Výsledky vyhledávání - "Daniel Peisach"

Akademický článek

Crystal Structure Of Photorespiratory Alanine:Glyoxylate Aminotransferase 1 (AGT1) From Arabidopsis thaliana

Autor: Aaron H. Liepman, J. Vijayalakshmi, Daniel Peisach, Brian Hulsebus, Laura J. Olsen, Mark A. Saper

Publikováno v: Frontiers in Plant Science, Vol 10 (2019)

Photorespiration is an energetically costly metabolic pathway for the recycling of phosphoglycolate produced by the oxygenase activity of ribulose-1,5-bisphosphate carboxylase/oxygenase (RUBISCO) to phosphoglycerate. Arabidopsis alanine:glyoxylate am

Externí odkaz: https://doaj.org/article/eab33e1b2b104eb18eb020effced6bea

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Crystal Structure Of Photorespiratory Alanine:Glyoxylate Aminotransferase 1 (AGT1) From Arabidopsis thaliana

Autor: J. Vijayalakshmi, Mark A. Saper, Daniel Peisach, Aaron H. Liepman, Laura J. Olsen, Brian Hulsebus

Publikováno v: Frontiers in Plant Science
Frontiers in Plant Science, Vol 10 (2019)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a26109d0f5d653d12a9f9a4a75e30a1
http://europepmc.org/articles/PMC6797613

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Amelioration of toxicity in neuronal models of amyotrophic lateral sclerosis by hUPF1

Autor: Arpana Arjun, Dagmar Ringe, Eric J. Huang, Gregory A. Petsko, Yuxi Zhang, Steven Finkbeiner, Daniel Peisach, Xingli Li, Anthony Batarse, Haiyan Qiu, Hilary C. Archbold, Elizabeth M. H. Tank, Shulin Ju, Sami J. Barmada

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America, vol 112, iss 25
Barmada, SJ; Ju, S; Arjun, A; Batarse, A; Archbold, HC; Peisach, D; et al.(2015). Amelioration of toxicity in neuronal models of amyotrophic lateral sclerosis by hUPF1. Proceedings of the National Academy of Sciences of the United States of America, 112(25), 7821-7826. doi: 10.1073/pnas.1509744112. UC San Francisco: Retrieved from: http://www.escholarship.org/uc/item/5dn3b2m6

© 2015, National Academy of Sciences. All rights reserved. Over 30% of patients with amyotrophic lateral sclerosis (ALS) exhibit cognitive deficits indicative of frontotemporal dementia (FTD), suggesting a common pathogenesis for both diseases. Cons

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b41a215b7bf5513f473f2324ad29053
https://escholarship.org/uc/item/5dn3b2m6

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The crystal structure of TrxA(CACA): Insights into the formation of a [2Fe-2S] iron-sulfur cluster in anEscherichia colithioredoxin mutant

Autor: Daniel Peisach, Jean-François Collet, James C.A. Bardwell, Zhaohui Xu

Publikováno v: Protein Science. 14:1863-1869

Escherichia coli thioredoxin is a small monomeric protein that reduces disulfide bonds in cytoplasmic proteins. Two cysteine residues present in a conserved CGPC motif are essential for this activity. Recently, we identified mutations of this motif t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a365e11d72292d01811f2dcea4867272
https://doi.org/10.1110/ps.051464705

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The Crystal Structure of Choline Kinase Reveals a Eukaryotic Protein Kinase Fold

Autor: Zhaohui Xu, Claudia Kent, Patricia Gee, Daniel Peisach

Publikováno v: Structure. 11:703-713

Choline kinase catalyzes the ATP-dependent phosphorylation of choline, the first committed step in the CDP-choline pathway for the biosynthesis of phosphatidylcholine. The 2.0 Å crystal structure of a choline kinase from C. elegans (CKA-2) reveals t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74322efcaef4f08a5a333d0b00ff4bf1
https://doi.org/10.1016/s0969-2126(03)00094-7

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Autophagy induction enhances TDP43 turnover and survival in neuronal ALS models

Autor: Daniel Peisach, Steven Finkbeiner, Andrea Serio, D. Michael Ando, Andrey S. Tsvetkov, Xingli Li, Siddharthan Chandran, Bilada Bilican, Michael A. Pleiss, Aaron C. Daub, Arpana Arjun, Christopher Shaw, Sami J. Barmada

Publikováno v: Nature Chemical Biology, vol 10, iss 8
Nature chemical biology
Barmada, SJ; Serio, A; Arjun, A; Bilican, B; Daub, A; Ando, DM; et al.(2014). Autophagy induction enhances TDP43 turnover and survival in neuronal ALS models. Nature Chemical Biology, 10(8), 677-685. doi: 10.1038/nchembio.1563. UC San Francisco: Retrieved from: http://www.escholarship.org/uc/item/6z83h67w

Amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) have distinct clinical features but a common pathology - cytoplasmic inclusions rich in transactive response element DNA-binding protein of 43 kDa (TDP43). Rare TDP43 mutations cau

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98215cb3c05240288400d81e357e01f9
https://escholarship.org/uc/item/6z83h67w

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Effects of the E177K Mutation in d-Amino Acid Transaminase. Studies on an Essential Coenzyme Anchoring Group That Contributes to Stereochemical Fidelity

Autor: S D Erickson, K Soda, P W van Ophem, James M. Manning, Dagmar Ringe, Daniel Peisach

Publikováno v: Biochemistry. 38:1323-1331

D-Amino acid transaminase is a bacterial enzyme that uses pyridoxal phosphate (PLP) as a cofactor to catalyze the conversion of D-amino acids into their corresponding alpha-keto acids. This enzyme has already been established as a target for novel an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90a9f5cbe83e551a340fa9cb7d053db8
https://doi.org/10.1021/bi982414z

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Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 A resolution: implication of the structural role of Leu201 in transamination

Autor: Daniel Peisach, Nobuyoshi Esaki, Gregory A. Petsko, Tohru Yoshimura, Kazuhisa Kishimoto, Dagmar Ringe, Shigetoshi Sugio, A. Kashima

Publikováno v: Protein Engineering Design and Selection. 11:613-619

The leucine-to-alanine mutation at residue 201 of D-amino acid aminotransferase provides a unique enzyme which gradually loses its activity while catalyzing the normal transamination; the co-enzyme form is converted from pyridoxal 5'-phosphate to pyr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcefd26a3ded9c0ebfe0782edd3b0601
https://doi.org/10.1093/protein/11.8.613

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Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins

Autor: P.N. Garrison, Gregory A. Petsko, John M. Lowenstein, Daniel Peisach, Jeffrey Gilmour, Charles Brenner, Dagmar Ringe

Publikováno v: Nature Structural Biology. 4:231-238

Histidine triad nucleotide-binding protein (HINT), a dimeric purine nucleotide-binding protein from rabbit heart, is a member of the HIT (histidine triad) superfamily which includes HINT homologues and FHIT (HIT protein encoded at the chromosome 3 fr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a024df156688443b5de804ce0a0d300b
https://doi.org/10.1038/nsb0397-231

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