D-Index & Metrics Best Publications

D-Index & Metrics D-index (Discipline H-index) only includes papers and citation values for an examined discipline in contrast to General H-index which accounts for publications across all disciplines.

Discipline name D-index D-index (Discipline H-index) only includes papers and citation values for an examined discipline in contrast to General H-index which accounts for publications across all disciplines. Citations Publications World Ranking National Ranking
Chemistry D-index 58 Citations 11,263 350 World Ranking 5787 National Ranking 143

Overview

What is he best known for?

The fields of study he is best known for:

  • Organic chemistry
  • Amino acid
  • Enzyme

His primary scientific interests are in Stereochemistry, Crystallography, Peptide, Helix and Amino acid. As part of his studies on Stereochemistry, Marco Crisma often connects relevant subjects like Oligopeptide. The study incorporates disciplines such as X-ray crystallography, Electron paramagnetic resonance, Molecule and Residue in addition to Crystallography.

In the subject of general Peptide, his work in Tripeptide is often linked to Alpha, thereby combining diverse domains of study. His research integrates issues of Turn, Chromophore, Internal conversion, Excitation and Atomic physics in his study of Helix. His Amino acid research integrates issues from Protein structure, Collagen helix, Polymer chemistry and Isotope.

His most cited work include:

  • Control of peptide conformation by the Thorpe-Ingold effect (C?-tetrasubstitution) (494 citations)
  • Circular Dichroism Spectrum of a Peptide 310-Helix (291 citations)
  • Structures of peptides from α-amino acids methylated at the α-carbon (197 citations)

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

His primary areas of study are Stereochemistry, Peptide, Crystallography, Amino acid and Residue. His Stereochemistry research incorporates themes from Tripeptide, Helix, Crystal structure, Dipeptide and Molecule. His studies deal with areas such as 310 helix and Circular dichroism as well as Peptide.

His research investigates the connection between Crystallography and topics such as Intramolecular force that intersect with problems in Hydrogen bond. His research in Amino acid intersects with topics in Chirality, Organic chemistry and Diastereomer. His Residue research is multidisciplinary, relying on both Proton NMR, Pentamer, Carboxylic acid, Protein structure and Infrared spectroscopy.

He most often published in these fields:

  • Stereochemistry (74.59%)
  • Peptide (39.16%)
  • Crystallography (30.77%)

What were the highlights of his more recent work (between 2011-2021)?

  • Stereochemistry (74.59%)
  • Peptide (39.16%)
  • Crystallography (30.77%)

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

His primary areas of investigation include Stereochemistry, Peptide, Crystallography, Amino acid and Combinatorial chemistry. His primary area of study in Stereochemistry is in the field of Nuclear magnetic resonance spectroscopy. Marco Crisma has researched Peptide in several fields, including Residue, Helix and Circular dichroism.

His Crystallography study combines topics in areas such as Spectral line, Molecule and Diffraction. The various areas that he examines in his Amino acid study include Electron paramagnetic resonance, Absolute configuration and Chirality. His Combinatorial chemistry research is multidisciplinary, incorporating perspectives in Atom, Redox, Naphthoquinone and Homopeptide.

Between 2011 and 2021, his most popular works were:

  • Helical screw-sense preferences of peptides based on chiral, Cα-tetrasubstituted α-amino acids. (42 citations)
  • Handedness preference and switching of peptide helices. Part I: Helices based on protein amino acids. (37 citations)
  • Rational design of gold(III)-dithiocarbamato peptidomimetics for the targeted anticancer chemotherapy. (34 citations)

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

  • Organic chemistry
  • Amino acid
  • Enzyme

His primary areas of study are Stereochemistry, Peptide, Combinatorial chemistry, Amino acid and Helix. Marco Crisma has included themes like Crystallography, Peptidomimetic, Oligopeptide and Antimicrobial in his Stereochemistry study. As a member of one scientific family, Marco Crisma mostly works in the field of Crystallography, focusing on Chirality and, on occasion, Steric effects, Axial chirality and Molecule.

His work deals with themes such as Residue, Computational biology, Hydrogen bond and Circular dichroism, which intersect with Peptide. His studies in Amino acid integrate themes in fields like Pyrrolidine, Atom, Terminal and Helical peptide. His study looks at the relationship between Helix and fields such as Peptide Conformation, as well as how they intersect with chemical problems.

This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.

Best Publications

Control of peptide conformation by the Thorpe-Ingold effect (C?-tetrasubstitution)

Claudio Toniolo;Marco Crisma;Fernando Formaggio;Cristina Peggion.
Biopolymers (2001)

645 Citations

Circular Dichroism Spectrum of a Peptide 310-Helix

Claudio Toniolo;Alessandra Polese;Fernando Formaggio;Marco Crisma.
Journal of the American Chemical Society (1996)

436 Citations

Structures of peptides from α-amino acids methylated at the α-carbon

C Toniolo;M Crisma;F Formaggio;G Valle.
Biopolymers (1993)

284 Citations

Energy transport in peptide helices

Virgiliu Botan;Ellen H. G. Backus;Rolf Pfister;Alessandro Moretto.
Proceedings of the National Academy of Sciences of the United States of America (2007)

182 Citations

Conformational Characterization of Terminally Blocked l-(αMe)Val Homopeptides Using Vibrational and Electronic Circular Dichroism. 310-Helical Stabilization by Peptide−Peptide Interaction

Gorm Yoder;Alessandra Polese;R. A. G. D. Silva;Fernando Formaggio.
Journal of the American Chemical Society (1997)

156 Citations

Lipopeptaibols, a novel family of membrane active, antimicrobial peptides.

C. Toniolo;M. Crisma;F. Formaggio;C. Peggion.
Cellular and Molecular Life Sciences (2001)

156 Citations

Comparison of the Effect of Five Guest Residues on the eta-Sheet Conformation of Host ${(L-Val)}_n$ Oligopeptides

V. Moretto;M. Crisma;G. M. Bonora;C. Toniolo.
Macromolecules (1989)

155 Citations

Structure determination of racemic trichogin A IV using centrosymmetric crystals

Claudio Toniolo;Cristina Peggion;Marco Crisma;Fernando Formaggio.
Nature Structural & Molecular Biology (1994)

153 Citations

ESR Characterization of Hexameric, Helical Peptides Using Double TOAC Spin Labeling

Paul Hanson;Glenn Millhauser;Fernando Formaggio;Marco Crisma.
Journal of the American Chemical Society (1996)

149 Citations

TOAC, a nitroxide spin‐labeled, achiral Cα‐tetrasubstituted α‐amino acid, is an excellent tool in material science and biochemistry

Claudio Toniolo;Marco Crisma;Fernando Formaggio.
Biopolymers (1998)

145 Citations

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