What is he best known for?
The fields of study he is best known for:
Yoshiki Yamaguchi mainly investigates Biochemistry, Stereochemistry, Glycan, Glycoprotein and Glycosylation.
His Biochemistry research is multidisciplinary, incorporating elements of Epitope and Moiety.
The study incorporates disciplines such as Protein structure, Peptide, Peptide sequence and Oligosaccharide in addition to Stereochemistry.
His Glycan research includes themes of In vitro, Sulfation, Sulfotransferase and High-performance liquid chromatography, Chromatography.
His study in Glycoprotein is interdisciplinary in nature, drawing from both Endoplasmic reticulum, Carbohydrate conformation, Function and Transmembrane protein.
His Glycosylation research incorporates themes from Fukutin, Muscular dystrophy, Ribitol and ATP synthase.
His most cited work include:
- Structural comparison of fucosylated and nonfucosylated Fc fragments of human immunoglobulin G1. (231 citations)
- Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domain (220 citations)
- Glycoform-dependent conformational alteration of the Fc region of human immunoglobulin G1 as revealed by NMR spectroscopy. (160 citations)
What are the main themes of his work throughout his whole career to date?
The scientist’s investigation covers issues in Biochemistry, Glycan, Stereochemistry, Glycosylation and Nuclear magnetic resonance spectroscopy.
His is involved in several facets of Biochemistry study, as is seen by his studies on Glycoprotein, Lectin, Plasma protein binding, Binding site and Endoplasmic reticulum.
His research in Binding site focuses on subjects like Biophysics, which are connected to Molecular dynamics.
His Glycan research includes elements of Oligosaccharide, Mannose, Fucose and Enzyme.
In his research on the topic of Stereochemistry, Proteasome is strongly related with Ubiquitin.
He interconnects Glycosyltransferase and N-linked glycosylation in the investigation of issues within Glycosylation.
He most often published in these fields:
- Biochemistry (40.22%)
- Glycan (25.09%)
- Stereochemistry (22.14%)
What were the highlights of his more recent work (between 2017-2021)?
- Glycan (25.09%)
- Biochemistry (40.22%)
- Glycosylation (13.28%)
In recent papers he was focusing on the following fields of study:
Yoshiki Yamaguchi spends much of his time researching Glycan, Biochemistry, Glycosylation, Biophysics and Stereochemistry.
The various areas that Yoshiki Yamaguchi examines in his Glycan study include Receptor, Sialic acid, Computational biology and Mannose.
His Glycosylation study combines topics from a wide range of disciplines, such as Adhesion, Osteopontin, Endoplasmic reticulum and Fucose.
His Biophysics research is multidisciplinary, incorporating perspectives in Rational design, Molecular dynamics, Yeast, Structural biology and Binding site.
His study of Nuclear magnetic resonance spectroscopy is a part of Stereochemistry.
The Glycoprotein study combines topics in areas such as Molecular mass and Fragment crystallizable region.
Between 2017 and 2021, his most popular works were:
- Molecular basis for diversification of yeast prion strain conformation. (26 citations)
- Structure and mechanism of cancer-associated N -acetylglucosaminyltransferase-V (25 citations)
- Characterization of Conformational Ensembles of Protonated N-glycans in the Gas-Phase. (23 citations)
In his most recent research, the most cited papers focused on:
Yoshiki Yamaguchi mainly focuses on Biochemistry, Glycosylation, Glycan, Glycosyltransferase and Plasma protein binding.
All of his Biochemistry and Glycolipid, Lectin and In vitro investigations are sub-components of the entire Biochemistry study.
As part of the same scientific family, Yoshiki Yamaguchi usually focuses on Lectin, concentrating on Antibody and intersecting with Cell biology.
His Glycosylation research integrates issues from Antibody-drug conjugate, Amide, Oxazoline, Fucose and Combinatorial chemistry.
Glycan is a subfield of Glycoprotein that Yoshiki Yamaguchi explores.
His work deals with themes such as Golgi apparatus and Transferase, which intersect with Plasma protein binding.
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