Adrian R. Ferré-D'Amaré

What is he best known for?

The fields of study he is best known for:

• DNA
• Gene
• Enzyme

His primary areas of study are RNA, Biochemistry, Stereochemistry, Riboswitch and Ribozyme. His study in the field of Ribonucleoprotein is also linked to topics like Nucleolus. His Stereochemistry research is multidisciplinary, incorporating perspectives in Crystallography, Basic helix-loop-helix, Leucine zipper and DNA.

His studies deal with areas such as Cobalamin riboswitch, TPP riboswitch and Thiamine as well as Riboswitch. The concepts of his Ribozyme study are interwoven with issues in Cleavage and Active site. His work in Hairpin ribozyme addresses subjects such as VS ribozyme, which are connected to disciplines such as GIR1 branching ribozyme and Mammalian CPEB3 ribozyme.

His most cited work include:

• Crystal structure of a hepatitis delta virus ribozyme (614 citations)
• Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain. (601 citations)
• Molecular basis of mouse microphthalmia ( mi ) mutations helps explain their developmental and phenotypic consequences (430 citations)

What are the main themes of his work throughout his whole career to date?

Adrian R. Ferré-D'Amaré spends much of his time researching RNA, Riboswitch, Biochemistry, Ribozyme and Stereochemistry. His RNA study combines topics from a wide range of disciplines, such as Crystallography, Biophysics, Aptamer, Computational biology and Binding site. His research investigates the connection between Crystallography and topics such as Crystallization that intersect with issues in RNA-binding protein.

The study incorporates disciplines such as Nucleic acid structure, Cobalamin riboswitch and Small molecule in addition to Riboswitch. Cleavage is closely connected to Active site in his research, which is encompassed under the umbrella topic of Ribozyme. His study in GlmS glucosamine-6-phosphate activated ribozyme is interdisciplinary in nature, drawing from both Cofactor and GIR1 branching ribozyme.

He most often published in these fields:

• RNA (65.33%)
• Riboswitch (44.00%)
• Biochemistry (31.33%)

What were the highlights of his more recent work (between 2017-2021)?

• RNA (65.33%)
• Aptamer (16.00%)
• Riboswitch (44.00%)

In recent papers he was focusing on the following fields of study:

RNA, Aptamer, Riboswitch, Biophysics and Crystal structure are his primary areas of study. Adrian R. Ferré-D'Amaré has researched RNA in several fields, including G-quadruplex, Transcription and Stereochemistry. His work deals with themes such as Nucleobase and Riboside, which intersect with Stereochemistry.

The various areas that he examines in his Aptamer study include Nucleotide, Base pair, Fluorophore, Combinatorial chemistry and Binding site. His Riboswitch research includes elements of Computational biology and Small molecule. His Small molecule research is included under the broader classification of Biochemistry.

Between 2017 and 2021, his most popular works were:

• Structural basis of G-quadruplex unfolding by the DEAH/RHA helicase DHX36 (105 citations)
• RNA G-quadruplex is resolved by repetitive and ATP-dependent mechanism of DHX36 (28 citations)
• Crystal Structures of the Mango-II RNA Aptamer Reveal Heterogeneous Fluorophore Binding and Guide Engineering of Variants with Improved Selectivity and Brightness. (26 citations)

In his most recent research, the most cited papers focused on:

• DNA
• Gene
• Enzyme

His scientific interests lie mostly in RNA, Aptamer, Biophysics, Fluorophore and Binding site. His RNA research integrates issues from Stereochemistry and Crystal structure. His studies deal with areas such as Nucleobase, Selectivity, Bacterial transcription and Mutant as well as Stereochemistry.

His Aptamer research incorporates themes from Nucleotide and Small molecule. His Riboswitch study combines topics in areas such as Nucleic acid tertiary structure, Computational biology and PreQ1 riboswitch. His DHX36 research is multidisciplinary, incorporating elements of A-DNA, Polymerase, Transcription and Cell biology.