abiotic stress (chilling). (tornero1997twopr1genes pages 8-9, goyal2016pathogenesisrelatedprotein1b1 pages 4-6)
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Mechanistic roles (modern view):
1) contributes to direct extracellular antimicrobial activity (family-level evidence includes anti-oomycete activity against P. infestans), and
2) serves as a pro-protein for generating the immune signaling peptide CAPE1 in the apoplast, which triggers ROS and defense gene activation and improves resistance to bacterial colonization. (loon1999thefamiliesof pages 3-5, han2023thefunctionof pages 6-8) -
Network position: a downstream output of immune signaling and a target of pathogen effectors that block PR1 processing or relocalize PR1 away from the apoplast, highlighting its functional relevance in immune execution. (han2023thefunctionof pages 8-9)
8) Evidence summary table (tomato-focused)
| Claim/Concept | Evidence in tomato (paper + key quantitative detail) | Experimental context | Interpretation for function/localization | Citation ID |
|---|---|---|---|---|
| Identity mapping of target gene | Tornero et al. 1997 cloned two tomato PR-1 genes and assigned PR1b1 = Y08804 and PR1a2 = Y08844; PR1b1 is the pathogen-responsive/basic isoform. | Tomato PR-1 gene cloning and expression analysis. | Confirms the core literature gene identity for tomato PR1b1, consistent with the target being a tomato PR-1/CAP-family protein rather than an unrelated PR-like symbol. | (tornero1997twopr1genes pages 1-2) |
| Dual localization and precursor processing of linked tomato PR-1 protein P1/P14 | Vera et al. 1989 localized tomato P1(P14) to both intercellular spaces/apoplast and vacuolar inclusion bodies; immunogold labeling reached about 137 particles/µm² in intercellular spaces and 120 particles/µm² in vacuolar inclusions. In vitro translation showed a larger precursor processed to mature ~14 kDa protein in the presence of microsomes. | Citrus exocortis viroid-infected tomato leaves; immunocytochemistry plus in vitro translation/microsome processing. | Strong evidence that closely linked tomato PR-1 proteins are secretory-pathway precursors and can accumulate in both apoplast and vacuole, supporting extracellular defense and/or vacuolar storage/trafficking. | (vera1989‘pathogenesisrelated’p1(p14)protein. pages 5-8, vera1989‘pathogenesisrelated’p1(p14)protein. pages 8-9) |
| Ethylene/SA induction and promoter motif in PR1b1 | Tornero et al. 1997 showed PR1b1 is induced by TMV, salicylic acid, ACC, and ethephon; deletion of a promoter region containing the GCCGCCTC motif caused a drastic loss of TMV responsiveness. | Tomato promoter-deletion and expression studies during hypersensitive response and hormone treatments. | Supports PR1b1 as a defense-induced signaling output gene, integrating ethylene- and SA-associated immune transcriptional control; likely functions in local defense around infection sites. | (tornero1997twopr1genes pages 8-9, tornero1997twopr1genes pages 1-2) |
| Ethylene-insensitive mutant still accumulates PR-1B1 | Lund et al. 1998 inoculated leaves with Xanthomonas campestris pv. vesicatoria at 1 × 10^6 CFU/mL and found PR-1B1 mRNA accumulation peaked at ~20-fold above mock by 10 days after inoculation in both wild type and Nr/Nr ethylene-insensitive plants. | Compatible bacterial infection in tomato; RNA gel blots in wild type vs Never ripe mutant. | Pathogen-triggered PR1b1 accumulation can occur without normal ethylene perception in this infection context, indicating PR1b1 is not a simple ethylene-only marker and is embedded in broader defense signaling. | (lund1998ethyleneregulatesthe pages 5-6, lund1998ethyleneregulatesthe pages 9-10) |
| Antifungal activity associated with tomato PR-1 family | van Loon & van Strien 1999 summarized evidence that tomato PR-1 proteins inhibit Phytophthora infestans zoospore germination in vitro and reduce lesion area on infected leaf discs in vivo; basic tomato PR-1 proteins were noted as more antifungal than acidic counterparts. | Comparative PR-protein review synthesizing tomato functional assays. | Supports a primary functional model in which tomato PR1b1-family proteins act as direct extracellular antimicrobial/anti-oomycete defense proteins. | (loon1999thefamiliesof pages 3-5) |
| Chilling/polyamine-responsive PR1b1 accumulation in fruit | Goyal et al. 2016 identified a ~14-kDa PR1b1 as a major chilling-responsive tomato fruit protein. Fruits were chilled 14 d at 2°C then rewarmed; putrescine increased 10–12-fold during chilling. In controls, PR1b1 peaked around 6 days after rewarming then declined; in high-polyamine lines, PR1b1 stayed elevated through 15 d and transcripts were several-fold higher at 2 and 6 d. | Tomato fruit abiotic-stress time course in azygous vs high-polyamine transgenic lines. | Extends PR1b1 biology beyond pathogen response to abiotic/cross-protection stress signaling; consistent with PR1b1 as a robust stress-responsive secreted defense protein linked to SA/polyamine-associated protection. | (goyal2016pathogenesisrelatedprotein1b1 pages 1-2, goyal2016pathogenesisrelatedprotein1b1 pages 6-7, goyal2016pathogenesisrelatedprotein1b1 pages 4-6) |
| CAPE1 processing and apoplastic generation | Han et al. 2023 reviewed tomato evidence that PR1 is proteolytically processed to release the 11-aa CAPE1 peptide; CAPE1 induces ROS, defense genes, limits Pseudomonas syringae colonization, and processing likely occurs in the apoplast/extracellular space because serine-protease inhibitors in apoplastic fluid block peptide accumulation. | Mechanistic synthesis of tomato PR1/CAP studies and CAPE1 signaling. | Indicates PR1 proteins have a second function beyond direct antimicrobial action: they are precursors of extracellular immune-signaling peptides, placing their action chiefly in the apoplast. | (han2023thefunctionof pages 6-8) |
Table: This table condenses the key tomato-specific evidence most useful for annotating PR1B1/P04284 and closely linked tomato PR-1 proteins. It highlights identity, localization, regulation, inferred function, and newer CAPE1-based mechanistic interpretations.
9) Key visual evidence (2023 model figures)
The following figure panels from Han et al. 2023 summarize PR1 CAP-domain features and a working model for ligand binding and CAPE1 peptide release regulation; these support the mechanistic interpretation above. (han2023thefunctionof media a5725da9, han2023thefunctionof media 95b772ed)
10) Source list with URLs and publication dates (as available in evidence)
- Vera P, Hernandez-Yago J, Conejero V. 1989-08. ‘Pathogenesis-related’ P1(p14) Protein… Journal of General Virology. https://doi.org/10.1099/0022-1317-70-8-1933 (vera1989‘pathogenesisrelated’p1(p14)protein. pages 5-8, vera1989‘pathogenesisrelated’p1(p14)protein. pages 8-9)
- Tornero P, Gadea J, Conejero V, Vera P. 1997-07. Two PR-1 genes from tomato… Molecular Plant-Microbe Interactions. https://doi.org/10.1094/mpmi.1997.10.5.624 (tornero1997twopr1genes pages 1-2, tornero1997twopr1genes pages 8-9)
- Lund ST, Stall RE, Klee HJ. 1998-03. Ethylene regulates the susceptible response… The Plant Cell. https://doi.org/10.1105/tpc.10.3.371 (lund1998ethyleneregulatesthe pages 5-6, lund1998ethyleneregulatesthe pages 9-10)
- van Loon LC, van Strien EA. 1999-08. The families of pathogenesis-related proteins… Physiological and Molecular Plant Pathology. https://doi.org/10.1006/pmpp.1999.0213 (loon1999thefamiliesof pages 3-5)
- Lin W-C et al. 2004-12. Transgenic tomato expressing Arabidopsis NPR1… Transgenic Research. https://doi.org/10.1007/s11248-004-2375-9 (lin2004transgenictomatoplants pages 6-8)
- Goyal RK et al. 2016-06. PR1b1 is a major tomato fruit protein responsive to chilling… Frontiers in Plant Science. https://doi.org/10.3389/fpls.2016.00901 (goyal2016pathogenesisrelatedprotein1b1 pages 4-6)
- Han Z et al. 2023-03. The function of plant PR1 and other CAP proteins… Molecular Plant Pathology. https://doi.org/10.1111/mpp.13320 (han2023thefunctionof pages 9-10, han2023thefunctionof pages 6-8)
- Jian Y et al. 2023-12. How plants manage pathogen infection. EMBO Reports. https://doi.org/10.1038/s44319-023-00023-3 (han2023thefunctionof pages 8-9)
- Han Z, Schneiter R. 2024-08. Dual functionality of pathogenesis-related proteins… Frontiers in Plant Science. https://doi.org/10.3389/fpls.2024.1368467 (han2024dualfunctionalityof pages 1-2)
11) Notable gaps and confidence notes
- Isoform mapping (P14/P1 vs PR1b1/P04284): current retrieved excerpts do not explicitly equate classic P1(P14) protein to a specific modern accession (Y08804/P04284). Claims about P1(P14) are therefore treated as informative for tomato PR-1 localization/processing generally, not definitive for P04284 without sequence cross-reference. (vera1989‘pathogenesisrelated’p1(p14)protein. pages 8-9)
- Direct biochemical substrate specificity: no enzyme reaction applies (PR1B1 is not an enzyme in these sources). A precise sterol-binding affinity for tomato PR1B1 specifically is not present in the retrieved excerpts; lipid-binding is discussed at CAP-superfamily level and in models/reviews. (han2023thefunctionof pages 9-10)
References
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(tornero1997twopr1genes pages 1-2): Pablo Tornero, José Gadea, Vicente Conejero, and Pablo Vera. Two pr-1 genes from tomato are differentially regulated and reveal a novel mode of expression for a pathogenesis-related gene during the hypersensitive response and development. Molecular plant-microbe interactions : MPMI, 10 5:624-34, Jul 1997. URL: https://doi.org/10.1094/mpmi.1997.10.5.624, doi:10.1094/mpmi.1997.10.5.624. This article has 201 citations.
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(vera1989‘pathogenesisrelated’p1(p14)protein. pages 8-9): P. Vera, J. Hernandez-Yago, and V. Conejero. ‘pathogenesis-related’ p1(p14) protein. vacuolar and apoplastic localization in leaf tissue from tomato plants infected with citrus exocortis viroid; in vitro synthesis and processing. Journal of General Virology, 70:1933-1942, Aug 1989. URL: https://doi.org/10.1099/0022-1317-70-8-1933, doi:10.1099/0022-1317-70-8-1933. This article has 38 citations and is from a peer-reviewed journal.
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(han2023thefunctionof pages 9-10): Zhu Han, Dianguang Xiong, Roger Schneiter, and Chengming Tian. The function of plant pr1 and other members of the cap protein superfamily in plant–pathogen interactions. Molecular Plant Pathology, 24:651-668, Mar 2023. URL: https://doi.org/10.1111/mpp.13320, doi:10.1111/mpp.13320. This article has 152 citations and is from a peer-reviewed journal.
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(han2023thefunctionof pages 1-2): Zhu Han, Dianguang Xiong, Roger Schneiter, and Chengming Tian. The function of plant pr1 and other members of the cap protein superfamily in plant–pathogen interactions. Molecular Plant Pathology, 24:651-668, Mar 2023. URL: https://doi.org/10.1111/mpp.13320, doi:10.1111/mpp.13320. This article has 152 citations and is from a peer-reviewed journal.
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(bai2023mopce1acappr pages 15-16): Huimin Bai, Xiaomin Chen, Dao Zhou, Jiayuan Guo, Ting Sun, Yuanhao Liu, Zecheng Lai, Dongmei Zhang, Wei Tang, Xiuxiu Li, Zhenhui Zhong, Guodong Lu, Zonghua Wang, and Huakun Zheng. Mopce1, a cap/pr domain containing effector is required for the pathogenicity of magnaporthe oryzae by interacting with the osdi19-5 in rice. Unknown journal, Nov 2023. URL: https://doi.org/10.20944/preprints202311.0510.v1, doi:10.20944/preprints202311.0510.v1.
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(loon1999thefamiliesof pages 3-5): L.C. VAN LOON and E.A. VAN STRIEN. The families of pathogenesis-related proteins, their activities, and comparative analysis of pr-1 type proteins. Physiological and Molecular Plant Pathology, 55:85-97, Aug 1999. URL: https://doi.org/10.1006/pmpp.1999.0213, doi:10.1006/pmpp.1999.0213. This article has 2778 citations and is from a peer-reviewed journal.
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(tornero1997twopr1genes pages 8-9): Pablo Tornero, José Gadea, Vicente Conejero, and Pablo Vera. Two pr-1 genes from tomato are differentially regulated and reveal a novel mode of expression for a pathogenesis-related gene during the hypersensitive response and development. Molecular plant-microbe interactions : MPMI, 10 5:624-34, Jul 1997. URL: https://doi.org/10.1094/mpmi.1997.10.5.624, doi:10.1094/mpmi.1997.10.5.624. This article has 201 citations.
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(lund1998ethyleneregulatesthe pages 5-6): Steven T. Lund, Robert E. Stall, and Harry J. Klee. Ethylene regulates the susceptible response to pathogen infection in tomato. Plant Cell, 10:371-382, Mar 1998. URL: https://doi.org/10.1105/tpc.10.3.371, doi:10.1105/tpc.10.3.371. This article has 537 citations and is from a highest quality peer-reviewed journal.
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(lund1998ethyleneregulatesthe pages 9-10): Steven T. Lund, Robert E. Stall, and Harry J. Klee. Ethylene regulates the susceptible response to pathogen infection in tomato. Plant Cell, 10:371-382, Mar 1998. URL: https://doi.org/10.1105/tpc.10.3.371, doi:10.1105/tpc.10.3.371. This article has 537 citations and is from a highest quality peer-reviewed journal.
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(vera1989‘pathogenesisrelated’p1(p14)protein. pages 5-8): P. Vera, J. Hernandez-Yago, and V. Conejero. ‘pathogenesis-related’ p1(p14) protein. vacuolar and apoplastic localization in leaf tissue from tomato plants infected with citrus exocortis viroid; in vitro synthesis and processing. Journal of General Virology, 70:1933-1942, Aug 1989. URL: https://doi.org/10.1099/0022-1317-70-8-1933, doi:10.1099/0022-1317-70-8-1933. This article has 38 citations and is from a peer-reviewed journal.
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(goyal2016pathogenesisrelatedprotein1b1 pages 4-6): Ravinder K. Goyal, Tahira Fatima, Muhamet Topuz, Anne Bernadec, Richard Sicher, Avtar K. Handa, and Autar K. Mattoo. Pathogenesis-related protein 1b1 (pr1b1) is a major tomato fruit protein responsive to chilling temperature and upregulated in high polyamine transgenic genotypes. Frontiers in Plant Science, Jun 2016. URL: https://doi.org/10.3389/fpls.2016.00901, doi:10.3389/fpls.2016.00901. This article has 74 citations.
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(han2023thefunctionof pages 6-8): Zhu Han, Dianguang Xiong, Roger Schneiter, and Chengming Tian. The function of plant pr1 and other members of the cap protein superfamily in plant–pathogen interactions. Molecular Plant Pathology, 24:651-668, Mar 2023. URL: https://doi.org/10.1111/mpp.13320, doi:10.1111/mpp.13320. This article has 152 citations and is from a peer-reviewed journal.
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(han2023thefunctionof pages 8-9): Zhu Han, Dianguang Xiong, Roger Schneiter, and Chengming Tian. The function of plant pr1 and other members of the cap protein superfamily in plant–pathogen interactions. Molecular Plant Pathology, 24:651-668, Mar 2023. URL: https://doi.org/10.1111/mpp.13320, doi:10.1111/mpp.13320. This article has 152 citations and is from a peer-reviewed journal.
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(han2023thefunctionof media a5725da9): Zhu Han, Dianguang Xiong, Roger Schneiter, and Chengming Tian. The function of plant pr1 and other members of the cap protein superfamily in plant–pathogen interactions. Molecular Plant Pathology, 24:651-668, Mar 2023. URL: https://doi.org/10.1111/mpp.13320, doi:10.1111/mpp.13320. This article has 152 citations and is from a peer-reviewed journal.
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(han2023thefunctionof media 95b772ed): Zhu Han, Dianguang Xiong, Roger Schneiter, and Chengming Tian. The function of plant pr1 and other members of the cap protein superfamily in plant–pathogen interactions. Molecular Plant Pathology, 24:651-668, Mar 2023. URL: https://doi.org/10.1111/mpp.13320, doi:10.1111/mpp.13320. This article has 152 citations and is from a peer-reviewed journal.
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(han2024dualfunctionalityof pages 1-2): Zhu Han and Roger Schneiter. Dual functionality of pathogenesis-related proteins: defensive role in plants versus immunosuppressive role in pathogens. Frontiers in Plant Science, Aug 2024. URL: https://doi.org/10.3389/fpls.2024.1368467, doi:10.3389/fpls.2024.1368467. This article has 52 citations.
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(goyal2016pathogenesisrelatedprotein1b1 pages 6-7): Ravinder K. Goyal, Tahira Fatima, Muhamet Topuz, Anne Bernadec, Richard Sicher, Avtar K. Handa, and Autar K. Mattoo. Pathogenesis-related protein 1b1 (pr1b1) is a major tomato fruit protein responsive to chilling temperature and upregulated in high polyamine transgenic genotypes. Frontiers in Plant Science, Jun 2016. URL: https://doi.org/10.3389/fpls.2016.00901, doi:10.3389/fpls.2016.00901. This article has 74 citations.
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(lin2004transgenictomatoplants pages 6-8): Wan-Chi Lin, Ching-Fang Lu, Jia-Wei Wu, Ming-Lung Cheng, Yu-Mei Lin, Ning-Sun Yang, Lowell Black, Sylvia K. Green, Jaw-Fen Wang, and Chiu-Ping Cheng. Transgenic tomato plants expressing the arabidopsis npr1 gene display enhanced resistance to a spectrum of fungal and bacterial diseases. Transgenic Research, 13:567-581, Dec 2004. URL: https://doi.org/10.1007/s11248-004-2375-9, doi:10.1007/s11248-004-2375-9. This article has 330 citations and is from a peer-reviewed journal.
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