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photosystem ii (6) 6
biochemistry & molecular biology (5) 5
crystal-structure (4) 4
psby (4) 4
psby protein (4) 4
thylakoid membrane (4) 4
amino acid sequence (3) 3
bacterial proteins - genetics (3) 3
biochemistry and molecular biology (3) 3
biokemi och molekylärbiologi (3) 3
biological sciences (3) 3
biologiska vetenskaper (3) 3
biophysics (3) 3
cell biology (3) 3
chlorophyll (3) 3
dimerization (3) 3
index medicus (3) 3
molecular sequence data (3) 3
mutagenesis (3) 3
natural sciences (3) 3
naturvetenskap (3) 3
photosynthesis (3) 3
photosystem ii protein complex - genetics (3) 3
arabidopsis (2) 2
bacteria (2) 2
bacterial proteins - metabolism (2) 2
binding (2) 2
biochemistry (2) 2
calcium (2) 2
complexes (2) 2
cyanobacteria (2) 2
cytochrome b (2) 2
cytochrome b559 (2) 2
genetics & heredity (2) 2
membrane proteins (2) 2
molecular weight (2) 2
peptides (2) 2
photosystem ii protein complex - metabolism (2) 2
plant physiology (2) 2
plant proteins (2) 2
plant sciences (2) 2
plants (2) 2
polypeptides (2) 2
resolution (2) 2
sequence analysis (2) 2
thylakoid membrane-proteins (2) 2
ureohydrolases - genetics (2) 2
ureohydrolases - metabolism (2) 2
12-kda protein (1) 1
abbreviations psb photosystem (1) 1
abscisic acid (1) 1
acceptor-side (1) 1
acclimation (1) 1
acclimatization (1) 1
acid production (1) 1
adaptation physiologique (1) 1
adaptation, physiological (1) 1
age (1) 1
algae (1) 1
alternative oxidase (1) 1
analysis (1) 1
angstrom resolution (1) 1
arabidopsis - genetics (1) 1
arabidopsis proteins (1) 1
arabidopsis thaliana (1) 1
arabidopsis-thaliana (1) 1
architecture (1) 1
arginine - metabolism (1) 1
autotetraploid (1) 1
bacterial proteins - chemistry (1) 1
base sequence (1) 1
binding affinity (1) 1
biochemistry, general (1) 1
biodegradation (1) 1
bioinformatics (1) 1
biological transport (1) 1
biology and life sciences (1) 1
botany (1) 1
brassica (1) 1
brassicaceae - genetics (1) 1
breeding (1) 1
calcium - metabolism (1) 1
calcium channels (1) 1
calcium signalling (1) 1
cbb (1) 1
cdna clones (1) 1
cell compartmentation (1) 1
cell culture (1) 1
cell nucleus - genetics (1) 1
cell processes (1) 1
cellular stress responses (1) 1
center core complex (1) 1
centrality (1) 1
chl (1) 1
chl chlorophyll (1) 1
chloroplast (1) 1
chloroplasts (1) 1
citrus (1) 1
citrus - genetics (1) 1
citrus - growth & development (1) 1
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1. Full Text The PsbY protein of Arabidopsis Photosystem II is important for the redox control of cytochrome b559
by von Sydow, Lotta and Schwenkert, Serena and Meurer, Jörg and Funk, Christiane and Mamedov, Fikret and Schröder, Wolfgang P and Umeå universitet and Teknisk-naturvetenskapliga fakulteten and Kemiska institutionen
BBA - Bioenergetics, ISSN 0005-2728, 09/2016, Volume 1857, Issue 9, pp. 1524 - 1533
Photosystem II is a protein complex embedded in the thylakoid membrane of photosynthetic organisms and performs the light driven water oxidation into electrons... 
Thylakoid membrane | Photosystem II | Cytochrome b559 | PsbY protein | TMH trans-membrane helix | Cytb | Abbreviations Psb photosystem | PsbYcom rescue plants complemented with the WT PsbY gene | Chl chlorophyll | cytochrome b | Biological Sciences | Naturvetenskap | Biokemi och molekylärbiologi | Biologiska vetenskaper | Biochemistry and Molecular Biology | Natural Sciences
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2. Full Text The PsbY protein of Arabidopsis Photosystem II is important for the redox control of cytochrome b(559)
by von Sydow, L and Schwenkert, S and Meurer, J and Funk, C and Mamedov, F and Schroder, WP and Teknisk-naturvetenskapliga vetenskapsområdet and Molekylär biomimetik and Institutionen för kemi - Ångström and Uppsala universitet and Kemiska sektionen
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, ISSN 0005-2728, 09/2016, Volume 1857, Issue 9, pp. 1524 - 1533
Photosystem II is a protein complex embedded in the thylalcoid membrane of photosynthetic organisms and performs the light driven water oxidation into... 
COMPLEX | MUTAGENESIS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RESOLUTION | Thylakoid membrane | WATER OXIDATION | Photosystem II | HIGH-POTENTIAL FORM | THYLAKOID MEMBRANE-PROTEINS | ACCEPTOR-SIDE | Cytochrome b | ELECTRON-TRANSFER | BIOPHYSICS | BINDING | PsbY protein | Biological Sciences | Naturvetenskap | Biokemi och molekylärbiologi | Biologiska vetenskaper | Biochemistry and Molecular Biology | Natural Sciences
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3. Full Text Location of PsbY in oxygen-evolving photosystem II revealed by mutagenesis and X-ray crystallography
by Kawakami, Keisuke and Iwai, Masako and Ikeuchi, Masahiko and Kamiya, Nobuo and Shen, Jian-Ren
FEBS Letters, ISSN 0014-5793, 2007, Volume 581, Issue 25, pp. 4983 - 4987
PsbY is one of the low molecular mass subunits of oxygen-evolving photosystem II (PSII). Its location, however, has not been identified in the current crystal... 
Photosystem II | PsbY | Mutant | Crystallization | Crystal structure | Membrane proteins | CBB | low molecular mass subunits | SDS | Chl | PSII | chlorophyll | Coomassie brilliant blue | PAGE | LMM | n-dodecyl-β-d-maltoside | photosystem II | polyacrylamide gel electrophoresis | sodium dodecyl sulfate | PCC-6803 | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RESOLUTION | COMPLEXES | COMPONENTS | THERMOSYNECHOCOCCUS-VULCANUS | CELL BIOLOGY | 12-KDA PROTEIN | membrane proteins | BIOPHYSICS | SYNECHOCOCCUS-VULCANUS | crystal structure | crystallization | THYLAKOID MEMBRANE | mutant | BINDING | Mutagenesis | Photosystem II Protein Complex - chemistry | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Cyanobacteria | Photosystem II Protein Complex - genetics | Models, Molecular | Crystallography, X-Ray | Protein Subunits - chemistry | Dimerization | Protein Subunits - genetics | Structure | Chlorophyll | Crystals
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4. Full Text Different adaptation strategies of two citrus scion/rootstock combinations in response to drought stress
by De Souza, Joadson Dutra and De Andrade Silva, Edson Mario and Filho, Mauricio Antönio Coelho and Morillon, Raphaél and Bonatto, Diego and Micheli, Fabienne and Da Silva Gesteira, Abelmon
PLoS ONE, ISSN 1932-6203, 05/2017, Volume 12, Issue 5, p. e0177993
Scion/rootstock interaction is important for plant development and for breeding programs. In this context, polyploid rootstocks presented several advantages,... 
HISTONE ACETYLTRANSFERASES | ALTERNATIVE OXIDASE | PSBY PROTEIN | CRYSTAL-STRUCTURE | TOLERANCE | MULTIDISCIPLINARY SCIENCES | RANGPUR LIME | ARABIDOPSIS | PHOTOSYSTEM-I | ELECTRON-TRANSPORT | SUBUNIT | Adaptation, Physiological | Polyploidy | Plant Roots - metabolism | Plant Roots - genetics | Gene Expression Profiling | Protein Interaction Maps | Plant Proteins - genetics | Citrus - growth & development | Citrus - metabolism | Citrus - genetics | Droughts | Gene Expression Regulation, Plant | Plant Proteins - metabolism | Plant Roots - growth & development | Citrus | Citrus fruits | Research | Analysis | Competition | Cell culture | Regulators | Multiplication | Defensive behavior | Biochemistry | Hormones | Polyamines | Proteins | Degradation | Transpiration | Signal transduction | Botany | Autotetraploid | Abscisic acid | Physiology | Pollen | Sensors | Inhibition | Drought | Bioinformatics | Enzymes | Chlorophyll | Breeding | Exposure | Plants | Metabolism | Gene expression | Acclimation | Flavonoids | Conductance | Photosynthesis | Irrigation | Senescence | Calcium | Homeostasis | Alternative oxidase | Calcium signalling | Leaves | Engineering | Lime | Metabolites | Ion channels | Plant sciences | Genotypes | Age | Cultivars | Biodegradation | Calcium channels | Corn | Acclimatization | Acid production | Plant stress | Respiration
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5. Full Text Evidence for a stable association of Psb30 (Ycf12) with photosystem II core complex in the cyanobacterium Synechocystis sp. PCC 6803
by Inoue-Kashino, Natsuko and Takahashi, Takeshi and Ban, Akiko and Sugiura, Miwa and Takahashi, Yuichiro and Satoh, Kazuhiko and Kashino, Yasuhiro
Photosynthesis Research, ISSN 0166-8595, 10/2008, Volume 98, Issue 1, pp. 323 - 335
Ycf12 (Psb30) is a small hydrophobic subunit of photosystem II (PS II) complexes found in the cyanobacterium, Thermosynechococcus elongatus. However, earlier... 
Life Sciences | Biochemistry, general | Low-molecular-weight polypeptide | Psb30 | Synechocystis 6803 | Ycf12 | Plant Physiology | Photosystem II | PsbY | Plant Sciences | Plant Genetics & Genomics | MUTAGENESIS | CRYSTAL-STRUCTURE | SP PCC-6803 | POLYPEPTIDES | SYNECHOCOCCUS-ELONGATUS | PLANT SCIENCES | MOLECULAR-MASS PROTEINS | ANGSTROM RESOLUTION | THERMOSYNECHOCOCCUS-ELONGATUS | GENE | ARCHITECTURE | Amino Acid Sequence | Phenotype | Sequence Alignment | Gene Deletion | Bacterial Proteins - genetics | Gene Silencing | Photosystem II Protein Complex - genetics | Molecular Sequence Data | Bacterial Proteins - metabolism | Synechocystis - genetics | Photosystem II Protein Complex - metabolism | Synechocystis - metabolism | Chlorophyll | Bacteria | Peptides | Photosynthesis | Molecular weight | Proteomics
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6. The PsbY Protein Is Not Essential for Oxygenic Photosynthesis in the Cyanobacterium Synechocystis sp. PCC 6803
by Meetam, M and Keren, N and Ohad, I and Pakrasi, HB
Plant Physiology, ISSN 0032-0889, 12/1999, Volume 121, Issue 4, pp. 1267 - 1272
A tetra-manganese cluster in the photosystem II (PSII) pigment-protein complex plays a critical role in the photosynthetic oxygen evolution process. PsbY, a... 
PsbY protein
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7. Full Text On the functional significance of the polypeptide PsbY for photosynthetic water oxidation in the cyanobacterium Synechocystis sp. strain PCC 6803
by Neufeld, S and Zinchenko, V and Stephan, D P and Bader, K P and Pistorius, E K
Molecular Genetics and Genomics, ISSN 1617-4615, 5/2004, Volume 271, Issue 4, pp. 458 - 467
Recent investigations have revealed that the cyanobacterial photosystem II complex contains more than 26 polypeptides. The functions of most of the... 
Photosystem II | Synechocystis sp. strain PCC 6803 | Calcium | LifeSciences | PsbY | PsbO | MANGANESE CLUSTER | calcium | STABILIZING PROTEIN | PCC6803 | EXTRINSIC POLYPEPTIDES | BIOCHEMISTRY & MOLECULAR BIOLOGY | MUTANTS LACKING | DELETION | photosystem II | PHOTOSYSTEM-II PREPARATION | EVOLUTION | VULCANUS | GENETICS & HEREDITY | STATE TRANSITIONS | Synechocystis sp strain PCC 6803 | Cyanobacteria - genetics | Oxidation-Reduction | Calcium - metabolism | Bacterial Proteins - genetics | Cyanobacteria - metabolism | Cyanobacteria - growth & development | Oxygen - metabolism | Photosystem II Protein Complex - metabolism | Membrane Proteins | Ureohydrolases - genetics | Photosynthesis - genetics | Light | Photosystem II Protein Complex - genetics | Water - chemistry | Photosystem II Protein Complex - isolation & purification | Bacterial Proteins - metabolism | Ureohydrolases - metabolism | Bacteria | Genes | Polypeptides
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8. Full Text The low molecular mass subunits of the photosynthetic supracomplex, photosystem II
by Shi, Lan-Xin and Schröder, Wolfgang P and Institutionen för kemi, biologi, geografi och miljövetenskap and Södertörns högskola
2004, Volume 1608, Issue 2, 22
The photosystem II (PSII) complex is located in the thylakoid membrane of higher plants, algae and cyanobacteria and drives the water oxidation process of... 
Small protein | Function | Synechocystis | Arabidopsis | PS2 | ARABIDOPSIS-THALIANA | LIGHT-HARVESTING ANTENNA | CENTER CORE COMPLEX | BIOCHEMISTRY & MOLECULAR BIOLOGY | SYNECHOCYSTIS SP PCC-6803 | REACTION-CENTER COMPLEX | THYLAKOID MEMBRANE-PROTEINS | OPEN READING FRAMES | PSII-H SUBUNIT | BIOPHYSICS | CYANOBACTERIUM SYNECHOCOCCUS-ELONGATUS | small protein | function | SEC-INDEPENDENT INSERTION | protein subunit | deletion mutant | Photosystem II Protein Complex | Peptides | structure analysis | protein function | cytochrome b559 | Crystallography | protein structure | Chloroplasts | Eukaryota | photosynthesis | Phosphoproteins | review | protein | Cyanobacteria | Biochemistry and Molecular Biology | eukaryote | Biological Sciences | Amino Acid Sequence | protein analysis | protein assembly | protein localization | mutation | protein psbtc | Naturvetenskap | genetic analysis | sequence homology | Embryophyta | nonhuman | protein psbtn | binding affinity | unclassified drug | comparative study | protein psbz | protein PsbJ | protein PsbL | Molecular Sequence Data | algae | protein psbr | protein psby | protein psbx | protein psbw | genetic code | protein psbm | protein psbk | chloroplast | protein psbn | protein psbe | sequence analysis | Natural Sciences | priority journal | protein psbi | protein psbh | dimerization | molecular weight | prokaryote | protein binding | protein stability | Biokemi och molekylärbiologi | Biologiska vetenskaper | membrane protein | Plant Proteins | Prokaryota
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9. Full Text PsbY, a novel manganese-binding, low-molecular-mass protein associated with photosystem II
by Gau, A. E and Thole, H. H and Sokolenko, A and Altschmied, L and Herrmann, R. G and Pistorius, E. K
MGG - Molecular and General Genetics, ISSN 0026-8925, 10/1998, Volume 260, Issue 1, pp. 56 - 68
We describe two related manganese-binding polypeptides with L-arginine metabolizing enzyme activity that can be detected as distinct components (designated... 
Topogenesis | Photosystem II | Gene duplication | PsbY | Polyprotein | L-Arginine metabolizing enzyme | L-arginine metabolizing enzyme | BIOCHEMISTRY & MOLECULAR BIOLOGY | COMPLEXES | topogenesis | photosystem II | CDNA CLONES | TRANSPORT | OXYGEN EVOLUTION | gene duplication | SPINACH | SEQUENCE | GENETICS & HEREDITY | DYNAMICS | PLANTS | THYLAKOID MEMBRANE | polyprotein | POLYPEPTIDE | Ureohydrolases - isolation & purification | DNA, Complementary - genetics | Molecular Sequence Data | Cell Compartmentation | Ureohydrolases - genetics | Arabidopsis Proteins | Biological Transport | Spinacia oleracea - genetics | Base Sequence | Ureohydrolases - metabolism | Membrane Proteins - metabolism | Dimerization | Amino Acid Sequence | Membrane Proteins - isolation & purification | Gene Library | Membrane Proteins - genetics | Gene Dosage | Protein Precursors - metabolism | Arabidopsis - genetics | Brassicaceae - genetics | Sequence Homology, Amino Acid | Manganese - metabolism | Cell Nucleus - genetics | Plant Proteins | Protein Processing, Post-Translational | Sequence Analysis | Arginine - metabolism | Evolution, Molecular
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