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Qiuju Zhou

Researcher at Chinese Academy of Sciences

Publications -  41
Citations -  798

Qiuju Zhou is an academic researcher from Chinese Academy of Sciences. The author has contributed to research in topics: Chemistry & Medicine. The author has an hindex of 14, co-authored 30 publications receiving 639 citations. Previous affiliations of Qiuju Zhou include Xinyang Normal University.

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Verification of specific G-quadruplex structure by using a novel cyanine dye supramolecular assembly: I. recognizing mixed G-quadruplex in human telomeres.

TL;DR: A novel cyanine dye supramolecular assembly was designed to recognize mixed G-quadruplex in human telomeres.
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Numerical simulation of rock fragmentation mechanisms subject to wedge penetration for TBMs

TL;DR: In this paper, a novel clustered assembly approach with irregular boundaries for grain-based brittle rock is incorporated into the particle flow code (PFC) to calibrate the macro-responses such as the low tensile to compressive strength ratio observed in laboratory tests.
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Verification of specific G-quadruplex structure by using a novel cyanine dye supramolecular assembly: II. The binding characterization with specific intramolecular G-quadruplex and the recognizing mechanism

TL;DR: Based on 1H-nuclear magnetic resonance and circular dichroism results, the preferring binding of ETC to specific intramolecular G-quadruplexes probably result from end-stacking, and the loop structure nearby also plays an important role.
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Stabilizing parallel G-quadruplex DNA by a new class of ligands: two non-planar alkaloids through interaction in lateral grooves.

TL;DR: Results have shown that planar structures are not essential for G-quadruplex stabilizers, which may represent a new class of G- quadruplex-targeted agents as potential antitumor drugs.
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Investigation on the interaction between a heterocyclic aminal derivative, SBDC, and human serum albumin.

TL;DR: It was observed that SBDC has a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure and data obtained by spectroscopic techniques and protein-ligand docking study suggested thatSBDC binds to residues located in subdomain IIA of H SA.