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Marco Crisma

Marco Crisma

D-Index & Metrics

Chemistry

D-Index
61
Citations
13323
World Ranking
9237
National Ranking
264

Overview

Marco Crisma is affiliated with the University of Padua in Italy. Their research spans multiple scientific fields including Biochemistry, Genetics and Molecular Biology, Chemistry, and Materials Science. The subfields actively explored include Molecular Biology, Organic Chemistry, Materials Chemistry, Electrical and Electronic Engineering, and Biomaterials.

The principal research topics covered by Crisma involve Chemical Synthesis and Analysis, Ferrocene Chemistry and Applications, Crystallization and Solubility Studies, X-ray Diffraction in Crystallography, Click Chemistry and Applications, RNA and protein synthesis mechanisms, and Protein Structure and Dynamics.

The scientist has contributed to several notable publications throughout their career. Key papers include:

  • "Photoresponsive Prion-Mimic Foldamer to Induce Controlled Protein Aggregation," 2020, Angewandte Chemie International Edition
  • "Flat, Cα,β-Didehydroalanine Foldamers with Ferrocene Pendants: Assessing the Role of α-Peptide Dipolar Moments," 2021, ChemPlusChem
  • "Helical versus Flat Bis-Ferrocenyl End-Capped Peptides: The Influence of the Molecular Skeleton on Redox Properties," 2022, Molecules
  • "Photoresponsive Prion-Mimic Foldamer to Induce Controlled Protein Aggregation," 2020, Angewandte Chemie
  • "Isolated α-turns in peptides: a selected literature survey," 2023, Journal of Peptide Science

The majority of Crisma's publications appear in several recognized venues, including but not limited to:

  • The Cambridge Structural Database
  • Journal of Peptide Science
  • Angewandte Chemie International Edition
  • ChemPlusChem
  • Molecules

Their collaborative work prominently involves frequent co-authors:

  • Fernando Formaggio
  • Barbara Biondi
  • Saverio Santi
  • Annalisa Bisello
  • Roberta Cardena

Best Publications

  • Control of peptide conformation by the Thorpe-Ingold effect (C alpha-tetrasubstitution).

    Claudio Toniolo;Marco Crisma;Fernando Formaggio;Cristina Peggion

  • Circular Dichroism Spectrum of a Peptide 310-Helix

    Claudio Toniolo;Alessandra Polese;Fernando Formaggio;Marco Crisma

  • Structures of peptides from alpha-amino acids methylated at the alpha-carbon.

    C Toniolo;M Crisma;F Formaggio;G Valle

  • Studies of peptides forming 3(10)- and alpha-helices and beta-bend ribbon structures in organic solution and in model biomembranes by Fourier transform infrared spectroscopy.

    Unknown

  • Energy transport in peptide helices

    Virgiliu Botan;Ellen H. G. Backus;Rolf Pfister;Alessandro Moretto

  • Linear oligopeptides. 81. Solid-state and solution conformation of homooligo(.alpha.-aminoisobutyric acids) from tripeptide to pentapeptide: evidence for a 310 helix

    E. Benedetti;Alfonso Bavoso;B. Di Blasio;V. Pavone

  • 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

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

    C Toniolo;M Crisma;F Formaggio;C Peggion

  • Comparison of the effect of five guest residues on the .beta.-sheet conformation of host (L-val)n oligopeptides

    V. Moretto;M. Crisma;G. M. Bonora;C. Toniolo

  • Structure determination of racemic trichogin A IV using centrosymmetric crystals

    Claudio Toniolo;Cristina Peggion;Marco Crisma;Fernando Formaggio

  • Peptide helices based on α‐amino acids

    Marco Crisma;Fernando Formaggio;Alessandro Moretto;Claudio Toniolo

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

    Paul Hanson;Glenn Millhauser;Fernando Formaggio;Marco Crisma

  • 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

  • Preferred conformation of the terminally blocked (Aib)10 homo-oligopeptide : a long, regular 310-helix

    Claudio Toniolo;Marco Crisma;Gian Maria Bonora;Ettore Benedetti

  • Synthesis and conformational studies of peptides containing TOAC, a spin-labelled Cα,α-disubstituted glycine

    Claudio Toniolo;Ezio Valente;Fernando Formaggio;Marco Crisma

  • The First Water‐Soluble 310‐Helical Peptides

    Fernando Formaggio;Marco Crisma;Paola Rossi;Paolo Scrimin

  • Effect of Nα-Acyl Chain Length on the Membrane-Modifying Properties of Synthetic Analogs of the Lipopeptaibol Trichogin GA IV

    Claudio Toniolo;M. Crisma;Fernando Formaggio;Cristina Peggion

  • A Bimetallic Helical Heptapeptide as a Transphosphorylation Catalyst in Water

    Paola Rossi;Fulvia Felluga;Paolo Tecilla;Fernando Formaggio

  • Trichogin: a paradigm for lipopeptaibols.

    Cristina Peggion;Fernando Formaggio;Marco Crisma;Raquel F. Epand

  • Orientation and immersion depth of a helical lipopeptaibol in membranes using TOAC as an ESR probe.

    Vania Monaco;Fernando Formaggio;Marco Crisma;Claudio Toniolo

  • Structural characterization of the .beta.-bend ribbon spiral: crystallographic analysis of two long (L-Pro-Aib)n sequential peptides

    B. Di Blasio;V. Pavone;M. Saviano;A. Lombardi

Frequent Co-Authors

Claudio Toniolo
Claudio Toniolo University of Padua
Fernando Formaggio
Fernando Formaggio University of Padua
Ettore Benedetti
Ettore Benedetti University of Naples Federico II
Carlo Pedone
Carlo Pedone University of Naples Federico II
Vincenzo Pavone
Vincenzo Pavone University of Naples Federico II
Hans E. Schoemaker
Hans E. Schoemaker DSM (Netherlands)
Antonello Santini
Antonello Santini University of Naples Federico II
Padmanabhan Balaram
Padmanabhan Balaram Indian Institute of Science
Clifford George
Clifford George United States Naval Research Laboratory
Glenn L. Millhauser
Glenn L. Millhauser University of California, Santa Cruz

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