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Einat Sitbon

Researcher at Weizmann Institute of Science

Publications -  11
Citations -  1091

Einat Sitbon is an academic researcher from Weizmann Institute of Science. The author has contributed to research in topics: Protein structure & Conserved sequence. The author has an hindex of 9, co-authored 11 publications receiving 972 citations.

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Network analysis of protein structures identifies functional residues.

TL;DR: This work transformed protein structures into residue interaction graphs (RIGs), where amino acid residues are graph nodes and their interactions with each other are the graph edges, and found that active site, ligand-binding and evolutionary conserved residues, typically have high closeness values.
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Chirality-induced spin polarization places symmetry constraints on biomolecular interactions.

TL;DR: It is shown that the charge reorganization in chiral molecules is accompanied by a polarization of the spins associated with the displaced charge, and conjecture that the spin polarization enforces symmetry constraints on the biorecognition process between two chiral molecule, and how these constraints can lead to selectivity in the interaction between enantiomers based on their handedness.
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hsa-miR-191 Is a Candidate Oncogene Target for Hepatocellular Carcinoma Therapy

TL;DR: In this study, inhibition of miR-191 decreased cell proliferation and induced apoptosis in vitro and significantly reduced tumor masses in vivo in an orthotopic xenograft mouse model of HCC.
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Discovery of microRNAs and other small RNAs in solid tumors

TL;DR: The sequencing of small RNAs from 23 breast, bladder, colon and lung tumor samples using high throughput sequencing is reported, and dozens of new miRNA sequence variants are identified that demonstrate the existence of miRNA-related SNP or post-transcriptional modifications.
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Occurrence of protein structure elements in conserved sequence regions

TL;DR: The detailed statistical analysis of diverse proteins links protein evolution to the biophysics of protein thermodynamic stability and folding and the basic structural features of conserved sequence regions are identified.