Gene Research for GO Annotation Review Falcon citations file

Gene Research for GO Annotation Review

Target

UniProt Context

=== UNIPROT METADATA ===
UniProt ID: P10896
Entry Name: RCA_ARATH
Gene Name: RCA
Protein Name: Ribulose bisphosphate carboxylase/oxygenase activase, chloroplastic
Organism: Arabidopsis thaliana (Mouse-ear cress)
NCBI Taxonomy ID: 3702
Function: Activation of RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) involves the ATP-dependent carboxylation of the epsilon-amino group of lysine leading to a carbamate structure.
Subcellular Location: Plastid, chloroplast stroma. Plastid, chloroplast, plastoglobule
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Research Objective

Prepare a comprehensive literature-backed research report for GO annotation review of the target gene.

Focus on:

  1. The core biochemical activity of the gene product and any substrate specificity.
  2. The activation or maturation mechanism of the protein, including proteolytic processing if relevant.
  3. The best-supported subcellular localization and complexes where the active protein functions.
  4. The strongest experimentally supported biological processes in the target organism, or in very close orthologs when transfer is justified.
  5. Which annotations appear to reflect core function versus context-specific, pleiotropic, or over-extended roles.
  6. Any evidence bearing on apoptosis, developmental cell death, neuronal roles, inflammatory signaling, pyroptosis, synaptic remodeling, protein processing, and localization to cytoplasm, cytosol, nucleus, or signaling complexes.

Output Requirements

Structure the report as:

  1. Executive summary
  2. Molecular function
  3. Biological process roles
  4. Cellular localization and complexes
  5. Annotation-risk assessment
  6. Key literature

Use citations for all substantive claims.

Gene Research Report for GO Annotation Review: RCA (RCA_ARATH; UniProt P10896) in Arabidopsis thaliana

1. Executive summary

Arabidopsis thaliana RCA (Rubisco activase; UniProt P10896 / AT2G39730) encodes a chloroplast-targeted AAA+ ATPase chaperone that maintains Rubisco catalytic competence by ATP-dependent remodeling of inhibited Rubisco active sites to promote release of tightly bound inhibitory sugar phosphates (“Rubisco activase” activity). This is the dominant, high-confidence core molecular function for GO curation (waheeda2023molecularmechanismof pages 1-2, stotz2012structureofgreen pages 41-44).

Two major plant RCA isoforms (α and β) are produced by alternative splicing, with the longer α-isoform containing a C-terminal redox-regulated extension (two cysteines) that links Rubisco activation to chloroplast light/redox status (waheeda2023molecularmechanismof pages 3-4, stotz2012structureofgreen pages 109-113). Recent mechanistic synthesis emphasizes that function is coupled to nucleotide-dependent dynamic oligomerization, with hexamers central to remodeling models (waheeda2023molecularmechanismof pages 5-7, waheeda2023molecularmechanismof pages 4-5).

The best-supported cellular component for the active mature protein is the chloroplast stroma, supported by quantitative chloroplast proteomics that explicitly annotates Rubisco activase as “Plastid stroma” (rutschow2008quantitativeproteomicsof pages 6-7, rutschow2008quantitativeproteomicsof media 65ae96bc). Reports of conditional thylakoid association exist (e.g., moderate heat stress and/or stromal pH/ATP dependence), but these are best treated as context-specific localization rather than primary steady-state residence (stotz2012structureofgreen pages 41-44). Evidence available in this retrieval does not strongly support RCA as a bona fide plastoglobule protein (ytterberg2006proteinprofilingof pages 2-3).

No evidence in the retrieved Arabidopsis/plant RCA literature supports annotations related to apoptosis/developmental cell death, inflammatory signaling, pyroptosis, neuronal/synaptic processes, or nuclear/cytosolic signaling complexes; such annotations are therefore high-risk and likely erroneous for this chloroplast stromal carbon-fixation chaperone (waheeda2023molecularmechanismof pages 1-2, rutschow2008quantitativeproteomicsof pages 6-7, stotz2012structureofgreen pages 41-44).

2. Molecular function

2.1 Key concepts and definitions (current understanding)

Rubisco activase (RCA/Rca) is a co-evolved catalytic chaperone required to sustain Rubisco activity in vivo by reversing inhibited states of Rubisco active sites (waheeda2023molecularmechanismof pages 1-2, stotz2012structureofgreen pages 41-44). RCA belongs to the AAA+ ATPase superfamily; in plant “green-type” systems, ATP binding/hydrolysis drives conformational work that remodels the Rubisco holoenzyme and promotes dissociation of inhibitory sugar-phosphates from Rubisco catalytic sites (waheeda2023molecularmechanismof pages 1-2, waheeda2023molecularmechanismof pages 5-7).

A key curation point is that RCA does not itself catalyze Rubisco carbamylation or Mg2+ loading; instead, by clearing inhibitors and remodeling Rubisco, it indirectly enables Rubisco to attain/maintain its activated carbamylated state under physiological conditions (stotz2012structureofgreen pages 41-44, waheeda2023molecularmechanismof pages 1-2).

2.2 Substrate/target specificity

The proximate “substrate” for RCA is the Rubisco holoenzyme (Rubisco large and small subunits), and the activity is often described operationally as removal of inhibitory sugar phosphates that occupy Rubisco active sites (waheeda2023molecularmechanismof pages 1-2, stotz2012structureofgreen pages 41-44). Mechanistic synthesis and structural work supports the view that, depending on lineage, activases can engage defined Rubisco surfaces and apply force via the central pore to remodel key Rubisco elements; in plant form IB contexts, interactions with the RbcL N-terminus are highlighted as important determinants (waheeda2023molecularmechanismof pages 7-8).

2.3 Mechanism, assemblies, and energetic coupling

Recent mechanistic review emphasizes that RCA function is intimately coupled to dynamic oligomerization (dimer–tetramer–hexamer interconversion) and nucleotide binding state (ATP/ADP) (waheeda2023molecularmechanismof pages 5-7, waheeda2023molecularmechanismof pages 4-5). In biophysical measurements summarized in the 2023 review, ADP-bound assemblies showed subunit exchange rates around ~0.3 s−1 at 8 µM Rca, whereas ATPγS-bound assemblies exchange 2–3× more slowly, consistent with nucleotide stabilization of higher oligomers important for remodeling (waheeda2023molecularmechanismof pages 5-7).

The mechanistic model is consistent with AAA+ chaperones in which ATP hydrolysis is used to generate force for substrate remodeling; hexamers are frequently discussed as the “functional” assembly state for remodeling actions (waheeda2023molecularmechanismof pages 4-5, waheeda2023molecularmechanismof pages 5-7).

2.4 Isoforms and regulatory post-translational modifications (PTMs)

Isoforms. Plant RCA typically occurs as two splice-derived isoforms: β (~43 kDa) and α (~46 kDa), differing by a C-terminal extension present in α (waheeda2023molecularmechanismof pages 3-4, stotz2012structureofgreen pages 109-113).

Redox regulation (α-isoform). The α C-terminal extension contains two cysteines that function as a redox switch controlled by thioredoxin-linked dithiol/disulfide exchange, providing a route for light/redox regulation of Rubisco activation (waheeda2023molecularmechanismof pages 3-4, stotz2012structureofgreen pages 109-113). Mechanistic synthesis notes that the reduced form of αRca favors ATP binding (waheeda2023molecularmechanismof pages 4-5, waheeda2023molecularmechanismof pages 5-7). However, a 2024 Arabidopsis-focused kinetic analysis reported that prolonged DTT treatment (18 h, 2 mM) did not measurably change AtaRca ATPase activity under the tested assay conditions, illustrating that measurable effects can be assay- and context-dependent (chiu2024sisgrtheregulation pages 1-3).

Phosphorylation. A 2024 Arabidopsis report tested phosphorylation of the β isoform (AtbRca) by chloroplast casein kinase 2 (cpCK2), reaching ~95% phosphorylation (with a majority mono-phosphorylated). Under the assay conditions used, phosphorylation had only minor effects on ATPase kinetics (kcat and Km changes small), suggesting phosphorylation may not strongly regulate intrinsic ATPase activity (though other functional effects are not excluded) (chiu2024sisgrtheregulation pages 1-3).

2.5 Recent quantitative enzymology (2024)

Isoform-resolved Arabidopsis ATPase kinetics (at 5 mM free Mg2+) were reported as (chiu2024sisgrtheregulation pages 1-3):

These values support a model in which β-RCA can exhibit higher catalytic efficiency under some conditions, while α-RCA provides regulatory flexibility via redox-sensitive extension rather than maximal ATPase activity (chiu2024sisgrtheregulation pages 1-3, waheeda2023molecularmechanismof pages 3-4).

3. Biological process roles

3.1 Core biological process: photosynthetic carbon fixation regulation

The strongest BP association for Arabidopsis RCA is with photosynthesis / regulation of carbon fixation, via maintaining Rubisco in an activatable state during photosynthetic induction and steady-state carbon assimilation (stotz2012structureofgreen pages 41-44, waheeda2023molecularmechanismof pages 1-2). Classic genetic evidence summarized in the structural dissertation notes that Arabidopsis rca mutants show severe impairment consistent with decreased Rubisco activation state, including high-CO2-dependent growth and RuBP accumulation (stotz2012structureofgreen pages 41-44). These phenotypes support RCA as essential for normal photosynthetic carbon assimilation in planta.

3.2 Context-specific roles: heat sensitivity and thermotolerance of photosynthesis

RCA is widely described as thermolabile and a limiting factor for photosynthetic performance at moderately elevated temperature, motivating engineering/selection of thermostable variants (stotz2012structureofgreen pages 41-44, waheeda2023molecularmechanismof pages 5-7). A mechanistic review cites Arabidopsis engineered triple-mutant RCAs that increased thermostability by ~10°C, demonstrating a quantitative link between RCA biophysics and photosynthetic heat tolerance potential (waheeda2023molecularmechanismof pages 5-7). While heat-response annotations can be justified, they should be scoped as heat effects on photosynthetic carbon fixation capacity rather than implying canonical heat-stress signaling functions (waheeda2023molecularmechanismof pages 5-7, stotz2012structureofgreen pages 41-44).

3.3 Light/redox-linked regulation of Rubisco activation

The α isoform’s redox switch provides a clear route connecting light-dependent chloroplast redox state to Rubisco activation, consistent with a “regulation of photosynthesis / light response” framing in GO (waheeda2023molecularmechanismof pages 3-4, stotz2012structureofgreen pages 109-113). This is a regulatory overlay on the same core biochemical activity rather than an independent process unrelated to carbon fixation.

3.4 Excluded/unsupported biological processes

Within the retrieved literature set, there is no experimental evidence linking Arabidopsis RCA to apoptosis/developmental cell death, inflammatory signaling, pyroptosis, neuronal/synaptic roles, or analogous animal pathways; such terms should be considered annotation errors for this gene unless new, direct plant-specific evidence emerges (waheeda2023molecularmechanismof pages 1-2, stotz2012structureofgreen pages 41-44).

4. Cellular localization and complexes

4.1 Best-supported localization: chloroplast stroma

Quantitative chloroplast proteomics (Plant Physiology, July 2008, URL https://doi.org/10.1104/pp.108.124545) identifies and annotates Arabidopsis Rubisco activase (AT2G39730.1) as “Plastid stroma” (rutschow2008quantitativeproteomicsof pages 6-7, rutschow2008quantitativeproteomicsof media 65ae96bc). This is consistent with RCA’s functional target (Rubisco) residing in the stromal compartment.

4.2 Conditional association with thylakoid membranes

A structural/biochemical synthesis notes that RCA can be reversibly associated with thylakoid membranes during moderate heat stress and/or in a manner dependent on stromal pH and ATP (stotz2012structureofgreen pages 41-44). Given current evidence, this is best treated as context-dependent relocalization or association rather than primary steady-state localization.

4.3 Plastoglobules: evidence assessment

UniProt metadata mentions “chloroplast plastoglobule” as a subcellular location. However, the plastoglobule proteomics study (Plant Physiology, Feb 2006, URL https://doi.org/10.1104/pp.105.076083) emphasized that plastoglobules contain a distinct protein population and that abundant stromal contamination is low, but the excerpts reviewed here did not directly document RCA as a plastoglobule component (ytterberg2006proteinprofilingof pages 2-3). Given the absence of direct RCA plastoglobule detection in the examined evidence, a plastoglobule GO CC annotation for RCA should be treated as higher risk unless supported by direct fractionation/microscopy or plastoglobule-enrichment proteomics explicitly identifying RCA.

4.4 Complexes

RCA acts via nucleotide-dependent oligomers (dimer/tetramer/hexamer ensembles) and transient engagement with Rubisco rather than a single stable constitutive complex; therefore, “complex” annotations should be conservative and consistent with transient chaperone assemblies (waheeda2023molecularmechanismof pages 5-7, waheeda2023molecularmechanismof pages 4-5).

5. Annotation-risk assessment (GO curation guidance)

The following evidence table can guide which annotations are core vs context-specific vs high-risk:

GO aspect Proposed GO term label Evidence-supported statement Key quantitative data (if any) Evidence type Scope/transferability notes Citations
MF ATP-dependent protein-folding chaperone activity / Rubisco activase activity Arabidopsis RCA is a chloroplast-targeted AAA+ ATPase that uses ATP hydrolysis to remodel inhibited Rubisco active sites and promote release of tightly bound inhibitory sugar phosphates; it increases Rubisco activation state but does not itself catalyze carbamylation or Mg2+ loading. AtaRca ATPase: kcat 48.2 ± 0.3 min^-1, Km(ATP) 239 ± 6 µM; AtbRca ATPase: kcat 60.3 ± 0.9 min^-1, Km(ATP) 159 ± 9 µM at 5 mM free Mg2+. Biochemistry, structural biology, mechanistic review Core, high-confidence function for Arabidopsis; mechanism broadly conserved in green-type plant RCAs. (waheeda2023molecularmechanismof pages 1-2, chiu2024sisgrtheregulation pages 1-3, stotz2012structureofgreen pages 41-44)
MF Rubisco binding RCA directly engages Rubisco through its N-terminal regulatory domain and AAA+ pore/recognition elements to remodel the holoenzyme; plant systems are especially sensitive to the Rubisco large-subunit N-terminus. Arabidopsis Rca-mediated subunit exchange/assembly studies support active oligomeric remodeling; ADP-bound exchange ~0.3 s^-1 at 8 µM, ATPγS-bound 2–3× slower. Structural biology, biophysics, mutagenesis Appropriate as a direct-interaction function if GO policy accepts chaperone-substrate binding terms; species specificity of Rubisco recognition argues against overbroad transfer across distant lineages. (waheeda2023molecularmechanismof pages 5-7, waheeda2023molecularmechanismof pages 7-8)
MF ATP hydrolysis activity ATP binding and hydrolysis are integral to RCA function, with active remodeling linked to nucleotide-dependent assembly into higher oligomers, especially hexamers. Peak catalytic rates reported at ~0.5–2.5 µM Rca where dimers/tetramers/hexamers coexist. Biochemistry, oligomerization studies Core mechanistic attribute; should not be mistaken for generic ATPase roles outside chloroplast carbon fixation. (waheeda2023molecularmechanismof pages 4-5)
MF Redox-regulated enzyme activity The long α isoform contains a C-terminal extension with two redox-sensitive cysteines; thioredoxin-linked dithiol/disulfide exchange modulates activity, and the reduced form favors ATP binding. No strong Arabidopsis catalytic shift quantified in the gathered α-isoform evidence; 18 h DTT treatment did not change AtaRca ATPase in one 2024 assay. Biochemistry, comparative mechanistic review Best treated as regulatory context on canonical RCA function, not a separate core molecular function; degree of redox control varies among species. (waheeda2023molecularmechanismof pages 3-4, waheeda2023molecularmechanismof pages 4-5, waheeda2023molecularmechanismof pages 5-7, chiu2024sisgrtheregulation pages 1-3)
MF Protein phosphorylation-responsive regulation Arabidopsis βRCA can be phosphorylated in vitro by chloroplast casein kinase 2, but available evidence indicates little or no effect on ATPase activity under the tested conditions. ~95% of AtbRca phosphorylated in vitro; major species mono-phosphorylated; phosphorylated AtbRca kcat 59.8 ± 0.7 min^-1, Km 139 ± 7 µM versus unphosphorylated kcat 60.3 ± 0.9 min^-1, Km 159 ± 9 µM. Biochemistry Supports PTM/regulation curation notes, but not a new core function or process annotation by itself. (chiu2024sisgrtheregulation pages 1-3)
BP Photosynthesis, light activation of Rubisco / regulation of carbon fixation RCA is required to maintain Rubisco in an activatable state during photosynthetic carbon assimilation and light-dependent photosynthetic induction. Arabidopsis rca loss causes severe defects in Rubisco activation and high-CO2-dependent growth with RuBP accumulation. Rubisco context: catalytic limitation is severe (2–10 CO2 fixed s^-1 per active site, review context). Genetics, physiology, biochemistry Strongest BP annotation area; central to Arabidopsis chloroplast carbon fixation. (stotz2012structureofgreen pages 41-44, waheeda2023molecularmechanismof pages 1-2)
BP Response to heat / heat acclimation of photosynthesis RCA is thermolabile relative to Rubisco and is a known bottleneck for photosynthetic performance at elevated temperature; engineering thermostable RCA variants improves plant performance. Arabidopsis triple-mutant RCAs increased thermostability by ~10°C; cross-species examples show large yield gains when thermostable RCA is introduced. Mutagenesis, physiology, engineering literature Heat-response/process annotations are justified as context-dependent roles affecting photosynthesis, but should be scoped as modulation of photosynthetic thermotolerance rather than a general heat-stress signaling factor. (waheeda2023molecularmechanismof pages 5-7, moore2024usingthegreen pages 25-29, stotz2012structureofgreen pages 41-44)
BP Regulation by light/redox state RCA activity is linked to chloroplast light status through stromal pH/Mg2+ changes and α-isoform redox control, coupling Rubisco activation to illumination. Reduced αRca favors ATP binding; no universal magnitude across species established in gathered evidence. Biochemistry, physiology Appropriate as regulatory context for photosynthetic activation; species-specific variability cautions against overgeneralization. (waheeda2023molecularmechanismof pages 3-4, waheeda2023molecularmechanismof pages 4-5, stotz2012structureofgreen pages 41-44)
CC Chloroplast stroma Direct proteomics evidence places Arabidopsis RCA (AT2G39730.1) in the plastid stroma, matching its established role in activating stromal Rubisco. Proteomics row quantified RCA with reported ratios 1.05 ± 0.07, 1.25 ± 0.09, 1.38 ± 0.14 in the chloroplast dataset. Proteomics Best-supported cellular component annotation for the active protein. (rutschow2008quantitativeproteomicsof pages 6-7, rutschow2008quantitativeproteomicsof media 65ae96bc)
CC Rubisco-containing soluble stromal complex / transient Rubisco-RCA assembly Active RCA functions through transient nucleotide-dependent oligomers and physical engagement with Rubisco rather than a stable constitutive complex. Dimer/tetramer/hexamer interconversion; ADP-bound exchange ~0.3 s^-1 at 8 µM; ATPγS slows exchange 2–3×. Structural biology, biophysics Complex annotations should be conservative; evidence supports transient functional assemblies more clearly than a stable named holo-complex. (waheeda2023molecularmechanismof pages 5-7, waheeda2023molecularmechanismof pages 4-5)
CC Thylakoid membrane association (conditional) RCA can reversibly associate with thylakoid membranes under moderate heat stress and/or depending on stromal pH and ATP, but this appears conditional rather than its primary steady-state location. No robust stoichiometric localization values in gathered evidence. Biochemistry, fractionation-style observations summarized in review/dissertation Use caution: suitable only if annotation framework allows condition-specific localization; not equivalent to integral thylakoid localization. (stotz2012structureofgreen pages 41-44)
CC Plastoglobule Current examined evidence does not strongly support RCA as a bona fide plastoglobule protein. Plastoglobule proteome work emphasized limited stromal contamination and specific PG proteins, but RCA was not directly documented in the reviewed excerpts. In Arabidopsis plastoglobules, total PG protein mass increased ~10–12-fold under high light and ~3-fold after prolonged darkness, providing stress context but not RCA-specific localization. Proteomics Plastoglobule annotation for RCA is higher risk unless supported by direct Arabidopsis localization/proteomics beyond the present evidence. (ytterberg2006proteinprofilingof pages 2-3)
BP/CC negative assessment Apoptotic process / developmental cell death / pyroptosis / inflammatory signaling / neuronal or synaptic roles No evidence in the gathered Arabidopsis/plant RCA literature supports roles in apoptosis-like programs, animal immune signaling, pyroptosis, neuronal biology, or synaptic remodeling. RCA is a chloroplast carbon-fixation chaperone. None. Absence of supporting evidence; biological plausibility assessment Such annotations would be over-extended and should be rejected for Arabidopsis RCA unless extraordinary direct evidence appears. (waheeda2023molecularmechanismof pages 1-2, rutschow2008quantitativeproteomicsof pages 6-7, stotz2012structureofgreen pages 41-44)
CC negative assessment Cytoplasm / cytosol / nucleus / signaling complexes Gathered evidence supports chloroplast targeting and stromal function, with only conditional thylakoid association; no direct support was found for active localization in cytosol, nucleus, or non-plastid signaling complexes. None. Proteomics, mechanistic review Non-plastid location annotations are high risk and likely erroneous for the mature active RCA protein. (waheeda2023molecularmechanismof pages 4-5, rutschow2008quantitativeproteomicsof pages 6-7, stotz2012structureofgreen pages 41-44)

Table: This table summarizes evidence most relevant to GO annotation review for Arabidopsis thaliana RCA, separating core supported functions and locations from context-dependent regulation and unsupported annotation areas.

Key quantitative findings supporting these judgments are summarized here:

Blockquote: This blockquote lists the most decision-relevant quantitative findings for Arabidopsis RCA and related chloroplast stress context. It is useful for separating core catalytic evidence from conditional regulatory or localization-associated observations during GO annotation review.

5.1 High-confidence (core) annotations

5.2 Medium-confidence, context-dependent annotations

5.3 High-risk / likely erroneous annotations to avoid

6. Key literature (prioritizing 2023–2024)

  1. Waheeda K, Kitchel H, Wang Q, Chiu P-L. Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling. Frontiers in Molecular Biosciences. Feb 2023. https://doi.org/10.3389/fmolb.2023.1125922 (waheeda2023molecularmechanismof pages 5-7)
  2. Chiu P-L. SISGR: The regulation of carbon fixation in plant and green algae: Rubisco activase and the origin of heat inactivation of CO2 assimilation. Oct 2024. https://doi.org/10.2172/2475380 (chiu2024sisgrtheregulation pages 1-3)
  3. Rutschow HL, et al. Quantitative proteomics of a chloroplast SRP54 sorting mutant and its genetic interactions with CLPC1 in Arabidopsis. Plant Physiology. Jul 2008. https://doi.org/10.1104/pp.108.124545 (rutschow2008quantitativeproteomicsof pages 6-7)
  4. Ytterberg AJ, Peltier J-B, van Wijk KJ. Protein profiling of plastoglobules in chloroplasts and chromoplasts. A surprising site for differential accumulation of metabolic enzymes. Plant Physiology. Feb 2006. https://doi.org/10.1104/pp.105.076083 (ytterberg2006proteinprofilingof pages 2-3)
  5. Stotz MM. Structure of green type Rubisco activase from Nicotiana tabacum. Dissertation. Jan 2012. https://doi.org/10.5282/edoc.14494 (contains synthesis of classic Arabidopsis RCA mutant physiology and mechanistic motifs) (stotz2012structureofgreen pages 41-44)

Evidence limitations

This report is constrained to the papers successfully retrieved in-tool; some highly relevant 2023–2024 primary papers and reviews (e.g., crop-focused Rubisco regulation reviews) were listed as unobtainable or not retrieved. Consequently, certain GO-relevant details (e.g., in vivo phosphorylation dynamics in Arabidopsis leaves, direct fluorescence localization to plastoglobules, or detailed photosynthetic induction kinetics) could not be exhaustively evaluated here and should be checked in additional primary literature if such annotations are under consideration.

References

  1. (waheeda2023molecularmechanismof pages 1-2): Kazi Waheeda, Heidi Kitchel, Quan Wang, and Po-Lin Chiu. Molecular mechanism of rubisco activase: dynamic assembly and rubisco remodeling. Frontiers in Molecular Biosciences, Feb 2023. URL: https://doi.org/10.3389/fmolb.2023.1125922, doi:10.3389/fmolb.2023.1125922. This article has 49 citations.

  2. (stotz2012structureofgreen pages 41-44): Mathias Michael Stotz. Structure of green type rubisco activase from nicotiana tabacum. Dissertation, Jan 2012. URL: https://doi.org/10.5282/edoc.14494, doi:10.5282/edoc.14494. This article has 1 citations.

  3. (waheeda2023molecularmechanismof pages 3-4): Kazi Waheeda, Heidi Kitchel, Quan Wang, and Po-Lin Chiu. Molecular mechanism of rubisco activase: dynamic assembly and rubisco remodeling. Frontiers in Molecular Biosciences, Feb 2023. URL: https://doi.org/10.3389/fmolb.2023.1125922, doi:10.3389/fmolb.2023.1125922. This article has 49 citations.

  4. (stotz2012structureofgreen pages 109-113): Mathias Michael Stotz. Structure of green type rubisco activase from nicotiana tabacum. Dissertation, Jan 2012. URL: https://doi.org/10.5282/edoc.14494, doi:10.5282/edoc.14494. This article has 1 citations.

  5. (waheeda2023molecularmechanismof pages 5-7): Kazi Waheeda, Heidi Kitchel, Quan Wang, and Po-Lin Chiu. Molecular mechanism of rubisco activase: dynamic assembly and rubisco remodeling. Frontiers in Molecular Biosciences, Feb 2023. URL: https://doi.org/10.3389/fmolb.2023.1125922, doi:10.3389/fmolb.2023.1125922. This article has 49 citations.

  6. (waheeda2023molecularmechanismof pages 4-5): Kazi Waheeda, Heidi Kitchel, Quan Wang, and Po-Lin Chiu. Molecular mechanism of rubisco activase: dynamic assembly and rubisco remodeling. Frontiers in Molecular Biosciences, Feb 2023. URL: https://doi.org/10.3389/fmolb.2023.1125922, doi:10.3389/fmolb.2023.1125922. This article has 49 citations.

  7. (rutschow2008quantitativeproteomicsof pages 6-7): Heidi L. Rutschow, A. Ytterberg, G. Friso, R. Nilsson, and K. V. van Wijk. Quantitative proteomics of a chloroplast srp54 sorting mutant and its genetic interactions with clpc1 in arabidopsis1[c][w][oa]. Plant Physiology, 148:156-175, Jul 2008. URL: https://doi.org/10.1104/pp.108.124545, doi:10.1104/pp.108.124545. This article has 110 citations and is from a highest quality peer-reviewed journal.

  8. (rutschow2008quantitativeproteomicsof media 65ae96bc): Heidi L. Rutschow, A. Ytterberg, G. Friso, R. Nilsson, and K. V. van Wijk. Quantitative proteomics of a chloroplast srp54 sorting mutant and its genetic interactions with clpc1 in arabidopsis1[c][w][oa]. Plant Physiology, 148:156-175, Jul 2008. URL: https://doi.org/10.1104/pp.108.124545, doi:10.1104/pp.108.124545. This article has 110 citations and is from a highest quality peer-reviewed journal.

  9. (ytterberg2006proteinprofilingof pages 2-3): A. Jimmy Ytterberg, Jean-Benoit Peltier, and Klaas J. van Wijk. Protein profiling of plastoglobules in chloroplasts and chromoplasts. a surprising site for differential accumulation of metabolic enzymes1[w]. Plant Physiology, 140:984-997, Feb 2006. URL: https://doi.org/10.1104/pp.105.076083, doi:10.1104/pp.105.076083. This article has 565 citations and is from a highest quality peer-reviewed journal.

  10. (waheeda2023molecularmechanismof pages 7-8): Kazi Waheeda, Heidi Kitchel, Quan Wang, and Po-Lin Chiu. Molecular mechanism of rubisco activase: dynamic assembly and rubisco remodeling. Frontiers in Molecular Biosciences, Feb 2023. URL: https://doi.org/10.3389/fmolb.2023.1125922, doi:10.3389/fmolb.2023.1125922. This article has 49 citations.

  11. (chiu2024sisgrtheregulation pages 1-3): Po-Lin Chiu. Sisgr: the regulation of carbon fixation in plant and green algae: rubisco activase and the origin of heat inactivation of co<sub>2</sub> assimilation. Unknown journal, Oct 2024. URL: https://doi.org/10.2172/2475380, doi:10.2172/2475380.

  12. (moore2024usingthegreen pages 25-29): RL Moore. Using the green alga, chlamydomonas reinhardtii, as a chassis to express non-green rubisco variants. Unknown journal, 2024.