Research Report: Functional Annotation of Rice **LSD1 / OsLSD1** (UniProt **Q0J7V9**; loci **LOC_Os08g06280 / Os08g0159500**) in *Oryza sativa* subsp. *japonica* Falcon Edison Scientific Literature 23 citations 2 artifacts 2026-05-30T10:04:00.713217

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
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Research Report: Functional Annotation of Rice LSD1 / OsLSD1 (UniProt Q0J7V9; loci LOC_Os08g06280 / Os08g0159500) in Oryza sativa subsp. japonica

Executive summary

Rice OsLSD1 (LESION SIMULATING DISEASE 1-like; “Protein LSD1”) is a plant-specific, small C2C2 zinc-finger protein that functions as a context-dependent regulator of programmed cell death (PCD) and is implicated in blast disease responses and tissue culture/callus differentiation. Primary experimental work in rice indicates OsLSD1 acts largely as a negative regulator of PCD, while promoting callus differentiation/regeneration, and its manipulation can alter defense marker expression and resistance phenotypes. OsLSD1 is also positioned mechanistically within PCD signaling via protein–protein interactions with rice type I metacaspases. A recent (2024) rice GWAS nominates OsLSD1 as a candidate gene affecting callus induction rate, reinforcing potential relevance to transformation/regeneration pipelines. (wang2005oslsd1arice pages 1-2, wang2005oslsd1arice pages 2-4, huang2015stressresponsiveexpressionsubcellular pages 13-15, huang2015stressresponsiveexpressionsubcellular pages 1-3, song2024acyclingene pages 2-4)

0) Mandatory gene/protein identity verification (disambiguation)

Correct target: rice OsLSD1 / LESION SIMULATING DISEASE 1-like zinc finger protein

The symbol “LSD1” is ambiguous across biology (notably, in mammals it often refers to lysine-specific demethylase 1/KDM1A, a large FAD-dependent amine oxidase). The rice protein requested here (UniProt Q0J7V9) matches the plant “LESION SIMULATING DISEASE 1” class, which is small (~143 aa) and defined by multiple C2C2 zinc-finger motifs, not an amine-oxidase/demethylase domain. (wang2005oslsd1arice pages 1-2, wang2005oslsd1arice pages 2-4)

Evidence linking OsLSD1 to rice genome identifiers

1) Key concepts and definitions (current understanding)

1.1 Programmed cell death (PCD) and hypersensitive response (HR)

In plant immunity, the hypersensitive response (HR) is a localized cell death program associated with defense signaling, often occurring alongside a burst of reactive oxygen species (ROS) and induction of pathogenesis-related (PR) genes. Lesion mimic phenotypes (spontaneous lesions without pathogens) are frequently used to dissect HR/PCD pathways. OsLSD1 was identified specifically in this conceptual framework: a rice functional homolog of Arabidopsis LSD1 that participates in HR/PCD regulation. (wang2005oslsd1arice pages 1-2)

1.2 LSD1/LOL family proteins as ROS–PCD “threshold” regulators

Work in Arabidopsis provides a widely used conceptual model for LSD1-like proteins: the plant-specific zinc-finger proteins LSD1 (negative regulator) and LOL1 (positive regulator) antagonistically regulate ROS-associated cell death and may set a threshold for commitment to PCD, partly via effects on antioxidant systems such as Cu/Zn superoxide dismutases. Although these mechanistic models were built in Arabidopsis, OsLSD1 is considered part of the same plant-specific family and is frequently interpreted through this ROS/PCD-threshold lens. (epple2003antagonisticcontrolof pages 5-6, epple2003antagonisticcontrolof pages 4-5)

2) Molecular features of rice OsLSD1 (Q0J7V9)

2.1 Protein size, motifs, and gene structure

In rice, OsLSD1 encodes a predicted protein of 143 amino acids (~14.8 kDa) with three internally conserved C2C2-type zinc-finger motifs described by the consensus CxxCxxLLMYxxGAxSVxCxxC. (wang2005oslsd1arice pages 1-2, wang2005oslsd1arice pages 2-4)

Wang et al. report:
* cDNA length 988 bp with 432 bp ORF (AY525368). (wang2005oslsd1arice pages 2-4)
* Genomic locus length 2,971 bp, consisting of six exons and five introns. (wang2005oslsd1arice pages 2-4)
* OsLSD1 behaves as a single-copy gene by Southern hybridization across multiple cultivars. (wang2005oslsd1arice pages 2-4, wang2005oslsd1arice pages 1-2)

2.2 Subcellular localization

An OsLSD1–GFP fusion was reported as nuclear localized in tobacco cells, consistent with a role in transcriptional regulation or nuclear protein complexes controlling PCD and differentiation. (wang2005oslsd1arice pages 1-2)

3) Biological functions and pathways

3.1 Core function in rice: negative regulation of PCD, modulation of HR-like responses

In rice, antisense suppression of OsLSD1 produced a lesion mimic phenotype and accelerated HR cell death upon inoculation with avirulent blast isolates, along with increased PR-1 mRNA—consistent with OsLSD1 functioning as a negative regulator of PCD/HR-like cell death. (wang2005oslsd1arice pages 1-2, wang2005oslsd1arice pages 2-4)

Environmental modulation (light/temperature) is reported for lesion phenotypes, highlighting that OsLSD1-linked cell death outcomes are condition-dependent. (wang2005oslsd1arice pages 6-7)

3.2 Callus differentiation and tissue culture competence

OsLSD1 overexpression promotes callus differentiation/regeneration:
* Differentiation time of hygromycin-resistant calli decreased from ~7–10 days (control) to ~3–5 days with OsLSD1 overexpression. (wang2005oslsd1arice pages 2-4)
* Overexpression increased chlorophyll b content and altered chlorophyll composition; Table 1 reports chlorophyll quantities (mg/g fresh weight) across representative lines (e.g., line S9 chlorophyll b 0.444 ± 0.004 vs WT 0.209 ± 0.006). (wang2005oslsd1arice pages 2-4)

These data support a model in which OsLSD1 has a dual role: restraining PCD while promoting differentiation/regeneration in tissue culture contexts. (wang2005oslsd1arice pages 1-2, wang2005oslsd1arice pages 2-4)

3.3 Disease resistance: blast interactions and defense marker induction

OsLSD1 is repeatedly linked to rice blast disease responses:
* In the original rice study, both sense (overexpression) and antisense OsLSD1 transgenic rice exhibited significantly enhanced resistance to a virulent blast isolate, though via potentially different physiological routes (antisense associated with heightened HR/defense gene induction; overexpression associated with growth/chlorophyll changes and toxin tolerance). (wang2005oslsd1arice pages 1-2, wang2005oslsd1arice pages 2-4, wang2005oslsd1arice pages 6-7)
* A subsequent rice ZFP/blast interaction analysis lists OsLSD1 (LOC_Os08g06280) among ZFP families associated with defense against Magnaporthe oryzae, and reports LSD1-family expression was repressed by M. oryzae inoculation in their dataset. (li2014identificationandnetwork pages 1-2)

3.4 Mechanistic placement: interaction with metacaspases (PCD protease network)

Plant metacaspases are caspase-like proteases implicated in PCD regulation. In rice:
* Yeast two-hybrid assays showed type I metacaspases OsMC1/OsMC2/OsMC3 interact with OsLSD1 (and OsLSD3) but not with OsLSD2/OsLOL1/OsLOL2, positioning OsLSD1 in metacaspase-linked PCD signaling. (huang2015stressresponsiveexpressionsubcellular pages 13-15)
* OsMC3 was reported to interact only with OsLSD1 in one summary of interactions. (huang2015stressresponsiveexpressionsubcellular pages 1-3)

The authors further propose these interactions may occur in the nucleus (supported indirectly by nuclear localization of OsMC1 and prior nuclear localization evidence for an LSD1 homolog), though in vivo confirmation is explicitly noted as needed. (huang2015stressresponsiveexpressionsubcellular pages 13-15)

4) Expression and regulation

4.1 Light responsiveness

OsLSD1 expression is light-induced / dark-suppressed:
* Dark treatment reduced OsLSD1 transcripts at 4 h and 24 h in darkness; re-exposure to light restored transcript accumulation within ~4–5 h. (wang2005oslsd1arice pages 2-4)

4.2 Tissue expression

RT-PCR indicated OsLSD1 expression is detectable constitutively in root, stem, and leaf (as reported in Wang et al.). (wang2005oslsd1arice pages 2-4)

5) Recent developments (prioritizing 2023–2024)

5.1 2024 GWAS nominates OsLSD1 as a callus-induction candidate gene

A 2024 rice GWAS on callus induction rate (CIR)—important for transformation and breeding pipelines—analyzed:
* 368 rice accessions
* 994,188 SNPs
* Identified 104 significant SNP loci
* Nominated 13 high-confidence candidate genes, including OsLSD1, citing prior evidence for roles in callus differentiation. (song2024acyclingene pages 2-4)

This is the strongest tool-accessible 2024 linkage connecting natural variation near OsLSD1 to tissue culture performance, although the paper did not functionally validate OsLSD1 directly. (song2024acyclingene pages 2-4)

5.2 2024–era expert framing: crop improvement leverage points and constraints

A focused 2019 review (still widely cited) argues LSD1/EDS1/PAD4 modules are attractive engineering targets because they coordinate ROS and hormone signaling (SA/ET) and acclimation responses, and highlights genome editing (e.g., CRISPR/Cas9) as a practical route for crop improvement—while emphasizing environment-dependent and pleiotropic outcomes that require careful tuning. (bernacki2019biotechnologicalpotentialof pages 1-3)

Rice-specific data in that review include that LSD1 antisense rice shows PR1 upregulation and lesion phenotype consistent with LSD1 as a negative regulator of cell death, and that expressing rice LSD1 in tobacco enhanced mycotoxin resistance. (bernacki2019biotechnologicalpotentialof pages 9-11)

6) Current applications and real-world implementations

6.1 Plant transformation and regeneration

Because OsLSD1 overexpression materially shortens callus differentiation time (7–10 days to 3–5 days) and is now implicated by GWAS as a CIR-associated candidate, OsLSD1 is conceptually relevant for:
* optimizing Agrobacterium-mediated transformation pipelines (callus induction/differentiation efficiency), and
* improving genotype-independent tissue culture response, a known bottleneck in rice functional genomics and breeding. (wang2005oslsd1arice pages 2-4, song2024acyclingene pages 2-4)

6.2 Disease resistance engineering and risk tradeoffs

OsLSD1 manipulation affects blast resistance phenotypes in transgenic experiments, and authors explicitly proposed OsLSD1 as a candidate for engineering crops with useful traits. (wang2005oslsd1arice pages 6-7)

However, expert synthesis emphasizes that LSD1-like regulation of ROS/PCD is highly context-dependent (environment, stress combinations), and engineering strategies must avoid runaway cell death and yield penalties by controlling expression level/tissue specificity or by targeting network partners. (bernacki2019biotechnologicalpotentialof pages 1-3, epple2003antagonisticcontrolof pages 5-6)

7) Relevant statistics and data highlights

7.1 Experimental scale and measured outcomes (Wang et al., 2005)

7.2 GWAS scale (Song et al., 2024)

8) Expert opinions and authoritative analyses

8.1 Threshold model and antagonism within LSD1-like family

Arabidopsis data support the idea that LSD1-like proteins (LSD1 vs LOL1) act antagonistically to gate ROS-associated PCD, potentially functioning like competing transcriptional regulators or scaffold proteins and establishing a threshold for death commitment. This framework is widely invoked for interpreting OsLSD1-like proteins in crops. (epple2003antagonisticcontrolof pages 5-6, epple2003antagonisticcontrolof pages 4-5)

8.2 Biotechnology perspective (LSD1/EDS1/PAD4 network)

The crop-biotech review argues LSD1/EDS1/PAD4 nodes can affect PCD, immunity, abiotic stress acclimation, cell wall modification, yield/biomass traits, and water-use efficiency, and are thus candidates for breeding and genome editing. It emphasizes ortholog presence in crops (including rice) and stresses the importance of balancing resistance with growth given environment-dependence. (bernacki2019biotechnologicalpotentialof pages 1-3)

9) Visual evidence from primary literature

A representative figure from the rice OsLSD1 primary study shows FB1 (fumonisin B1) treatment outcomes in transgenic tobacco seedlings, illustrating the reported phenotype of enhanced tolerance associated with OsLSD1 overexpression (note: the paper states GFP localization images were “data not shown”). (wang2005oslsd1arice media ab6a47f9)

Evidence map (quick reference)

Claim/Aspect Key evidence/details Source DOI/URL Pub date
Identity / disambiguation Rice OsLSD1 is a plant-specific small zinc-finger protein, not the mammalian LSD1/KDM1A demethylase. Cloned as GenBank AY525368 from Oryza sativa; cDNA 988 bp, ORF 432 bp, predicted protein 143 aa (~14.8 kDa), mapped to chromosome 8 (PAC clone P0672D01). Rice literature also links OsLSD1 to LOC_Os08g06280 and review/table evidence links the family entry to Os08g0159500. (wang2005oslsd1arice pages 2-4, wang2005oslsd1arice pages 1-2, kang2021ricelesionmimic pages 4-4, li2014identificationandnetwork pages 1-2) Wang 2005, Molecular Plant-Microbe Interactions; Li 2014, POJ; Kang 2021, Plants https://doi.org/10.1094/mpmi-18-0375 ; https://doi.org/10.3316/informit.897038318452468 ; https://doi.org/10.3390/plants10081598 May 2005; 2014; Aug 2021
Domains / family features OsLSD1 contains three internally conserved C2C2-type zinc finger / LSD1-like domains with consensus motif reported as CxxCxxLLMYxxGAxSVxCxxC; it shows 58% identity to Arabidopsis LSD1 and 85% identity to Arabidopsis LOL1. Rice lesion-mimic review classifies it as a C2C2-type zinc finger protein. (wang2005oslsd1arice pages 1-2, kang2021ricelesionmimic pages 4-4) Wang 2005, Molecular Plant-Microbe Interactions; Kang 2021, Plants https://doi.org/10.1094/mpmi-18-0375 ; https://doi.org/10.3390/plants10081598 May 2005; Aug 2021
Subcellular localization OsLSD1-GFP localized to the nucleus in tobacco cells/root tips, supporting nuclear function. A later metacaspase study notes OsMC1–OsLSD1 interaction may occur in the nucleus and cites nucleus-localized LSD1 homolog evidence. (wang2005oslsd1arice pages 1-2, huang2015stressresponsiveexpressionsubcellular pages 13-15) Wang 2005, Molecular Plant-Microbe Interactions; Huang 2015, International Journal of Molecular Sciences https://doi.org/10.1094/mpmi-18-0375 ; https://doi.org/10.3390/ijms160716216 May 2005; Jul 2015
Function in programmed cell death (PCD) Core interpretation: OsLSD1 is a negative regulator of plant PCD. Antisense suppression produced lesion mimic phenotype, increased PR-1 mRNA, and accelerated hypersensitive response to avirulent blast isolates; overexpression in tobacco enhanced tolerance to the PCD-inducing toxin fumonisin B1 (FB1). Reviews summarize OsLSD1 as regulating PCD and hypersensitive response. (wang2005oslsd1arice pages 1-2, wang2005oslsd1arice pages 2-4, wang2005oslsd1arice pages 6-7, huang2015stressresponsiveexpressionsubcellular pages 1-3, kang2021ricelesionmimic pages 4-4) Wang 2005, Molecular Plant-Microbe Interactions; Huang 2015, International Journal of Molecular Sciences; Kang 2021, Plants https://doi.org/10.1094/mpmi-18-0375 ; https://doi.org/10.3390/ijms160716216 ; https://doi.org/10.3390/plants10081598 May 2005; Jul 2015; Aug 2021
Callus differentiation / regeneration Overexpression of OsLSD1 accelerated callus differentiation and plant regeneration. In transformed rice calli, differentiation time decreased from 7–10 days in vector controls to 3–5 days in OsLSD1-overexpression lines. Authors conclude OsLSD1 plays a positive role in callus differentiation. (wang2005oslsd1arice pages 1-2, wang2005oslsd1arice pages 2-4) Wang 2005, Molecular Plant-Microbe Interactions https://doi.org/10.1094/mpmi-18-0375 May 2005
Disease resistance / blast interaction OsLSD1 is linked to rice blast defense. In Wang et al., both sense and antisense transgenics showed significantly enhanced resistance to a virulent blast isolate; antisense plants also showed faster defense/HR responses to avirulent blast. Expression/network analysis later listed OsLSD1 (LOC_Os08g06280) among rice ZFP genes associated with defense against Magnaporthe oryzae, and reported the LSD1 family was repressed after inoculation in their expression dataset. (wang2005oslsd1arice pages 1-2, wang2005oslsd1arice pages 2-4, wang2005oslsd1arice pages 6-7, li2014identificationandnetwork pages 1-2) Wang 2005, Molecular Plant-Microbe Interactions; Li 2014, POJ https://doi.org/10.1094/mpmi-18-0375 ; https://doi.org/10.3316/informit.897038318452468 May 2005; 2014
Interaction partners Yeast two-hybrid assays showed OsMC1, OsMC2, and OsMC3 interact with OsLSD1 and OsLSD3, but not with OsLSD2/OsLOL1/OsLOL2; OsMC3 only interacted with OsLSD1 in one summary. N- and C-terminal regions of OsMC1 also interacted with OsLSD1. These data place OsLSD1 in metacaspase-linked PCD signaling. (huang2015stressresponsiveexpressionsubcellular pages 13-15, huang2015stressresponsiveexpressionsubcellular pages 1-3) Huang 2015, International Journal of Molecular Sciences https://doi.org/10.3390/ijms160716216 Jul 2015
Expression regulation OsLSD1 transcript abundance is light-induced / dark-suppressed: after 24 h dark treatment, transcript levels decreased markedly by 4 h and 24 h in darkness, then recovered after re-exposure to light (4–5 h). RT-PCR detected constitutive expression in root, stem, and leaf. (wang2005oslsd1arice pages 1-2, wang2005oslsd1arice pages 2-4) Wang 2005, Molecular Plant-Microbe Interactions https://doi.org/10.1094/mpmi-18-0375 May 2005
Recent GWAS association (2024) A 2024 rice GWAS for callus induction rate (CIR) used 368 accessions and 994,188 SNPs, identifying 104 significant SNPs and 13 candidate genes. OsLSD1 was nominated as a candidate based on annotation/transcriptome overlap, reinforcing prior evidence that OsLSD1 contributes to callus differentiation, although this study did not functionally validate OsLSD1 directly. (song2024acyclingene pages 2-4) Song 2024, Rice https://doi.org/10.1186/s12284-024-00742-8 Oct 2024

Table: This table compiles key evidence for rice OsLSD1/Protein LSD1 (UniProt Q0J7V9; LOC_Os08g06280; Os08g0159500), emphasizing identity verification, molecular features, biological roles, and recent 2024 genetic association data. It is useful as a compact evidence map linking specific claims to primary and review sources.

Limitations of this report (tool-access constraints)

Key primary sources (with URLs and publication dates)

References

  1. (wang2005oslsd1arice pages 1-2): Lijuan Wang, Zhongyou Pei, Yingchuan Tian, and Chaozu He. Oslsd1, a rice zinc finger protein, regulates programmed cell death and callus differentiation. Molecular plant-microbe interactions : MPMI, 18 5:375-84, May 2005. URL: https://doi.org/10.1094/mpmi-18-0375, doi:10.1094/mpmi-18-0375. This article has 196 citations.

  2. (wang2005oslsd1arice pages 2-4): Lijuan Wang, Zhongyou Pei, Yingchuan Tian, and Chaozu He. Oslsd1, a rice zinc finger protein, regulates programmed cell death and callus differentiation. Molecular plant-microbe interactions : MPMI, 18 5:375-84, May 2005. URL: https://doi.org/10.1094/mpmi-18-0375, doi:10.1094/mpmi-18-0375. This article has 196 citations.

  3. (huang2015stressresponsiveexpressionsubcellular pages 13-15): Lei Huang, Huijuan Zhang, Yongbo Hong, Shixia Liu, Dayong Li, and Fengming Song. Stress-responsive expression, subcellular localization and protein–protein interactions of the rice metacaspase family. International Journal of Molecular Sciences, 16:16216-16241, Jul 2015. URL: https://doi.org/10.3390/ijms160716216, doi:10.3390/ijms160716216. This article has 59 citations.

  4. (huang2015stressresponsiveexpressionsubcellular pages 1-3): Lei Huang, Huijuan Zhang, Yongbo Hong, Shixia Liu, Dayong Li, and Fengming Song. Stress-responsive expression, subcellular localization and protein–protein interactions of the rice metacaspase family. International Journal of Molecular Sciences, 16:16216-16241, Jul 2015. URL: https://doi.org/10.3390/ijms160716216, doi:10.3390/ijms160716216. This article has 59 citations.

  5. (song2024acyclingene pages 2-4): Wenjing Song, Jian Zhang, Wenyu Lu, Siyi Liang, Hairong Cai, Yuanyuan Guo, Shiyi Chen, Jiafeng Wang, Tao Guo, Hong Liu, and Dehua Rao. A cyclin gene oscycb1;5 regulates seed callus induction in rice revealed by genome wide association study. Rice, Oct 2024. URL: https://doi.org/10.1186/s12284-024-00742-8, doi:10.1186/s12284-024-00742-8. This article has 1 citations and is from a peer-reviewed journal.

  6. (li2014identificationandnetwork pages 1-2): WT Li, WL Chen, C Yang, J Wang, L Yang, and M He. Identification and network construction of zinc finger protein (zfp) genes involved in the rice-'magnaporthe oryzae'interaction. Unknown journal, 2014. URL: https://doi.org/10.3316/informit.897038318452468, doi:10.3316/informit.897038318452468.

  7. (kang2021ricelesionmimic pages 4-4): Sang Gu Kang, Kyung Eun Lee, Mahendra Singh, Pradeep Kumar, and Mohammad Nurul Matin. Rice lesion mimic mutants (lmm): the current understanding of genetic mutations in the failure of ros scavenging during lesion formation. Plants, 10:1598, Aug 2021. URL: https://doi.org/10.3390/plants10081598, doi:10.3390/plants10081598. This article has 46 citations.

  8. (epple2003antagonisticcontrolof pages 5-6): Petra Epple, Amanda A. Mack, Veronica R. F. Morris, and Jeffery L. Dangl. Antagonistic control of oxidative stress-induced cell death in arabidopsis by two related, plant-specific zinc finger proteins. Proceedings of the National Academy of Sciences of the United States of America, 100:6831-6836, May 2003. URL: https://doi.org/10.1073/pnas.1130421100, doi:10.1073/pnas.1130421100. This article has 237 citations and is from a highest quality peer-reviewed journal.

  9. (epple2003antagonisticcontrolof pages 4-5): Petra Epple, Amanda A. Mack, Veronica R. F. Morris, and Jeffery L. Dangl. Antagonistic control of oxidative stress-induced cell death in arabidopsis by two related, plant-specific zinc finger proteins. Proceedings of the National Academy of Sciences of the United States of America, 100:6831-6836, May 2003. URL: https://doi.org/10.1073/pnas.1130421100, doi:10.1073/pnas.1130421100. This article has 237 citations and is from a highest quality peer-reviewed journal.

  10. (wang2005oslsd1arice pages 6-7): Lijuan Wang, Zhongyou Pei, Yingchuan Tian, and Chaozu He. Oslsd1, a rice zinc finger protein, regulates programmed cell death and callus differentiation. Molecular plant-microbe interactions : MPMI, 18 5:375-84, May 2005. URL: https://doi.org/10.1094/mpmi-18-0375, doi:10.1094/mpmi-18-0375. This article has 196 citations.

  11. (bernacki2019biotechnologicalpotentialof pages 1-3): Maciej Jerzy Bernacki, Weronika Czarnocka, Magdalena Szechyńska-Hebda, Ron Mittler, and Stanisław Karpiński. Biotechnological potential of lsd1, eds1, and pad4 in the improvement of crops and industrial plants. Plants, 8:290, Aug 2019. URL: https://doi.org/10.3390/plants8080290, doi:10.3390/plants8080290. This article has 22 citations.

  12. (bernacki2019biotechnologicalpotentialof pages 9-11): Maciej Jerzy Bernacki, Weronika Czarnocka, Magdalena Szechyńska-Hebda, Ron Mittler, and Stanisław Karpiński. Biotechnological potential of lsd1, eds1, and pad4 in the improvement of crops and industrial plants. Plants, 8:290, Aug 2019. URL: https://doi.org/10.3390/plants8080290, doi:10.3390/plants8080290. This article has 22 citations.

  13. (wang2005oslsd1arice media ab6a47f9): Lijuan Wang, Zhongyou Pei, Yingchuan Tian, and Chaozu He. Oslsd1, a rice zinc finger protein, regulates programmed cell death and callus differentiation. Molecular plant-microbe interactions : MPMI, 18 5:375-84, May 2005. URL: https://doi.org/10.1094/mpmi-18-0375, doi:10.1094/mpmi-18-0375. This article has 196 citations.

Artifacts

Citations

  1. li2014identificationandnetwork pages 1-2
  2. kang2021ricelesionmimic pages 4-4
  3. huang2015stressresponsiveexpressionsubcellular pages 13-15
  4. huang2015stressresponsiveexpressionsubcellular pages 1-3
  5. song2024acyclingene pages 2-4
  6. bernacki2019biotechnologicalpotentialof pages 1-3
  7. bernacki2019biotechnologicalpotentialof pages 9-11
  8. epple2003antagonisticcontrolof pages 4-5
  9. epple2003antagonisticcontrolof pages 5-6
  10. https://doi.org/10.1094/mpmi-18-0375
  11. https://doi.org/10.3316/informit.897038318452468
  12. https://doi.org/10.3390/plants10081598
  13. https://doi.org/10.3390/ijms160716216
  14. https://doi.org/10.1186/s12284-024-00742-8
  15. https://doi.org/10.3390/plants8080290
  16. https://doi.org/10.1073/pnas.1130421100
  17. https://doi.org/10.1094/mpmi-18-0375,
  18. https://doi.org/10.3390/ijms160716216,
  19. https://doi.org/10.1186/s12284-024-00742-8,
  20. https://doi.org/10.3316/informit.897038318452468,
  21. https://doi.org/10.3390/plants10081598,
  22. https://doi.org/10.1073/pnas.1130421100,
  23. https://doi.org/10.3390/plants8080290,