scholarly article | Q13442814 |
P50 | author | Hou-Fu Guo | Q55240722 |
P2093 | author name string | Craig W Vander Kooi | |
David A Meekins | |||
Hou-Fu Guo | |||
Matthew S Gentry | |||
Bradley C Paasch | |||
Diana Santelia | |||
Oliver Kötting | |||
Satrio Husodo | |||
Travis M Bridges | |||
P2860 | cites work | A novel protein tyrosine phosphatase gene is mutated in progressive myoclonus epilepsy of the Lafora type (EPM2) | Q22001499 |
Glycogen and its Metabolism | Q22305786 | ||
The catalytic role of Cys124 in the dual specificity phosphatase VHR | Q24337058 | ||
The starch-related R1 protein is an alpha -glucan, water dikinase | Q24531406 | ||
Molecular basis for substrate recognition by MTMR2, a myotubularin family phosphoinositide phosphatase | Q24538782 | ||
The Arabidopsis sex1 mutant is defective in the R1 protein, a general regulator of starch degradation in plants, and not in the chloroplast hexose transporter | Q24543516 | ||
Identification of a novel enzyme required for starch metabolism in Arabidopsis leaves. The phosphoglucan, water dikinase | Q24556653 | ||
PHENIX: a comprehensive Python-based system for macromolecular structure solution | Q24654617 | ||
The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics | Q24655377 | ||
MolProbity: all-atom contacts and structure validation for proteins and nucleic acids | Q24684673 | ||
Processing of X-ray diffraction data collected in oscillation mode | Q26778468 | ||
Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaccharides | Q27641973 | ||
Crystal structure of human slingshot phosphatase 2 | Q27644410 | ||
The 'pair of sugar tongs' site on the non-catalytic domain C of barley alpha-amylase participates in substrate binding and activity | Q27647824 | ||
SusG: a unique cell-membrane-associated alpha-amylase from a prominent human gut symbiont targets complex starch molecules | Q27659874 | ||
Structural basis for the glucan phosphatase activity of Starch Excess4 | Q27663820 | ||
Structural and functional analysis of PTPMT1, a phosphatase required for cardiolipin synthesis | Q27670687 | ||
Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B | Q27729426 | ||
Crystal structure of the dual specificity protein phosphatase VHR | Q27732778 | ||
Molecular structure of a barley alpha-amylase-inhibitor complex: implications for starch binding and catalysis | Q27756754 | ||
The interpretation of protein structures: Estimation of static accessibility | Q27860750 | ||
Overview of the CCP4 suite and current developments | Q27860782 | ||
Dali server: conservation mapping in 3D | Q27860994 | ||
Refinement of macromolecular structures by the maximum-likelihood method | Q27861011 | ||
Features and development of Coot | Q27861079 | ||
Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates | Q28116113 | ||
Phosphorylation of C6- and C3-positions of glucosyl residues in starch is catalysed by distinct dikinases | Q28258207 | ||
Glycogen and related polysaccharides inhibit the laforin dual-specificity protein phosphatase | Q28585159 | ||
Conservation of the glucan phosphatase laforin is linked to rates of molecular evolution and the glucan metabolism of the organism | Q28752185 | ||
Carbohydrate-binding modules: fine-tuning polysaccharide recognition | Q29547768 | ||
Protein tyrosine phosphatases: from genes, to function, to disease | Q29614826 | ||
Starch-binding domains in the post-genome era. | Q30159621 | ||
Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo. | Q30441600 | ||
Amylopectin aggregation as a function of starch phosphate content studied by size exclusion chromatography and on-line refractive index and light scattering. | Q30666191 | ||
Glucan, water dikinase activity stimulates breakdown of starch granules by plastidial beta-amylases | Q33290860 | ||
Starch phosphorylation--maltosidic restrains upon 3'- and 6'-phosphorylation investigated by chemical synthesis, molecular dynamics and NMR spectroscopy | Q33382804 | ||
Laforin, a dual specificity phosphatase involved in Lafora disease, is present mainly as monomeric form with full phosphatase activity | Q34009801 | ||
A redox-regulated chloroplast protein phosphatase binds to starch diurnally and functions in its accumulation | Q34687203 | ||
Mutations in a gene encoding a novel protein tyrosine phosphatase cause progressive myoclonus epilepsy | Q34754070 | ||
Starch phosphorylation: a new front line in starch research | Q34979837 | ||
The phosphatase laforin crosses evolutionary boundaries and links carbohydrate metabolism to neuronal disease. | Q36119725 | ||
Starch metabolism in Arabidopsis | Q36480045 | ||
A malachite green-based assay to assess glucan phosphatase activity | Q36625218 | ||
Probing the role of aromatic residues at the secondary saccharide-binding sites of human salivary alpha-amylase in substrate hydrolysis and bacterial binding | Q37101576 | ||
Evolution of protein phosphatases in plants and animals | Q37355920 | ||
Eukaryotic starch degradation: integration of plastidial and cytosolic pathways. | Q37424661 | ||
Advances and pitfalls of protein structural alignment | Q37501173 | ||
Lafora disease: insights into neurodegeneration from plant metabolism | Q37612219 | ||
Helix-breaking news: fighting crystalline starch energy deposits in the cell | Q37690974 | ||
Regulation of starch metabolism: the age of enlightenment? | Q37695690 | ||
Progress in Arabidopsis starch research and potential biotechnological applications | Q37824053 | ||
Occurrence and functional significance of secondary carbohydrate binding sites in glycoside hydrolases | Q37895266 | ||
Biochemistry and genetics of starch synthesis | Q37963041 | ||
Structure of the complex of a yeast glucoamylase with acarbose reveals the presence of a raw starch binding site on the catalytic domain | Q38313766 | ||
A chloroplast-localized dual-specificity protein phosphatase in Arabidopsis contains a phylogenetically dispersed and ancient carbohydrate-binding domain, which binds the polysaccharide starch | Q38314121 | ||
Oligosaccharide binding to barley alpha-amylase 1. | Q38323448 | ||
The Laforin-like dual-specificity phosphatase SEX4 from Arabidopsis hydrolyzes both C6- and C3-phosphate esters introduced by starch-related dikinases and thereby affects phase transition of alpha-glucans | Q43216933 | ||
The carbohydrate-binding domain of Lafora disease protein targets Lafora polyglucosan bodies. | Q44714579 | ||
A novel isoform of glucan, water dikinase phosphorylates pre-phosphorylated alpha-glucans and is involved in starch degradation in Arabidopsis | Q45247928 | ||
Two secondary carbohydrate binding sites on the surface of barley alpha-amylase 1 have distinct functions and display synergy in hydrolysis of starch granules | Q45858174 | ||
STARCH-EXCESS4 is a laforin-like Phosphoglucan phosphatase required for starch degradation in Arabidopsis thaliana. | Q46164576 | ||
Starch-binding domains in the CBM45 family--low-affinity domains from glucan, water dikinase and α-amylase involved in plastidial starch metabolism | Q50527353 | ||
A putative phosphatase, LSF1, is required for normal starch turnover in Arabidopsis leaves. | Q53486358 | ||
The distribution of covalently bound phosphate in the starch granule in relation to starch crystallinity | Q56956398 | ||
Similar Protein Phosphatases Control Starch Metabolism in Plants and Glycogen Metabolism in Mammals | Q58035365 | ||
The Phosphoglucan Phosphatase Like Sex Four2 Dephosphorylates Starch at the C3-Position inArabidopsis | Q58036586 | ||
Starch synthesis in Arabidopsis. Granule synthesis, composition, and structure | Q58036632 | ||
Starch granules: structure and biosynthesis | Q62570635 | ||
Mutants of Arabidopsis with altered regulation of starch degradation | Q83271271 | ||
Special issue: Protein phosphatases: from molecules to networks: introduction | Q85823495 | ||
P433 | issue | 6 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | cell biology | Q7141 |
P304 | page(s) | 2302-14 | |
P577 | publication date | 2013-06-01 | |
P1433 | published in | The Plant Cell | Q3988745 |
P1476 | title | Structure of the Arabidopsis Glucan Phosphatase LIKE SEX FOUR2 Reveals a Unique Mechanism for Starch Dephosphorylation | |
P478 | volume | 25 |
Q27684899 | A conformational landscape for alginate secretion across the outer membrane ofPseudomonas aeruginosa |
Q44301821 | A new mechanism for starch dephosphorylation: insight from the structure of like sex four2. |
Q57572147 | Analysis of surface binding sites (SBSs) in carbohydrate active enzymes with focus on glycoside hydrolase families 13 and 77 — a mini-review |
Q42127368 | Assessing the Biological Activity of the Glucan Phosphatase Laforin |
Q91019592 | Brain Glycogen Structure and Its Associated Proteins: Past, Present and Future |
Q35137007 | Expression, purification and characterization of soluble red rooster laforin as a fusion protein in Escherichia coli |
Q59329234 | Functional Roles of Starch Binding Domains and Surface Binding Sites in Enzymes Involved in Starch Biosynthesis |
Q48184278 | Identification and analysis of OsttaDSP, a phosphoglucan phosphatase from Ostreococcus tauri. |
Q36281719 | Mechanistic Insights into Glucan Phosphatase Activity against Polyglucan Substrates |
Q27683649 | Phosphoglucan-bound structure of starch phosphatase Starch Excess4 reveals the mechanism for C6 specificity |
Q40111975 | Plant α-glucan phosphatases SEX4 and LSF2 display different affinity for amylopectin and amylose |
Q38920799 | Structural biology of glucan phosphatases from humans to plants |
Q29465784 | Structural mechanism of laforin function in glycogen dephosphorylation and lafora disease |
Q37072101 | Structural mechanisms of plant glucan phosphatases in starch metabolism |
Q46552171 | Structure and expression of phosphoglucan phosphatase genes of Like Sex Four1 and Like Sex Four2 in barley. |
Q48227515 | The Starch Granule-Associated Protein EARLY STARVATION1 Is Required for the Control of Starch Degradation in Arabidopsis thaliana Leaves |
Q37037323 | Unique carbohydrate binding platforms employed by the glucan phosphatases |
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