The Experts below are selected from a list of 321 Experts worldwide ranked by ideXlab platform
Cynthia J. Burrows - One of the best experts on this subject based on the ideXlab platform.
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Structural Context effects in the oxidation of 8-Oxo-7,8-dihydro-2′- deoxyguanosine to hydantoin products: Electrostatics, base stacking, and base pairing
Journal of the American Chemical Society, 2012Co-Authors: Aaron M. Fleming, James G. Muller, Adrienne C. Dlouhy, Cynthia J. BurrowsAbstract:8-Oxo-7,8-dihydroguanine (OG) is the most common base damage found in cells, where it resides in many Structural Contexts, including the nucleotide pool, single-stranded DNA at transcription forks and replication bubbles, and duplex DNA base-paired with either adenine (A) or cytosine (C). OG is prone to further oxidation to the highly mutagenic hydantoin products spiroiminodihydantoin (Sp) and 5-guanidinohydantoin (Gh) in a sharply pH-dependent fashion within nucleosides. In the present work, studies were conducted to determine how the Structural Context affects OG oxidation to the hydantoins. These studies revealed a trend in which the Sp yield was greatest in unencumbered Contexts, such as nucleosides, while the Gh yield increased in oligodeoxynucleotide (ODN) Contexts or at reduced pH. Oxidation of oligomers containing hydrogen-bond modulators (2,6-diaminopurine, N4-ethylcytidine) or alteration of the reaction conditions (pH, temperature, and salt) identify base stacking, electrostatics, and base pairi...
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Structural Context effects in the oxidation of 8 oxo 7 8 dihydro 2 deoxyguanosine to hydantoin products electrostatics base stacking and base pairing
Journal of the American Chemical Society, 2012Co-Authors: Aaron M. Fleming, James G. Muller, Adrienne C. Dlouhy, Cynthia J. BurrowsAbstract:8-Oxo-7,8-dihydroguanine (OG) is the most common base damage found in cells, where it resides in many Structural Contexts, including the nucleotide pool, single-stranded DNA at transcription forks and replication bubbles, and duplex DNA base-paired with either adenine (A) or cytosine (C). OG is prone to further oxidation to the highly mutagenic hydantoin products spiroiminodihydantoin (Sp) and 5-guanidinohydantoin (Gh) in a sharply pH-dependent fashion within nucleosides. In the present work, studies were conducted to determine how the Structural Context affects OG oxidation to the hydantoins. These studies revealed a trend in which the Sp yield was greatest in unencumbered Contexts, such as nucleosides, while the Gh yield increased in oligodeoxynucleotide (ODN) Contexts or at reduced pH. Oxidation of oligomers containing hydrogen-bond modulators (2,6-diaminopurine, N4-ethylcytidine) or alteration of the reaction conditions (pH, temperature, and salt) identify base stacking, electrostatics, and base pairi...
Aaron M. Fleming - One of the best experts on this subject based on the ideXlab platform.
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Structural Context effects in the oxidation of 8-Oxo-7,8-dihydro-2′- deoxyguanosine to hydantoin products: Electrostatics, base stacking, and base pairing
Journal of the American Chemical Society, 2012Co-Authors: Aaron M. Fleming, James G. Muller, Adrienne C. Dlouhy, Cynthia J. BurrowsAbstract:8-Oxo-7,8-dihydroguanine (OG) is the most common base damage found in cells, where it resides in many Structural Contexts, including the nucleotide pool, single-stranded DNA at transcription forks and replication bubbles, and duplex DNA base-paired with either adenine (A) or cytosine (C). OG is prone to further oxidation to the highly mutagenic hydantoin products spiroiminodihydantoin (Sp) and 5-guanidinohydantoin (Gh) in a sharply pH-dependent fashion within nucleosides. In the present work, studies were conducted to determine how the Structural Context affects OG oxidation to the hydantoins. These studies revealed a trend in which the Sp yield was greatest in unencumbered Contexts, such as nucleosides, while the Gh yield increased in oligodeoxynucleotide (ODN) Contexts or at reduced pH. Oxidation of oligomers containing hydrogen-bond modulators (2,6-diaminopurine, N4-ethylcytidine) or alteration of the reaction conditions (pH, temperature, and salt) identify base stacking, electrostatics, and base pairi...
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Structural Context effects in the oxidation of 8 oxo 7 8 dihydro 2 deoxyguanosine to hydantoin products electrostatics base stacking and base pairing
Journal of the American Chemical Society, 2012Co-Authors: Aaron M. Fleming, James G. Muller, Adrienne C. Dlouhy, Cynthia J. BurrowsAbstract:8-Oxo-7,8-dihydroguanine (OG) is the most common base damage found in cells, where it resides in many Structural Contexts, including the nucleotide pool, single-stranded DNA at transcription forks and replication bubbles, and duplex DNA base-paired with either adenine (A) or cytosine (C). OG is prone to further oxidation to the highly mutagenic hydantoin products spiroiminodihydantoin (Sp) and 5-guanidinohydantoin (Gh) in a sharply pH-dependent fashion within nucleosides. In the present work, studies were conducted to determine how the Structural Context affects OG oxidation to the hydantoins. These studies revealed a trend in which the Sp yield was greatest in unencumbered Contexts, such as nucleosides, while the Gh yield increased in oligodeoxynucleotide (ODN) Contexts or at reduced pH. Oxidation of oligomers containing hydrogen-bond modulators (2,6-diaminopurine, N4-ethylcytidine) or alteration of the reaction conditions (pH, temperature, and salt) identify base stacking, electrostatics, and base pairi...
So Iwata - One of the best experts on this subject based on the ideXlab platform.
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band 3 the human red cell chloride bicarbonate anion exchanger ae1 slc4a1 in a Structural Context
Biochimica et Biophysica Acta, 2016Co-Authors: Reinhart A. F. Reithmeier, Joseph R Casey, Antreas C Kalli, Mark S P Sansom, Yilmaz Alguel, So IwataAbstract:The crystal structure of the dimeric membrane domain of human Band 31, the red cell chloride/bicarbonate anion exchanger 1 (AE1, SLC4A1), provides a Structural Context for over four decades of studies into this historic and important membrane glycoprotein. In this review, we highlight the key Structural features responsible for anion binding and translocation and have integrated the following topological markers within the Band 3 structure: blood group antigens, N-glycosylation site, protease cleavage sites, inhibitor and chemical labeling sites, and the results of scanning cysteine and N-glycosylation mutagenesis. Locations of mutations linked to human disease, including those responsible for Southeast Asian ovalocytosis, hereditary stomatocytosis, hereditary spherocytosis, and distal renal tubular acidosis, provide molecular insights into their effect on Band 3 folding. Finally, molecular dynamics simulations of phosphatidylcholine self-assembled around Band 3 provide a view of this membrane protein within a lipid bilayer.
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Band 3, the human red cell chloride/bicarbonate anion exchanger (AE1, SLC4A1), in a Structural Context.
Biochimica et Biophysica Acta, 2016Co-Authors: Reinhart A. F. Reithmeier, Joseph R Casey, Antreas C Kalli, Mark S P Sansom, Yilmaz Alguel, So IwataAbstract:The crystal structure of the dimeric membrane domain of human Band 31, the red cell chloride/bicarbonate anion exchanger 1 (AE1, SLC4A1), provides a Structural Context for over four decades of studies into this historic and important membrane glycoprotein. In this review, we highlight the key Structural features responsible for anion binding and translocation and have integrated the following topological markers within the Band 3 structure: blood group antigens, N-glycosylation site, protease cleavage sites, inhibitor and chemical labeling sites, and the results of scanning cysteine and N-glycosylation mutagenesis. Locations of mutations linked to human disease, including those responsible for Southeast Asian ovalocytosis, hereditary stomatocytosis, hereditary spherocytosis, and distal renal tubular acidosis, provide molecular insights into their effect on Band 3 folding. Finally, molecular dynamics simulations of phosphatidylcholine self-assembled around Band 3 provide a view of this membrane protein within a lipid bilayer.
Robert E Engdahl - One of the best experts on this subject based on the ideXlab platform.
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Structural Context of the great sumatra andaman islands earthquake
Geophysical Research Letters, 2008Co-Authors: N M Shapiro, Michael H Ritzwoller, Robert E EngdahlAbstract:[1] A new three-dimensional seismic model and relocated regional seismicity are used to illuminate the great Sumatra-Andaman Islands earthquake of December 26, 2004. The earthquake initiated where the incoming Indian Plate lithosphere is warmest and the dip of the Wadati-Benioff zone is least steep along the subduction zone extending from the Andaman Trench to the Java Trench. Anomalously high temperatures are observed in the supra-slab mantle wedge in the Andaman back-arc. The subducting slab is observed along the entire plate boundary to a depth of at least 200 km. These factors contribute to the location of the initiation of rupture, the strength of seismic coupling, the differential rupture properties between the northern and southern segments of the earthquake, and the cause of convergence in the Andaman segment.
Reinhart A. F. Reithmeier - One of the best experts on this subject based on the ideXlab platform.
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Band 3 function and dysfunction in a Structural Context
Current Opinion in Hematology, 2018Co-Authors: Yazan M. Abbas, Ashley M. Toye, John L. Rubinstein, Reinhart A. F. ReithmeierAbstract:Current research on the human band 3 glycoprotein, the red cell chloride/bicarbonate anion exchanger (AE1), is highlighted and placed within a Structural Context. The determination of the crystal structure of the membrane domain of human band 3, the founding member of the solute carrier 4 (SLC4) family of bicarbonate transporters, is a major breakthrough toward understanding the mechanism of action of this membrane transport protein, its interaction with partner proteins, and how mutations linked to disease affect its ability to fold and function. Band 3 contains 14 transmembrane segments arranged in a 7+7 transmembrane inverted repeat topology common to all members of the SLC4 family and the unrelated SLC26 anion transporter family. A functional feature of this fold is the presence of a core and a gate domain: the core domain contains two short transmembrane helices (TM3 and 10) that face each other in the middle of the membrane with the positive N-terminal helix dipoles creating the anion-binding site, whereas the gate domain forms the dimer interface. During transport, the movement of these two domains relative to each other provides the intracellular and extracellular compartments with alternating access to the central anion-binding site.
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band 3 the human red cell chloride bicarbonate anion exchanger ae1 slc4a1 in a Structural Context
Biochimica et Biophysica Acta, 2016Co-Authors: Reinhart A. F. Reithmeier, Joseph R Casey, Antreas C Kalli, Mark S P Sansom, Yilmaz Alguel, So IwataAbstract:The crystal structure of the dimeric membrane domain of human Band 31, the red cell chloride/bicarbonate anion exchanger 1 (AE1, SLC4A1), provides a Structural Context for over four decades of studies into this historic and important membrane glycoprotein. In this review, we highlight the key Structural features responsible for anion binding and translocation and have integrated the following topological markers within the Band 3 structure: blood group antigens, N-glycosylation site, protease cleavage sites, inhibitor and chemical labeling sites, and the results of scanning cysteine and N-glycosylation mutagenesis. Locations of mutations linked to human disease, including those responsible for Southeast Asian ovalocytosis, hereditary stomatocytosis, hereditary spherocytosis, and distal renal tubular acidosis, provide molecular insights into their effect on Band 3 folding. Finally, molecular dynamics simulations of phosphatidylcholine self-assembled around Band 3 provide a view of this membrane protein within a lipid bilayer.
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Band 3, the human red cell chloride/bicarbonate anion exchanger (AE1, SLC4A1), in a Structural Context.
Biochimica et Biophysica Acta, 2016Co-Authors: Reinhart A. F. Reithmeier, Joseph R Casey, Antreas C Kalli, Mark S P Sansom, Yilmaz Alguel, So IwataAbstract:The crystal structure of the dimeric membrane domain of human Band 31, the red cell chloride/bicarbonate anion exchanger 1 (AE1, SLC4A1), provides a Structural Context for over four decades of studies into this historic and important membrane glycoprotein. In this review, we highlight the key Structural features responsible for anion binding and translocation and have integrated the following topological markers within the Band 3 structure: blood group antigens, N-glycosylation site, protease cleavage sites, inhibitor and chemical labeling sites, and the results of scanning cysteine and N-glycosylation mutagenesis. Locations of mutations linked to human disease, including those responsible for Southeast Asian ovalocytosis, hereditary stomatocytosis, hereditary spherocytosis, and distal renal tubular acidosis, provide molecular insights into their effect on Band 3 folding. Finally, molecular dynamics simulations of phosphatidylcholine self-assembled around Band 3 provide a view of this membrane protein within a lipid bilayer.
