J
James D. Baleja
Researcher at Tufts University
Publications - 85
Citations - 3453
James D. Baleja is an academic researcher from Tufts University. The author has contributed to research in topics: Nuclear magnetic resonance spectroscopy & Protein structure. The author has an hindex of 31, co-authored 84 publications receiving 3202 citations. Previous affiliations of James D. Baleja include Cincinnati Children's Hospital Medical Center & Beth Israel Deaconess Medical Center.
Papers
More filters
Journal ArticleDOI
SMN oligomerization defect correlates with spinal muscular atrophy severity.
Christian L. Lorson,John Strasswimmer,Jun Mei Yao,James D. Baleja,E. Hahnen,Brunhilde Wirth,Thanh Le,Arthur H.M. Burghes,Elliot J. Androphy +8 more
TL;DR: These findings identify decreased SMN self-association as a biochemical defect in SMA, and imply that disease severity is proportional to the intracellu-lar concentration of oligomerization-competent SMN proteins.
Journal ArticleDOI
Involvement of a gut–retina axis in protection against dietary glycemia-induced age-related macular degeneration
Sheldon Rowan,Shuhong Jiang,Tal Korem,Jedrzej Szymanski,Min Lee Chang,Jason Szelog,Christa Cassalman,Kalavathi Dasuri,Christina McGuire,Ryoji Nagai,Xue Liang Du,Michael Brownlee,Naila Rabbani,Paul J. Thornalley,James D. Baleja,Amy Deik,Kerry A. Pierce,Justin M. Scott,Clary B. Clish,Donald Smith,Adina Weinberger,Tali Avnit-Sagi,Maya Lotan-Pompan,Eran Segal,Allen Taylor +24 more
TL;DR: A nexus of metabolites and microbiota that appear to act within a gut–retina axis to protect against diet- and age-induced AMDf is revealed, indicating a functional interaction between dietary carbohydrates, the metabolome, including microbial cometabolites, and AMDf.
Journal ArticleDOI
Identification of the Phospholipid Binding Site in the Vitamin K-dependent Blood Coagulation Protein Factor IX
Steven J. Freedman,Mark D. Blostein,James D. Baleja,Margaret Jacobs,Barbara C. Furie,Bruce Furie +5 more
TL;DR: Results indicate that the NH2 terminus of the Gla domain, specifically including leucine 6 and phenylalanine 9 in the hydrophobic patch, is the contact surface on Factor IX that interacts with the phospholipid bilayer.
Journal ArticleDOI
Solution structure of the DNA-binding domain of Cd2-GAL4 from S. cerevisiae.
TL;DR: The structure obtained for the GAL4DNA-binding domain represents a novel DNA-binding motif that is observed for the compact domain in solution using NMR techniques as was seen for the central core of the N-terminal fragment bound to DNA using crystallographic techniques12.
Journal ArticleDOI
Distance measurement and structure refinement with NOE data
TL;DR: In this paper, the interproton distances from NOE data are estimated for a DNA decamer, d (TCTATCACCG). d (CGGTGATAGA ), which comprises the left 10 base pairs ( LlO) of the bacteriophage X OR3 operator.