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1. Full Text The FtsH Protease Heterocomplex in Arabidopsis: Dispensability of Type-B Protease Activity for Proper Chloroplast Development
by Yusuke Kato and Lingang Zhang and Masaru Fujimoto and Nobuhiro Tsutsumi and Wataru Sakamoto
The Plant Cell, ISSN 1040-4651, 11/2010, Volume 22, Issue 11, pp. 3710 - 3725
FtsH is an ATP-dependent metalioprotease present as a hexameric heterocomplex in thyiakoid membranes. Encoded in the Arabidopsis thaliana YELLOW VARIEGATED2... 
Phenotypes | Chloroplasts | Adenosine triphosphatases | Thylakoids | Complementation | Plants | Isomers | Chlorophylls | Plant cells | Seedlings | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | PLANT DEVELOPMENT | QUALITY-CONTROL | PLANT SCIENCES | CELL BIOLOGY | THYLAKOID MEMBRANES | PLASTID BIOGENESIS | ATP-DEPENDENT PROTEASE | LEAF VARIEGATION | YELLOW VARIEGATED2 | PHOTOSYSTEM-II REPAIR | CLP PROTEASE | Promoter Regions, Genetic | Arabidopsis Proteins - genetics | Arabidopsis - enzymology | Mutagenesis, Site-Directed | Chloroplasts - ultrastructure | Isoenzymes - genetics | Arabidopsis - cytology | Metalloproteases - genetics | Genetic Complementation Test | Metalloproteases - metabolism | Arabidopsis - genetics | Arabidopsis Proteins - metabolism | Thylakoids - ultrastructure | Plant Leaves - genetics | Plant Leaves - metabolism | Escherichia coli - genetics | Isoenzymes - metabolism | Plants, Genetically Modified | Escherichia coli - metabolism | Chloroplasts - physiology | Plant Leaves - anatomy & histology | Intracellular Membranes - metabolism | Arabidopsis thaliana | Physiological aspects | Research | Properties | Proteases | Index Medicus
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2. Full Text Structural switching of Staphylococcus aureus Clp protease: A key to understanding protease dynamics
by Zhang, Jie and Ye, Fei and Lan, Lefu and Jiang, Hualiang and Luo, Cheng and Yang, Cai-Guang
Journal of Biological Chemistry, ISSN 0021-9258, 10/2011, Volume 286, Issue 43, pp. 37590 - 37601
ATP-dependent Clp protease (ClpP) is an attractive new target for the development of anti-infective agents. The ClpP protease consists of two heptameric rings... 
MAXIMUM-LIKELIHOOD | ATP HYDROLYSIS | ANTIBIOTICS | DEPENDENT PROTEASES | ACTIVE-SITE | BIOCHEMISTRY & MOLECULAR BIOLOGY | COMPLEXES | ESCHERICHIA-COLI CLPP | N-TERMINUS | MODEL | STRESS TOLERANCE | Protein Structure, Tertiary | Endopeptidase Clp - chemistry | Staphylococcus aureus - enzymology | Structure-Activity Relationship | Bacterial Proteins - chemistry | Index Medicus | Protein Structure and Folding | Bacteria | Molecular Dynamics | Protein Structure | Protein Degradation | Protease
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3. Full Text Sequestration from Protease Adaptor Confers Differential Stability to Protease Substrate
by Yeom, Jinki and Wayne, Kyle J and Groisman, Eduardo A
Molecular Cell, ISSN 1097-2765, 04/2017, Volume 66, Issue 2, pp. 234 - 246.e5
According to the N-end rule, the N-terminal residue of a protein determines its stability. In bacteria, the adaptor ClpS mediates proteolysis by delivering... 
protease ClpAP | Salmonella | protease adaptor ClpS | PhoP | protein stability | MgtC | protease substrate specificity | ACIDIC PH | BACTERIAL SENSOR KINASE | SYSTEM PHOP-PHOQ | UBIQUITIN LIGASE | STRUCTURAL BASIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | SALMONELLA-TYPHIMURIUM | END RULE PATHWAY | VIRULENCE OPERON | REGULATORY SYSTEM | CELL BIOLOGY | Endopeptidase Clp - chemistry | Bacterial Proteins - chemistry | Half-Life | Substrate Specificity | Structure-Activity Relationship | Time Factors | Cation Transport Proteins - metabolism | Proteolysis | Cation Transport Proteins - genetics | Transcription, Genetic | Protein Interaction Domains and Motifs | Protein Stability | Salmonella typhimurium - enzymology | Binding, Competitive | Amino Acid Sequence | Salmonella typhimurium - genetics | Bacterial Proteins - genetics | Models, Molecular | Endopeptidase Clp - genetics | Endopeptidase Clp - metabolism | Protein Binding | Bacterial Proteins - metabolism | Mutation | Cation Transport Proteins - chemistry | Gene Expression Regulation, Bacterial | Medical colleges | Genetic transcription | Proteases | Blood proteins | Protein stability | Protease ClpAP | Protease substrate specificity | Protease adaptor ClpS
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4. Full Text Arginine phosphorylation marks proteins for degradation by a Clp protease
by Trentini, Débora Broch and Suskiewicz, Marcin Józef and Heuck, Alexander and Kurzbauer, Robert and Deszcz, Luiza and Mechtler, Karl and Clausen, Tim
Nature, ISSN 0028-0836, 2016, Volume 539, Issue 7627, pp. 48 - 53
Protein turnover is a tightly controlled process that is crucial for the removal of aberrant polypeptides and for cellular signalling. Whereas ubiquitin marks... 
GRAM-POSITIVE BACTERIA | HEAT | BACILLUS-SUBTILIS | PEPTIDE IDENTIFICATION | TYROSINE KINASE | MULTIDISCIPLINARY SCIENCES | STRESS-RESPONSE | UBIQUITIN-LIKE PROTEIN | QUALITY CONTROL | ADAPTER PROTEIN | CTSR | Protein Kinases - metabolism | Endopeptidase Clp - chemistry | Phosphorylation | Adenosine Triphosphatases - metabolism | Crystallography, X-Ray | Endopeptidase Clp - genetics | Bacillus subtilis - enzymology | Endopeptidase Clp - metabolism | Organophosphorus Compounds - metabolism | Arginine - analogs & derivatives | Proteolysis | Adenosine Triphosphatases - chemistry | Bacterial Proteins - metabolism | Adenosine Triphosphatases - genetics | Mutation | Binding Sites | Arginine - metabolism | Physiological aspects | Arginine | Observations | Proteases | Adenosine triphosphatase | Gram-positive bacteria | Kinases | Phosphatase | Protein folding | Index Medicus
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5. Full Text Temporal proteomics of inducible RNAi lines of Clp protease subunits identifies putative protease substrates
by Moreno, Juan C and Martínez-Jaime, Silvia and Schwartzmann, Joram and Karcher, Daniel and Tillich, Michael and Graf, Alexander and Bock, Ralph
Plant Physiology, ISSN 0032-0889, 02/2018, Volume 176, Issue 2, pp. 1485 - 1508
The Clp protease in the chloroplasts of plant cells is a large complex composed of at least 13 nucleus-encoded subunits and one plastid-encoded subunit, which... 
CAROTENOID BIOSYNTHESIS | N-END RULE | ARABIDOPSIS-THALIANA | NITROGEN STARVATION | CHLAMYDOMONAS-REINHARDTII | PLASTID GENE-EXPRESSION | ATP-DEPENDENT PROTEASE | ESCHERICHIA-COLI | CHLOROPLAST DEVELOPMENT | MOLECULAR CHAPERONE | PLANT SCIENCES | Substrate Specificity | Endopeptidase Clp - genetics | Proteome | Endopeptidase Clp - metabolism | Chloroplasts - metabolism | Plant Proteins - genetics | Phenotype | Cell Nucleus - metabolism | RNA Interference | Proteolysis | Tobacco - genetics | Proteomics | Plant Proteins - metabolism | Tobacco - enzymology | Physiological aspects | Botanical research | Substrates (Biochemistry) | Research | Proteases | Index Medicus
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6. Full Text The mechanism of caseinolytic protease (ClpP) inhibition
by Gersch, Malte and Gut, Felix and Korotkov, Vadim S and Lehmann, Johannes and Böttcher, Thomas and Rusch, Marion and Hedberg, Christian and Waldmann, Herbert and Klebe, Gerhard and Sieber, Stephan A
Angewandte Chemie - International Edition, ISSN 1433-7851, 2013, Volume 52, Issue 10, pp. 3009 - 3014
  Catch me if you can: The ClpP protease mediates protein homeostasis and can be efficiently inhibited by β-lactones. A combination of molecular docking,... 
ClpP | lactones | molecular docking | enzyme inhibitors | structure-activity relationship | NETWORK | ACTIVE-SITE | ESCHERICHIA-COLI | structureactivity relationship | TERMINAL ALKYNES | BACTERIAL | POTENT INHIBITORS | CHEMISTRY, MULTIDISCIPLINARY | VIRULENCE FACTORS | BETA-LACTONES | TARGETS | STAPHYLOCOCCUS-AUREUS | Models, Molecular | Protease Inhibitors - chemistry | Protease Inhibitors - pharmacology | Enzyme Activation - drug effects | Endopeptidase Clp - antagonists & inhibitors | Humans | Proteases | Enzyme inhibitors | Lactones | Index Medicus | Proteins | Binding | Residues | Profiling | Protease | Pocket | Inhibition | Aliphatic compounds
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7. Full Text Subunits of the Plastid ClpPR Protease Complex Have Differential Contributions to Embryogenesis, Plastid Biogenesis, and Plant Development in Arabidopsis
by Kim, J and Rudella, A and Rodriguez, VR and Zybailov, B and Olinares, PDB and van Wijk, KJ
PLANT CELL, ISSN 1040-4651, 06/2009, Volume 21, Issue 6, pp. 1669 - 1692
The plastid ClpPR protease complex in Arabidopsis thaliana consists of five catalytic ClpP and four noncatalytic ClpR subunits. An extensive analysis of the... 
SHOTGUN PROTEOMICS | BIOCHEMISTRY & MOLECULAR BIOLOGY | BINDING PROTEIN | PLANT SCIENCES | CELL BIOLOGY | EMBRYO DEVELOPMENT | GENE | CHLAMYDOMONAS-REINHARDTII | THALIANA | CHLOROPLAST DEVELOPMENT | IN-VIVO | MOLECULAR CHAPERONE | EXPRESSION | Chloroplasts - enzymology | Arabidopsis - enzymology | Arabidopsis - growth & development | Seeds - enzymology | RNA, Messenger - metabolism | Genetic Complementation Test | Plant Extracts - metabolism | Seeds - growth & development | Protein Subunits - physiology | Endopeptidase Clp - physiology | Plant Leaves - enzymology | Protein Subunits - genetics | Microscopy, Electron, Transmission | Arabidopsis Proteins - genetics | Arabidopsis Proteins - physiology | Chloroplasts - ultrastructure | Seeds - ultrastructure | Gene Silencing | Endopeptidase Clp - genetics | Reverse Transcriptase Polymerase Chain Reaction | Chloroplasts - metabolism | Arabidopsis - genetics | Plastids - enzymology | Phenotype | Proteomics | Mutation | Plant Leaves - ultrastructure | Arabidopsis thaliana | Proteases | Plant molecular genetics | Physiological aspects | Plant embryology | Genetic aspects | Research | Chemical properties | Genetic regulation | Plastids | Index Medicus
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8. Full Text Inhibition of the Mitochondrial Protease ClpP as a Therapeutic Strategy for Human Acute Myeloid Leukemia
by Cole, Alicia and Wang, Xiaoming and Wang, Jean C.Y and Wang, Zezhou and Coyaud, Etienne and Voisin, Veronique and Gronda, Marcela and Jitkova, Yulia and Mattson, Rachel and Hurren, Rose and Babovic, Sonja and Maclean, Neil and Restall, Ian and Jeyaraju, Danny V and Sukhai, Mahadeo A and Prabha, Swayam and Bashir, Shaheena and Ramakrishnan, Ashwin and Leung, Elisa and Qia, Yi Hua and Zhang, Nianxian and Combes, Kevin R and Ketela, Troy and Lin, Fengshu and Houry, Walid A and Aman, Ahmed and Al-awar, Rima and Zheng, Wei and Wienholds, Erno and Xu, Chang Jiang and Dick, John and Moffat, Jason and Minden, Mark D and Eaves, Connie J and Bader, Gary D and Hao, Zhenyue and Kornblau, Steven M and Raught, Brian and Schimmer, Aaron D
Cancer Cell, ISSN 1535-6108, 06/2015, Volume 27, Issue 6, pp. 864 - 876
From an shRNA screen, we identified ClpP as a member of the mitochondrial proteome whose knockdown reduced the viability of K562 leukemic cells. Expression of... 
ADVERSE PROGNOSTIC-FACTOR | CARFILZOMIB | ONCOLOGY | TARGETS | BORTEZOMIB | EXPRESSION | HUMAN HOMOLOG | SOFTWARE | CELL BIOLOGY | RNA, Small Interfering - genetics | Humans | Enzyme Inhibitors - pharmacology | Male | Endopeptidase Clp - metabolism | Mice, SCID | Endopeptidase Clp - antagonists & inhibitors | Mice, Knockout | Leukemia, Myeloid, Acute - enzymology | Animals | Heterografts | Leukemia, Myeloid, Acute - drug therapy | Mice | Physiological aspects | Drug discovery | Molecular genetics | Proteases | Health aspects | Index Medicus
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9. Full Text Assembly of the Chloroplast ATP-Dependent Clp Protease in Arabidopsis Is Regulated by the ClpT Accessory Proteins
by Lars L.E. Sjögren and Adrian K. Clarke and Naturvetenskapliga fakulteten and Faculty of Sciences and Göteborgs universitet and Gothenburg University and Department of Plant and Environmental Sciences and Institutionen för växt- och miljövetenskaper
The Plant Cell, ISSN 1040-4651, 1/2011, Volume 23, Issue 1, pp. 322 - 332
The ATP-dependent caseinolytic protease (CIp) is an essential housekeeping enzyme in plant chloroplasts. It is by far the most complex of all known CIp... 
Proteins | Oligomers | Chloroplasts | Antibodies | Immunoblotting | Dimers | Plants | Physiological regulation | Monomers | Plant cells | TRANSLOCATION | COMPLEX | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | PLANT DEVELOPMENT | PROTEOLYSIS | PLANT SCIENCES | CELL BIOLOGY | GENE | BIOGENESIS | THALIANA | MOLECULAR CHAPERONE | SUBUNIT | Arabidopsis - genetics | Arabidopsis Proteins - metabolism | Arabidopsis Proteins - genetics | Chloroplasts - enzymology | Arabidopsis - enzymology | Gene Expression Regulation, Plant | Endopeptidase Clp - genetics | Endopeptidase Clp - metabolism | Mutagenesis, Insertional | Mutation | Arabidopsis thaliana | Physiological aspects | Genetic aspects | Research | Plant physiology | Plant genetics | Index Medicus | Biological Sciences | Biologiska vetenskaper
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10. Full Text Loss of mitochondrial protease ClpP protects mice from diet‐induced obesity and insulin resistance
by Bhaskaran, Shylesh and Pharaoh, Gavin and Ranjit, Rojina and Murphy, Ashley and Matsuzaki, Satoshi and Nair, Binoj C and Forbes, Brittany and Gispert, Suzana and Auburger, Georg and Humphries, Kenneth M and Kinter, Michael and Griffin, Timothy M and Deepa, Sathyaseelan S
EMBO reports, ISSN 1469-221X, 03/2018, Volume 19, Issue 3, pp. e45009 - n/a
Caseinolytic peptidase P (ClpP) is a mammalian quality control protease that is proposed to play an important role in the initiation of the mitochondrial... 
adipose tissue | insulin sensitivity | mitochondria | caseinolytic peptidase P | obesity | PGC-1-ALPHA | BIOCHEMISTRY & MOLECULAR BIOLOGY | UNCOUPLING PROTEIN-2 UCP2 | SENSITIVITY | QUALITY CONTROL | MUSCLE-CELLS | CELL BIOLOGY | WHITE ADIPOSE-TISSUE | OPA1 | GENE-EXPRESSION | FAT | DYSFUNCTION | Fatty Liver - genetics | Adipose Tissue, White - pathology | Fatty Liver - metabolism | Unfolded Protein Response - genetics | Fatty Liver - pathology | Adipose Tissue, White - metabolism | Diet, High-Fat - adverse effects | Endopeptidase Clp - genetics | Mitochondria - metabolism | Obesity - genetics | Mice, Knockout | Obesity - metabolism | Obesity - pathology | Animals | Mitochondria - genetics | Insulin Resistance - genetics | Mice | Energy Metabolism - genetics | Adipose tissue | Liver | Proteinase | Homeostasis | Biosynthesis | Glucose | High fat diet | Proteins | Mitochondria | Fatty liver | Protein folding | Protease | Rodents | Obesity | Peptidase | Markers | Energy expenditure | Mammals | Metabolism | Retrograde transport | Insulin | Steatosis | Glucose tolerance | Intolerance | Signaling | Sensitivity | Diet | Quality control | Insulin resistance | Electron transport | Metabolic disorders | Index Medicus | Post-translational Modifications, Proteolysis & Proteomics
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11. Full Text Regulation of Escherichia coli starvation sigma factor (sigma s) by ClpXP protease
by T Schweder and K H Lee and O Lomovskaya and A Matin
Journal of Bacteriology, ISSN 0021-9193, 01/1996, Volume 178, Issue 2, pp. 470 - 476
Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
STATIONARY-PHASE | BACTERIA | CARBON-STARVATION | DEPENDENT PROTEASES | TRANSCRIPTION | SEQUENCE | DEGRADATION | MICROBIOLOGY | KATF | PROTEINS | GENE-PRODUCT | Sigma Factor - metabolism | Endopeptidase Clp | Serine Endopeptidases - physiology | Molecular Sequence Data | Heat-Shock Proteins - genetics | Base Sequence | Serine Endopeptidases - genetics | Nuclear Proteins - genetics | Sigma Factor - genetics | Escherichia coli - physiology | ATP-Dependent Proteases | Protease La | Recombinant Fusion Proteins - biosynthesis | ATPases Associated with Diverse Cellular Activities | Molecular Chaperones | Escherichia coli - enzymology | Bacterial Proteins - genetics | DNA-Binding Proteins - genetics | Gene Expression Regulation, Bacterial - physiology | Escherichia coli Proteins | beta-Galactosidase - biosynthesis | Escherichia coli - genetics | Bacterial Proteins - metabolism | Sigma Factor - biosynthesis | Adenosine Triphosphatases - genetics | Bacterial Proteins - biosynthesis | Mutation | beta-Galactosidase - genetics | Heat-Shock Proteins - physiology | Adenosine Triphosphatases - physiology | Physiological aspects | Microbial enzymes | Research | Biological control systems | Proteases | Escherichia coli | Bacteria | Cellular biology | Genes | Bacteriology | Index Medicus
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12. Full Text A conformational switch underlies ClpP protease function
by Geiger, Sebastian R and Böttcher, Thomas and Sieber, Stephan A and Cramer, Patrick
Angewandte Chemie - International Edition, ISSN 1433-7851, 06/2011, Volume 50, Issue 25, pp. 5749 - 5752
protein structures | ClpP heat shock protein | virulence regulation | conformational switch | protease complex | RECOGNITION | PROTEOLYSIS | CHEMISTRY, MULTIDISCIPLINARY | Catalytic Domain | Endopeptidase Clp - chemistry | Staphylococcus aureus - enzymology | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Substrate Specificity | Bacterial Proteins - metabolism | Endopeptidase Clp - genetics | Endopeptidase Clp - metabolism | Kinetics | Mutation | Index Medicus
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13. Full Text Control of plastidial metabolism by the Clp protease complex
by Rodriguez-Concepcion, Manuel and D'Andrea, Lucio and Pulido, Pablo
Journal of Experimental Botany, ISSN 0022-0957, 04/2019, Volume 70, Issue 7, pp. 2049 - 2058
The Clp protease complex, the main stromal protease, acts in coordination with nuclear-encoded plastidial chaperones for the control of client enzyme levels... 
SYSTEM | Clp protease | CHLOROPHYLL BIOSYNTHESIS | chlorophyll | proteostasis | PLANT SCIENCES | tetrapyrrole | unfolded protein response | METHYLERYTHRITOL PHOSPHATE | chaperone | chloroplast | PATHWAY | MOLECULAR CHAPERONE | FUNCTIONAL-ANALYSIS | ARABIDOPSIS | ACCUMULATION | PROTEINS | Carotenoid | PHYTOENE SYNTHASE | chromoplasts | isoprenoid
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14. Full Text β-lactam resistance in methicillin-resistant Staphylococcus aureus USA300 is increased by inactivation of the ClpXP protease
by Bæk, Kristoffer T and Gründling, Angelika and Mogensen, René G and Thøgersen, Louise and Petersen, Andreas and Paulander, Wilhelm and Frees, Dorte
Antimicrobial Agents and Chemotherapy, ISSN 0066-4804, 2014, Volume 58, Issue 8, pp. 4593 - 4603
Methicillin-resistant Staphylococcus aureus (MRSA) has acquired the mecA gene encoding a peptidoglycan transpeptidase, penicillin binding protein 2a (PBP2a),... 
STRAINS | ANTIBIOTICS | CELL-WALL | PEPTIDOGLYCAN CROSS-LINKING | WALL TEICHOIC-ACID | MRSA | SUSCEPTIBILITY | PENICILLIN-BINDING PROTEINS | MICROBIOLOGY | PHARMACOLOGY & PHARMACY | STRESS TOLERANCE | VIRULENCE | Endopeptidase Clp - deficiency | Peptidoglycan - metabolism | Isoenzymes - genetics | Methicillin-Resistant Staphylococcus aureus - drug effects | Cell Wall - genetics | Endopeptidase Clp - genetics | Cell Wall - enzymology | Isoenzymes - deficiency | N-Acetylmuramoyl-L-alanine Amidase - genetics | Bacterial Proteins | N-Acetylmuramoyl-L-alanine Amidase - metabolism | Penicillin-Binding Proteins | Metabolic Networks and Pathways - genetics | beta-Lactams - pharmacology | Cell Wall - drug effects | Anti-Bacterial Agents - pharmacology | beta-Lactam Resistance - genetics | Mutation | Gene Expression Regulation, Bacterial | Methicillin-Resistant Staphylococcus aureus - enzymology | Methicillin-Resistant Staphylococcus aureus - genetics | Index Medicus | Mechanisms of Resistance
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15. Full Text ClpS1 Is a Conserved Substrate Selector for the Chloroplast Clp Protease System in Arabidopsis
by Kenji Nishimura and Yukari Asakura and Giulia Friso and Jitae Kim and Soo-hyun Oh and Heidi Rutschow and Lalit Ponnala and Klaas J. van Wijk
The Plant Cell, ISSN 1040-4651, 6/2013, Volume 25, Issue 6, pp. 2276 - 2301
Whereas the plastid caseinolytic peptidase (Clp) P protease system is essential for plant development, substrates and substrate selection mechanisms are... 
Proteins | Datasets | Phenotypes | Protein metabolism | Chloroplasts | RESEARCH ARTICLES | Plants | Proteomes | Plastids | Chlorophylls | Plant cells | FUNCTIONAL IMPLICATIONS | PROCESSING PEPTIDASE | SHOTGUN PROTEOMICS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | PLANT SCIENCES | CELL BIOLOGY | AAA+ PROTEASES | TRANSFER-RNA REDUCTASE | IN-VIVO | MOLECULAR CHAPERONE | SALMONELLA-TYPHIMURIUM | END RULE PATHWAY | Molecular Chaperones - metabolism | Molecular Sequence Data | Substrate Specificity | Phylogeny | Isoenzymes - classification | Arabidopsis Proteins - metabolism | Isoenzymes - metabolism | Endopeptidase Clp - classification | Plants, Genetically Modified | Chloroplasts - genetics | Amino Acid Sequence | Arabidopsis Proteins - genetics | Isoenzymes - genetics | Electrophoresis, Polyacrylamide Gel | Molecular Chaperones - genetics | Endopeptidase Clp - genetics | Endopeptidase Clp - metabolism | Blotting, Western | Chloroplasts - metabolism | Arabidopsis - metabolism | Protein Interaction Mapping | Arabidopsis - genetics | Sequence Homology, Amino Acid | Protein Binding | Models, Genetic | Mutation | Arabidopsis Proteins - classification | Arabidopsis thaliana | Physiological aspects | Proteases | Index Medicus
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