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 114 Citations 38,301 475 World Ranking 359 National Ranking 181
Biology and Biochemistry D-index 114 Citations 38,826 491 World Ranking 564 National Ranking 383

Overview

What is he best known for?

The fields of study he is best known for:

  • Enzyme
  • Gene
  • Amino acid

Peptide, Stereochemistry, Protein structure, Circular dichroism and Peptide sequence are his primary areas of study. His Peptide research is multidisciplinary, incorporating perspectives in Amino acid, Chromatography and Antimicrobial. His Stereochemistry study integrates concerns from other disciplines, such as Side chain, Coiled coil, Gramicidin S and Beta sheet.

In his work, Protein engineering, Isoleucine, Folding and Antiparallel is strongly intertwined with Protein folding, which is a subfield of Protein structure. His Circular dichroism study combines topics from a wide range of disciplines, such as Guanidine, Alanine and Denaturation. His Peptide sequence study combines topics in areas such as Random coil, Lysine, Tropomyosin, Biological activity and Antibody.

His most cited work include:

  • New hydrophilicity scale derived from high-performance liquid chromatography peptide retention data: correlation of predicted surface residues with antigenicity and X-ray-derived accessible sites. (896 citations)
  • 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. (846 citations)
  • The Duchenne muscular dystrophy gene product is localized in sarcolemma of human skeletal muscle (574 citations)

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

His main research concerns Peptide, Stereochemistry, Biochemistry, Chromatography and Peptide sequence. His work deals with themes such as Amino acid, Crystallography, Protein structure and Pilin, which intersect with Peptide. His Crystallography research incorporates themes from Ionic bonding, Bilayer and Alanine.

His Stereochemistry research focuses on Circular dichroism in particular. His Circular dichroism research is multidisciplinary, relying on both Coiled coil, Heptad repeat, Guanidine, Denaturation and Hydrophobic effect. His Chromatography study incorporates themes from Phase and Analytical chemistry.

He most often published in these fields:

  • Peptide (48.98%)
  • Stereochemistry (27.19%)
  • Biochemistry (23.84%)

What were the highlights of his more recent work (between 2007-2020)?

  • Peptide (48.98%)
  • Peptide sequence (19.74%)
  • Biochemistry (23.84%)

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

The scientist’s investigation covers issues in Peptide, Peptide sequence, Biochemistry, Microbiology and Antimicrobial peptides. The Peptide study combines topics in areas such as Amino acid, Crystallography, High-performance liquid chromatography, Chromatography and Stereochemistry. His research in Crystallography focuses on subjects like Protein structure, which are connected to Protein folding, Biophysics, Antiparallel and Plasma protein binding.

He studies Circular dichroism which is a part of Stereochemistry. His Circular dichroism research incorporates elements of Hydrophobic effect and Tropomyosin. The study incorporates disciplines such as Binding domain, Pilin, Molecular biology, Alanine and Biological activity in addition to Peptide sequence.

Between 2007 and 2020, his most popular works were:

  • Effects of net charge and the number of positively charged residues on the biological activity of amphipathic α-helical cationic antimicrobial peptides (264 citations)
  • High-Performance Liquid Chromatography of Peptides and Proteins : Separation, Analysis, and Conformation (167 citations)
  • The role of position a in determining the stability and oligomerization state of alpha-helical coiled coils: 20 amino acid stability coefficients in the hydrophobic core of proteins. (147 citations)

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

  • Enzyme
  • Gene
  • Amino acid

His primary areas of study are Peptide, Peptide sequence, Stereochemistry, Microbiology and Protein structure. His study in Peptide is interdisciplinary in nature, drawing from both Amino acid, Ion exchange, Crystallography and Antimicrobial. His work investigates the relationship between Peptide sequence and topics such as Biological activity that intersect with problems in Hemolysis, Structure–activity relationship, Cationic Antimicrobial Peptides and Alpha.

Circular dichroism is the focus of his Stereochemistry research. His research in Circular dichroism intersects with topics in Coiled coil and Guanidine. His Protein structure research includes themes of Biophysics and Protein folding.

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

1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects.

David S. Wishart;Colin G. Bigam;Arne Holm;Robert S. Hodges.
Journal of Biomolecular NMR (1995)

1912 Citations

New hydrophilicity scale derived from high-performance liquid chromatography peptide retention data: correlation of predicted surface residues with antigenicity and X-ray-derived accessible sites.

J. M. R. Parker;D. Guo;R. S. Hodges.
Biochemistry (1986)

1537 Citations

The Duchenne muscular dystrophy gene product is localized in sarcolemma of human skeletal muscle

Elizabeth E. Zubrzycka-Gaarn;Dennis E. Bulman;George Karpati;Arthur H. M. Burghes.
Nature (1988)

801 Citations

Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide.

F. D. Sonnichsen;J. E. Van Eyk;R. S. Hodges;B. D. Sykes.
Biochemistry (1992)

772 Citations

Synthesis of a model protein of defined secondary and quaternary structure. Effect of chain length on the stabilization and formation of two-stranded alpha-helical coiled-coils.

S Y Lau;A K Taneja;R S Hodges.
Journal of Biological Chemistry (1984)

746 Citations

Rational Design of α-Helical Antimicrobial Peptides with Enhanced Activities and Specificity/Therapeutic Index

Yuxin Chen;Colin T. Mant;Susan W. Farmer;Robert E. W. Hancock.
Journal of Biological Chemistry (2005)

641 Citations

Role of Peptide Hydrophobicity in the Mechanism of Action of α-Helical Antimicrobial Peptides

Yuxin Chen;Michael T. Guarnieri;Adriana I. Vasil;Michael L. Vasil.
Antimicrobial Agents and Chemotherapy (2007)

605 Citations

Effects of net charge and the number of positively charged residues on the biological activity of amphipathic α-helical cationic antimicrobial peptides

Ziqing Jiang;Adriana I. Vasil;John D. Hale;Robert E. W. Hancock.
Biopolymers (2008)

485 Citations

Synthetic model proteins. Positional effects of interchain hydrophobic interactions on stability of two-stranded alpha-helical coiled-coils.

N E Zhou;C M Kay;R S Hodges.
Journal of Biological Chemistry (1992)

441 Citations

Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions

Oscar D. Monera;Cyril M. Kay;Robert S. Hodges.
Protein Science (1994)

434 Citations

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