S
Sandra B. Gabelli
Researcher at Johns Hopkins University School of Medicine
Publications - 103
Citations - 5792
Sandra B. Gabelli is an academic researcher from Johns Hopkins University School of Medicine. The author has contributed to research in topics: Hydrolase & Nudix hydrolase. The author has an hindex of 31, co-authored 91 publications receiving 4764 citations. Previous affiliations of Sandra B. Gabelli include Johns Hopkins University & Howard Hughes Medical Institute.
Papers
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Journal ArticleDOI
Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab
Hyun Soo Cho,Karen Mason,Kasra X. Ramyar,Ann Marie Stanley,Sandra B. Gabelli,Dan W. Denney,Daniel J. Leahy +6 more
TL;DR: Crystal structures of the entire extracellular regions of rat and human HER2 reveal a fixed conformation for HER2 that resembles a ligand-activated state, and show HER2 poised to interact with other ErbB receptors in the absence of direct ligand binding.
Journal ArticleDOI
The Structure of a Human p110α/p85α Complex Elucidates the Effects of Oncogenic PI3Kα Mutations
Chuan Hsiang Huang,Chuan Hsiang Huang,Diana Mandelker,Diana Mandelker,Oleg Schmidt-Kittler,Oleg Schmidt-Kittler,Yardena Samuels,Yardena Samuels,Victor E. Velculescu,Victor E. Velculescu,Kenneth W. Kinzler,Kenneth W. Kinzler,Bert Vogelstein,Bert Vogelstein,Sandra B. Gabelli,Sandra B. Gabelli,L. Mario Amzel,L. Mario Amzel +17 more
TL;DR: The structure of PI3Kα shows that many of the mutations occur at residues lying at the interfaces between p110 α and p85α or between the kinase domain of p110α and other domains within the catalytic subunit, which suggests specific mechanisms for the effect of oncogenic mutations.
Journal ArticleDOI
Structures and Mechanisms of Nudix Hydrolases
Albert S. Mildvan,Zuyong Xia,Hugo F. Azurmendi,V. Saraswat,Patricia M. Legler,Michael A. Massiah,Sandra B. Gabelli,Mario A. Bianchet,Lin-Woo Kang,L.M. Amzel +9 more
TL;DR: Nudix hydrolases catalyze the hydrolysis of nucleoside diphosphates linked to other moieties, X, and contain the sequence motif or Nudix box, GX(5)EX(7)REUXEEXGU, which are highly diverse in the position on the substrate at which nucleophilic substitution occurs, and in the number of required cations.
Journal ArticleDOI
A frequent kinase domain mutation that changes the interaction between PI3Kα and the membrane
Diana Mandelker,Sandra B. Gabelli,Oleg Schmidt-Kittler,Jiuxiang Zhu,Ian Cheong,Chuan Hsiang Huang,Kenneth W. Kinzler,Bert Vogelstein,L.M. Amzel +8 more
TL;DR: Structural and biochemical data suggest a previously undescribed mechanism for mutational activation of a kinase that involves perturbation of its interaction with the cellular membrane, which is differentially regulated by lipid membrane composition.
Book ChapterDOI
Salting out of Proteins Using Ammonium Sulfate Precipitation
TL;DR: In this protocol, ammonium sulfate will be added incrementally to an E. coli cell lysate to isolate a recombinantly over-expressed protein of 20 kDa containing no cysteine residues or tags.