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The PII Signal Transduction Protein of Arabidopsis thaliana Forms an Arginine-regulated Complex with Plastid N-Acetyl Glutamate Kinase
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1016/0014-5793(95)00197-hopenalex-snapshot
Purification of the hepatic glycogen‐associated form of protein phosphatase‐1 by microcystin‐Sepharose affinity chromatography
inferredcites →https://doi.org/10.1016/j.bbapap.2004.02.009openalex-snapshot
Lack of evidence for phosphorylation of Arabidopsis thaliana PII: implications for plastid carbon and nitrogen signaling
inferredcites →https://doi.org/10.1016/j.ceb.2005.02.008openalex-snapshot
The expanding TOR signaling network
inferredcites →https://doi.org/10.1016/j.femsre.2003.11.001openalex-snapshot
Global carbon/nitrogen control by PIIsignal transduction in cyanobacteria: from signals to targets
inferredcites →https://doi.org/10.1016/j.mib.2005.02.011openalex-snapshot
PII signal transduction proteins: sensors of α-ketoglutarate that regulate nitrogen metabolism
inferredcites →https://doi.org/10.1016/s0014-5793(03)00384-3openalex-snapshot
Transcriptional effects of the signal transduction protein PII (glnB gene product) on NtcA‐dependent genes in Synechococcus sp. PCC 7942
inferredcites →https://doi.org/10.1016/s0014-5793(99)01624-5openalex-snapshot
Protein PII regulates both inorganic carbon and nitrate uptake and is modified by a redox signal in Synechocystis PCC 6803
inferredcites →https://doi.org/10.1016/s0966-842x(00)01709-1openalex-snapshot
PII signal transduction proteins
inferredcites →https://doi.org/10.1016/s0966-842x(00)01849-7openalex-snapshot
PII: a remarkable regulatory protein
inferredcites →https://doi.org/10.1016/s1046-5928(02)00018-9openalex-snapshot
Expression and purification of the chloroplast putative nitrogen sensor, PII, of Arabidopsis thaliana
inferredcites →https://doi.org/10.1038/sj.embor.7400479openalex-snapshot
The phosphoinositide‐3‐OH‐kinase‐related kinases of Arabidopsis thaliana
inferredcites →https://doi.org/10.1046/j.1365-313x.2003.01634.xopenalex-snapshot
Molecular properties of the putative nitrogen sensor PII from Arabidopsis thaliana
inferredcites →https://doi.org/10.1046/j.1432-1327.2000.01043.xopenalex-snapshot
Phosphorylation of the signal transducer PII protein and an additional effector are required for the PII‐mediated regulation of nitrate and nitrite uptake in the cyanobacterium Synechococcus sp. PCC 7942
inferredcites →https://doi.org/10.1073/pnas.95.23.13965openalex-snapshot
A PII-like protein in Arabidopsis : Putative role in nitrogen sensing
inferredcites →https://doi.org/10.1074/jbc.c500169200openalex-snapshot
Rheb Binding to Mammalian Target of Rapamycin (mTOR) Is Regulated by Amino Acid Sufficiency
inferredcites →https://doi.org/10.1074/jbc.m410971200openalex-snapshot
Complex Formation and Catalytic Activation by the PII Signaling Protein of N-Acetyl-l-glutamate Kinase from Synechococcus elongatus Strain PCC 7942
inferredcites →https://doi.org/10.1074/mcp.m300115-mcp200openalex-snapshot
Proteomic Characterization of Protein Phosphatase Complexes of the Mammalian Nucleus
inferredcites →https://doi.org/10.1093/pcp/pch199openalex-snapshot
Interaction of N-Acetylglutamate Kinase with a PII-Like Protein in Rice
inferredcites →https://doi.org/10.1104/pp.103.025627openalex-snapshot
Interpreting the Plastid Carbon, Nitrogen, and Energy Status. A Role for PII?
inferredcites →https://doi.org/10.1111/j.1365-2958.2004.04058.xopenalex-snapshot
The Synechococcus elongatus PII signal transduction protein controls arginine synthesis by complex formation with N‐acetyl‐ l ‐glutamate kinase
inferredcites →https://doi.org/10.1128/jb.176.1.84-91.1994openalex-snapshot
The PII protein in the cyanobacterium Synechococcus sp. strain PCC 7942 is modified by serine phosphorylation and signals the cellular N-status
inferredcites →https://doi.org/10.1128/jb.185.8.2582-2591.2003openalex-snapshot
Signal Transduction Protein P II Is Required for NtcA-Regulated Gene Expression during Nitrogen Deprivation in the Cyanobacterium Synechococcus elongatus Strain PCC 7942
inferredcites →https://doi.org/10.1128/jb.186.11.3346-3354.2004openalex-snapshot
Interactions between the Nitrogen Signal Transduction Protein PII and N -Acetyl Glutamate Kinase in Organisms That Perform Oxygenic Photosynthesis
inferredcites →https://doi.org/10.1128/jb.186.18.6142-6149.2004openalex-snapshot
Arginine Biosynthesis inThermotoga maritima: Characterization of the Arginine-SensitiveN-Acetyl- l -Glutamate Kinase
inferredcites →https://doi.org/10.1128/mmbr.65.1.80-105.2001openalex-snapshot
PIISignal Transduction Proteins, Pivotal Players in Microbial Nitrogen Control
inferredcites →https://doi.org/10.1199/tab.0010openalex-snapshot
Primary N-assimilation into Amino Acids in Arabidopsis
inferredcites →https://doi.org/10.1199/tab.0018openalex-snapshot
Purine and Pyrimidine Nucleotide Synthesis and Metabolism
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Incoming claims: where this work appears in other papers’ reference lists and arguments.
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inferred← citeshttps://doi.org/10.1007/s00425-012-1801-0openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s00425-026-05157-xopenalex-snapshot
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inferred← citeshttps://doi.org/10.1016/b978-0-12-811308-0.00003-xopenalex-snapshot
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inferred← citeshttps://doi.org/10.1016/b978-0-443-18675-2.00005-5openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ab.2007.06.032openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.bbapap.2007.07.015openalex-snapshot
The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G
inferred← citeshttps://doi.org/10.1016/j.bbrc.2009.07.088openalex-snapshot
Metabolite regulation of the interaction between Arabidopsis thaliana PII and N-acetyl-l-glutamate kinase
inferred← citeshttps://doi.org/10.1016/j.febslet.2006.02.075openalex-snapshot
The regulatory PII protein controls arginine biosynthesis in Arabidopsis
inferred← citeshttps://doi.org/10.1016/j.febslet.2008.02.056openalex-snapshot
Chloroplast nitrite uptake is enhanced in Arabidopsis PII mutants
inferred← citeshttps://doi.org/10.1016/j.jbiotec.2011.12.008openalex-snapshot
Isolation of cyanophycin from tobacco and potato plants with constitutive plastidic cphATe gene expression
inferred← citeshttps://doi.org/10.1016/j.jmb.2009.04.053openalex-snapshot
N-Acetyl-l-Glutamate Kinase (NAGK) from Oxygenic Phototrophs: PII Signal Transduction across Domains of Life Reveals Novel Insights in NAGK Control
inferred← citeshttps://doi.org/10.1016/j.phytochem.2014.04.012openalex-snapshot
Evidence that glutamine transaminase and omega-amidase potentially act in tandem to close the methionine salvage cycle in bacteria and plants
inferred← citeshttps://doi.org/10.1016/j.plantsci.2024.112327openalex-snapshot
Loss of PII-dependent control of arginine biosynthesis in Dunaliella salina
inferred← citeshttps://doi.org/10.1016/j.plaphy.2023.107719openalex-snapshot
Expression of ZmNAGK in tobacco enhances heat stress tolerance via activation of antioxidant-associated defense
inferred← citeshttps://doi.org/10.1016/j.sbi.2008.11.002openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.tim.2007.11.004openalex-snapshot
PII signal transducers: novel functional and structural insights
inferred← citeshttps://doi.org/10.1016/j.tplants.2009.07.003openalex-snapshot
PII in higher plants: a modern role for an ancient protein
inferred← citeshttps://doi.org/10.1016/j.tplants.2012.05.005openalex-snapshot
Unusual cyanobacterial TCA cycles: not broken just different
inferred← citeshttps://doi.org/10.1038/s41467-023-40002-9openalex-snapshot
Comparative genomics reveals a unique nitrogen-carbon balance system in Asteraceae.
inferred← citeshttps://doi.org/10.1038/s41477-025-02080-zopenalex-snapshot
RETICULATA1 is a plastid-localized basic amino acid transporter
inferred← citeshttps://doi.org/10.1038/s41598-017-16644-3openalex-snapshot
Evidence for PII with NAGK interaction that regulates Arg synthesis in the microalga Myrmecia incisa in response to nitrogen starvation
inferred← citeshttps://doi.org/10.1042/bj20090722openalex-snapshot
Metabolic control exerted by the 2-oxoglutarate dehydrogenase reaction: a cross-kingdom comparison of the crossroad between energy production and nitrogen assimilation
inferred← citeshttps://doi.org/10.1042/bj20101035openalex-snapshot
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inferred← citeshttps://doi.org/10.1042/bj20110536openalex-snapshot
Signal-transduction protein PII from Synechococcus elongatus PCC 7942 senses low adenylate energy charge in vitro
inferred← citeshttps://doi.org/10.1042/bst0390189openalex-snapshot
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inferred← citeshttps://doi.org/10.1073/pnas.0602278103openalex-snapshot
Regulation of nitrogenase by 2-oxoglutarate-reversible, direct binding of a PII-like nitrogen sensor protein to dinitrogenase
inferred← citeshttps://doi.org/10.1073/pnas.0705987104openalex-snapshot
The crystal structure of the complex of P II and acetylglutamate kinase reveals how P II controls the storage of nitrogen as arginine
inferred← citeshttps://doi.org/10.1073/pnas.0910097107openalex-snapshot
Chloroplast acetyl-CoA carboxylase activity is 2-oxoglutarate–regulated by interaction of PII with the biotin carboxyl carrier subunit
inferred← citeshttps://doi.org/10.1074/jbc.m602477200openalex-snapshot
In Vitro Analysis of the Escherichia coli AmtB-GlnK Complex Reveals a Stoichiometric Interaction and Sensitivity to ATP and 2-Oxoglutarate
inferred← citeshttps://doi.org/10.1074/jbc.m707127200openalex-snapshot
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inferred← citeshttps://doi.org/10.1074/mcp.m700171-mcp200openalex-snapshot
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inferred← citeshttps://doi.org/10.1093/jxb/eraf260openalex-snapshot
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inferred← citeshttps://doi.org/10.1093/jxb/erm016openalex-snapshot
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inferred← citeshttps://doi.org/10.1093/jxb/erm121openalex-snapshot
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inferred← citeshttps://doi.org/10.1093/jxb/ern123openalex-snapshot
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inferred← citeshttps://doi.org/10.1093/jxb/erp072openalex-snapshot
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inferred← citeshttps://doi.org/10.1093/jxb/erq060openalex-snapshot
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inferred← citeshttps://doi.org/10.1093/jxb/erq453openalex-snapshot
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inferred← citeshttps://doi.org/10.1093/pcp/pcab030openalex-snapshot
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inferred← citeshttps://doi.org/10.1093/pcp/pcj062openalex-snapshot
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inferred← citeshttps://doi.org/10.1093/pcp/pcj088openalex-snapshot
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inferred← citeshttps://doi.org/10.1093/pcp/pcm072openalex-snapshot
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inferred← citeshttps://doi.org/10.1094/mpmi-12-11-0322openalex-snapshot
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inferred← citeshttps://doi.org/10.1099/mic.0.037309-0openalex-snapshot
Effects of spontaneous mutations in PipX functions and regulatory complexes on the cyanobacterium Synechococcus elongatus strain PCC 7942
inferred← citeshttps://doi.org/10.1099/mic.0.047266-0openalex-snapshot
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inferred← citeshttps://doi.org/10.1099/mic.0.2006/003574-0openalex-snapshot
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inferred← citeshttps://doi.org/10.1104/pp.106.088500openalex-snapshot
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inferred← citeshttps://doi.org/10.1104/pp.109.152694openalex-snapshot
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inferred← citeshttps://doi.org/10.1104/pp.112.210583openalex-snapshot
The ArabidopsisTUMOR PRONE5Gene Encodes an Acetylornithine Aminotransferase Required for Arginine Biosynthesis and Root Meristem Maintenance in Blue Light
inferred← citeshttps://doi.org/10.1105/tpc.112.107292openalex-snapshot
Arabidopsis BPM Proteins Function as Substrate Adaptors to a CULLIN3-Based E3 Ligase to Affect Fatty Acid Metabolism in Plants
inferred← citeshttps://doi.org/10.1111/febs.13584openalex-snapshot
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inferred← citeshttps://doi.org/10.1111/j.1365-2958.2006.05231.xopenalex-snapshot
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inferred← citeshttps://doi.org/10.1111/j.1365-3040.2006.01580.xopenalex-snapshot
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inferred← citeshttps://doi.org/10.1111/j.1365-313x.2007.03196.xopenalex-snapshot
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inferred← citeshttps://doi.org/10.1111/j.1365-313x.2010.04332.xopenalex-snapshot
PII is induced by WRINKLED1 and fine-tunes fatty acid composition in seeds of Arabidopsis thaliana
inferred← citeshttps://doi.org/10.1111/j.1365-313x.2012.04984.xopenalex-snapshot
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inferred← citeshttps://doi.org/10.1111/j.1574-6976.2012.00351.xopenalex-snapshot
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inferred← citeshttps://doi.org/10.1111/jipb.12536openalex-snapshot
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inferred← citeshttps://doi.org/10.1111/nph.16492openalex-snapshot
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inferred← citeshttps://doi.org/10.1111/ppl.70228openalex-snapshot
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inferred← citeshttps://doi.org/10.1111/tpj.16684openalex-snapshot
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inferred← citeshttps://doi.org/10.1111/tpj.16700openalex-snapshot
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inferred← citeshttps://doi.org/10.1128/aem.00039-20openalex-snapshot
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inferred← citeshttps://doi.org/10.1128/jb.00557-09openalex-snapshot
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inferred← citeshttps://doi.org/10.1134/s1021443713040055openalex-snapshot
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inferred← citeshttps://doi.org/10.1139/b07-040openalex-snapshot
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inferred← citeshttps://doi.org/10.1146/annurev.arplant.58.032806.103750openalex-snapshot
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inferred← citeshttps://doi.org/10.1146/annurev.micro.61.080706.093409openalex-snapshot
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inferred← citeshttps://doi.org/10.11606/t.105.2021.tde-09092021-145727openalex-snapshot
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inferred← citeshttps://doi.org/10.1186/1471-2229-8-120openalex-snapshot
Arabidopsis At5g39790 encodes a chloroplast-localized, carbohydrate-binding, coiled-coil domain-containing putative scaffold protein
inferred← citeshttps://doi.org/10.1186/1471-2229-8-40openalex-snapshot
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inferred← citeshttps://doi.org/10.1199/tab.0140openalex-snapshot
Proline Metabolism and Its Implications for Plant-Environment Interaction
inferred← citeshttps://doi.org/10.1371/journal.pone.0010098openalex-snapshot
Distinct Pathways Mediate the Sorting of Tail-Anchored Proteins to the Plastid Outer Envelope
inferred← citeshttps://doi.org/10.1371/journal.pone.0035845openalex-snapshot
Mutational Analysis of the Cyanobacterial Nitrogen Regulator PipX
inferred← citeshttps://doi.org/10.1371/journal.pone.0039510openalex-snapshot
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inferred← citeshttps://doi.org/10.17169/refubium-11376openalex-snapshot
Functional characterisation of the TUP5 gene in Arabidopsis thaliana
inferred← citeshttps://doi.org/10.21203/rs.2.17483/v1openalex-snapshot
Isopentenyl Phosphate Kinases are Ubiquitous and Copy Numbers are Conserved in Plant Genomes
inferred← citeshttps://doi.org/10.2134/agronmonogr51.c3openalex-snapshot
Changing Metabolic Pathways to Manipulate Legume Seed Maturation and Composition
inferred← citeshttps://doi.org/10.2174/187231309789054904openalex-snapshot
Regulation of Catalysis Within Cellular Network: Metabolic and Signaling Implications of the 2-Oxoglutarate Oxidative Decarboxylation
inferred← citeshttps://doi.org/10.3354/ab00335openalex-snapshot
Nutrient availability alters levels of non-translationally synthesized nitrogen-rich dipeptides in Emiliania huxleyi
inferred← citeshttps://doi.org/10.3389/fpls.2015.00534openalex-snapshot
Physiological implications of arginine metabolism in plants
inferred← citeshttps://doi.org/10.3389/fpls.2017.01299openalex-snapshot
Ectopic Expression of PII Induces Stomatal Closure in Lotus japonicus
inferred← citeshttps://doi.org/10.3389/fpls.2018.01496openalex-snapshot
New Insights Into Sunflower (Helianthus annuus L.) FatA and FatB Thioesterases, Their Regulation, Structure and Distribution
inferred← citeshttps://doi.org/10.3389/fpls.2018.01902openalex-snapshot
Over-Expression of a Maize N-Acetylglutamate Kinase Gene (ZmNAGK) Improves Drought Tolerance in Tobacco
inferred← citeshttps://doi.org/10.3389/fpls.2020.00194openalex-snapshot
Primary Metabolite Responses to Oxidative Stress in Early-Senescing and Paraquat Resistant Arabidopsis thaliana rcd1 (Radical-Induced Cell Death1)
inferred← citeshttps://doi.org/10.3389/fpls.2020.00823openalex-snapshot
Structural and Functional Characteristics of Two Molecular Variants of the Nitrogen Sensor PII in Maritime Pine
inferred← citeshttps://doi.org/10.3389/fpls.2022.894208openalex-snapshot
Histidine kinase inhibitors impair shoot regeneration in Arabidopsis thaliana via cytokinin signaling and SAM patterning determinants
inferred← citeshttps://doi.org/10.3390/agronomy6020026openalex-snapshot
Nitrogen Economy and Nitrogen Environmental Interactions in Conifers
inferred← citeshttps://doi.org/10.3390/ijms222312666openalex-snapshot
Arabidopsis PII Proteins Form Characteristic Foci in Chloroplasts Indicating Novel Properties in Protein Interaction and Degradation
inferred← citeshttps://doi.org/10.3390/ijms241612873openalex-snapshot
N-Acetyl-L-glutamate Kinase of Chlamydomonas reinhardtii: In Vivo Regulation by PII Protein and Beyond
inferred← citeshttps://doi.org/10.3390/plants13233331openalex-snapshot
Understanding the Physiological and Molecular Basis for Differences in Nitrogen Use Efficiency in the Parents of a Winter Wheat MAGIC Population
inferred← citeshttps://doi.org/10.35537/10915/76535openalex-snapshot
Metabolismo de nitrógeno en Bradyrhizobium diazoefficiens: caracterización funcional de las proteínas PII y glutamino sintetasas
inferred← citeshttps://doi.org/10.4236/ajps.2015.618275openalex-snapshot
Nitrogen Nutrition, Its Regulation and Biotechnological Approaches to Improve Crop Productivity
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