The solution structure of (+)-spongistatin 1 in DMSO.

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The solution structure of (+)-spongistatin 1 in DMSO. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1021/OL100417D
P932PMC publication ID2856070
P698PubMed publication ID20297809
P5875ResearchGate publication ID42343400

P2093author name stringAmos B Smith
Onur Atasoylu
Christina Risatti
George Furst
P2860cites workImproved spectral resolution in cosy 1H NMR spectra of proteins via double quantum filteringQ29618846
Janocchio--a Java applet for viewing 3D structures and calculating NMR couplings and NOEsQ33286052
The spongistatins, potently cytotoxic inhibitors of tubulin polymerization, bind in a distinct region of the vinca domainQ71936206
Spongistatin 1, a highly cytotoxic, sponge-derived, marine natural product that inhibits mitosis, microtubule assembly, and the binding of vinblastine to tubulinQ72584846
Altohyrtins B and C and 5-desacetylaltohyrtin A, potent cytotoxic macrolide congeners of altohyrtin A, from the Okinawan marine sponge Hyrtios altumQ72852099
Compensation of refocusing inefficiency with synchronized inversion sweep (CRISIS) in multiplicity-edited HSQCQ79329448
P433issue8
P407language of work or nameEnglishQ1860
P921main subjectsolution structureQ99235426
P304page(s)1788-1791
P577publication date2010-04-01
P1433published inOrganic LettersQ2396276
P1476titleThe solution structure of (+)-spongistatin 1 in DMSO.
P478volume12

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Q51033732Bayesian inference of conformational state populations from computational models and sparse experimental observables.
Q35645437Conformation-activity relationships of polyketide natural products
Q37624604Conformational preferences of zampanolide and dactylolide
Q34985541Improved stereochemical analysis of conformationally flexible diamines by binding to a bisporphyrin molecular clip
Q35234700In vitro and in vivo anticancer activity of (+)-spongistatin 1.
Q38636770Macrocycles All Aflutter: Substitution at an Allylic Center Reveals Conformational Dynamics of [13]-Macrodilactones.
Q88003407Model Selection Using BICePs: A Bayesian Approach for Force Field Validation and Parameterization

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