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R.M. Immormino

Researcher at Duke University

Publications -  20
Citations -  14405

R.M. Immormino is an academic researcher from Duke University. The author has contributed to research in topics: Medicine & Immunology. The author has an hindex of 9, co-authored 12 publications receiving 11519 citations. Previous affiliations of R.M. Immormino include University of Washington & Hauptman-Woodward Medical Research Institute.

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Journal ArticleDOI

MolProbity: all-atom structure validation for macromolecular crystallography

TL;DR: MolProbity structure validation will diagnose most local errors in macromolecular crystal structures and help to guide their correction.
Book ChapterDOI

Chapter 21.6 MolProbity: all-atom structure validation for macromolecular crystallography

TL;DR: MolProbity is the authors’ contribution to helping solve the problem of local errors in X-ray crystallography and this chapter reviews its general capabilities, reports on recent enhancements and usage, and presents evidence that the resulting improvements are now beneficially affecting the global database.
Journal ArticleDOI

Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones.

TL;DR: A crystal structure of mammalian GRP94 in complex with AMPPNP and ADP is reported and a model for the role of ATP binding and hydrolysis in theGRP94 chaperone cycle is suggested.
Journal ArticleDOI

RNA backbone: consensus all-angle conformers and modular string nomenclature (an RNA Ontology Consortium contribution).

TL;DR: A consensus classification and nomenclature are defined for RNA backbone structure using all of the backbone torsion angles and this new backbone system will combine with others that define base pairs, base-stacking, and hydrogen-bond relationships to provide a full description of RNA structural motifs.
Journal ArticleDOI

Identification of potent water soluble purine-scaffold inhibitors of the heat shock protein 90.

TL;DR: Hsp90 is a chaperone protein that allows cancer cells to tolerate the many components of dysregulated pathways as discussed by the authors, and its inactivation may result in targeting multiple molecular alterations and, thus, in...