M. Pacella
Molecular Biology · 2013–2020
A researcher in the Science corpus: 6 papers; trusts 1 researcher and is trusted by 0 researchers here, as inferred from the citation graph.
Subfields
- Molecular Biology — 333 citations into it
- Materials Chemistry — 160 citations into it
Whom M. Pacella trusts overall
Their strongest outbound trust, strongest first, inferred from their citations.
Who trusts M. Pacella overall
Papers from M. Pacella's perspective
Ordered by how strongly the researchers M. Pacella trusts endorse each paper. Same corpus, a different order for every researcher.
- Alternate states of proteins revealed by detailed energy landscape mapping
- Calculation of conformational ensembles from potentials of mean force. An approach to the knowledge-based prediction of local structures in globular proteins.
- Computational design of proteins targeting the conserved stem region of influenza hemagglutinin
- Modeling T cell receptor recognition of CD1-lipid and MR1-metabolite complexes
- T-Cell Transfer Therapy Targeting Mutant KRAS in Cancer
- Systematic Comparison of Amber and Rosetta Energy Functions for Protein Structure Evaluation.
- Repurposing Citizen Science Games as Software Tools for Professional Scientists
- A flexible docking approach for prediction of T cell receptor–peptide–MHC complexes
- Systematic Analysis of Helical Protein Interfaces Reveals Targets for Synthetic Inhibitors
- Rosetta3: An Object-Oriented Software Suite for the Simulation and Design of Macromolecules
Their papers
- The Rosetta all-atom energy function for macromolecular modeling and design (2017) — 1,486 citations
- Macromolecular modeling and design in Rosetta: recent methods and frameworks (2020) — 783 citations
- A Benchmarking Study of Peptide–Biomineral Interactions (2017) — 12 citations
- Using the RosettaSurface Algorithm to Predict Protein Structure at Mineral Surfaces (2013) — 21 citations
- A Parametric Rosetta Energy Function Analysis with LK Peptides on SAM Surfaces. (2018) — 4 citations
- Community‐wide evaluation of methods for predicting the effect of mutations on protein–protein interactions (2013) — 102 citations