Glycoinformatics
390 views | +0 today
Follow
Your new post is loading...
Your new post is loading...
Scooped by Bernard Offmann
Scoop.it!

Glycoinformatics book at Springer

Glycoinformatics book at Springer | Glycoinformatics | Scoop.it

Editors: Lütteke Thomas & Frank Martin (Eds.)

 

This book provides current glycoinformatics methods and protocols used to support the determination of carbohydrate structures in biological samples as well as carbohydrate structure databases, the interaction of carbohydrates with proteins, and theoretical and experimental methods to study their three-dimensional structure and dynamics. Glycoinformatics explores this recently emerged field, which has come into being in order to address the needs of encoding, storing, and analyzing carbohydrate ‘sequences’ and their taxonomy using computers. Written in the highly successful Methods in Molecular Biology series format, chapters contain the kind of detailed description and key implementation advice to ensure successful results.

 

Authoritative and timely, Glycoinformatics demonstrates the progress that has been achieved in glycoinformatics, which indicates that it is no longer a niche subject covered by only a few scientists but is truly coming of age.

Bernard Offmann's insight:

Definitely, I'm ordering the book for my lab !

more...
No comment yet.
Scooped by Bernard Offmann
Scoop.it!

A Method for In-Depth Structural Annotation of Human Serum Glycans That Yields Biological Variations

A Method for In-Depth Structural Annotation of Human Serum Glycans That Yields Biological Variations | Glycoinformatics | Scoop.it

Ting Song , Danielle Aldredge , and Carlito B. Lebrilla


Abstract

Glycosylation is an important post-translational modification of proteins present in the vast majority of human proteins. For this reason, they are potentially new sources of biomarkers and active targets of therapeutics and vaccines. However, the absence of a biosynthetic template as in the genome and the general complexity of the structures have limited the development of methods for comprehensive structural analysis. Even now, the exact structures of many abundant N-glycans in serum are not known. Structural elucidation of oligosaccharides remains difficult and time-consuming. Here, we introduce a means of rapidly identifying released N-glycan structures using their accurate masses and retention times based on a glycan library. This serum glycan library, significantly expanded from a previous one covering glycans released from a handful of serum glycoproteins, has more than 170 complete and partial structures and constructed instead from whole serum. The method employs primarily nanoflow liquid chromatography and accurate mass spectrometry. The method allows us to readily profile N-glycans in biological fluids with deep structural analysis. This approach is used to determine the relative abundances and variations in the N-glycans from several individuals providing detailed variations in the abundances of the important N-glycans in blood.

more...
No comment yet.
Scooped by Bernard Offmann
Scoop.it!

Pioneer from France receives the Novozymes Prize | Novo Nordisk Fonden

Pioneer from France receives the Novozymes Prize | Novo Nordisk Fonden | Glycoinformatics | Scoop.it
Bernard Offmann's insight:

Bernard Henrissat is receiving the Novozymes Prize for pioneering research on characterizing and systematizing enzymes.

more...
No comment yet.
Scooped by Bernard Offmann
Scoop.it!

Recent advances in employing molecular modelling to determine the specificity of glycan-binding proteins

Recent advances in employing molecular modelling to determine the specificity of glycan-binding proteins | Glycoinformatics | Scoop.it

Impressive improvements in docking performance can be achieved by applying energy bonuses to poses in which glycan hydroxyl groups occupy positions otherwise preferred by bound waters. In addition, inclusion of glycosidic conformational energies allows unlikely glycan conformations to be appropriately penalized. A method for predicting the binding specificity of glycan-binding proteins has been developed, which is based on grafting glycan branches onto a minimal binding determinant in the binding site. Grafting can be used either to screen virtual libraries of glycans, such as the known glycome, or to identify docked poses of minimal binding determinants that are consistent with specificity data. The reviewed advances allow accurate modelling of carbohydrate-protein 3D co-complexes, but challenges remain in ranking the affinity of congeners.

more...
No comment yet.
Scooped by Bernard Offmann
Scoop.it!

X marks the spot: Does it matter that O-GlcNAc Transferase is an X-linked gene?

X marks the spot: Does it matter that O-GlcNAc Transferase is an X-linked gene? | Glycoinformatics | Scoop.it
X marks the spot: Does it matter that O-GlcNAc Transferase is an X-linked gene?Abstract

O-GlcNAcylation has emerged as a critical post-translational modification important for a wide array of cellular processes. This modification has been identified on a large pool of intracellular proteins that have wide-ranging roles, including transcriptional regulation, cell cycle progression, and signaling, among others. Interestingly, in mammals the single gene encoding O-GlcNAc Transferase (OGT) is located on the X-chromosome near the Xist locus suggesting that tight dosage regulation is necessary for normal development. Herein, we highlight the importance of OGT dosage and consider how its genomic location can contribute to a gender-specific increased risk for a number of diseases.

more...
No comment yet.
Scooped by Bernard Offmann
Scoop.it!

A systematic study of chemogenomics of carbohydrates

A systematic study of chemogenomics of carbohydrates | Glycoinformatics | Scoop.it

Authors : Gu J, Luo F, Chen L, Yuan G, Xu X.

 

Abstract 

 

Chemogenomics focuses on the interactions between biologically active molecules and protein targets for drug discovery. Carbohydrates are the most abundant compounds in natural products. Compared with other drugs, the carbohydrate drugs show weaker side effects. Searching for multi-target carbohydrate drugs can be regarded as a solution to improve therapeutic efficacy and safety. In this work, we collected 60344 carbohydrates from the Universal Natural Products Database (UNPD) and explored the chemical space of carbohydrates by principal component analysis. We found that there is a large quantity of potential lead compounds among carbohydrates. Then we explored the potential of carbohydrates in drug discovery by using a network-based multi-target computational approach. All carbohydrates were docked to 2389 target proteins. The most potential carbohydrates for drug discovery and their indications were predicted based on a docking score-weighted prediction model. We also explored the interactions between carbohydrates and target proteins to find the pathological networks, potential drug candidates and new indications.

Bernard Offmann's insight:

This is a typical example of usefulness computational approaches in the field of glycobiology. I'm impressed by the amount of work the authors seem to have performed. However, it is known that docking of carbohydrates on proteins is not a trivial problem due to weak interactions and their inherent flexibility. The authors does not seem to discuss how they address these issues. 

more...
No comment yet.
Rescooped by Bernard Offmann from Bio-informatics
Scoop.it!

Understanding the interactions between bacteria in the human gut through metabolic modeling

Understanding the interactions between bacteria in the human gut through metabolic modeling | Glycoinformatics | Scoop.it
The human gut microbiome plays an influential role in maintaining human health, and it is a potential target for prevention and treatment of disease.

Via Dmitry Alexeev, Loiret David
more...
Dmitry Alexeev's curator insight, October 4, 2013 6:14 AM

little bit on metabolomic modelling from gurus. Surprising is the journal chosen for that

Scooped by Bernard Offmann
Scoop.it!

Chemical Glycobiology - Carolyn Bertozzi - iBioSeminars (iBiology)

Chemical Glycobiology - Carolyn Bertozzi - iBioSeminars (iBiology) | Glycoinformatics | Scoop.it

Part 1
A large part of an organism’s complexity is not encoded by its genome but results from post-translational modification. Glycosylation, or the addition of sugar molecules to a protein is an example of such a modification. These sugars, or glycans, are often complex, branched molecules specific to particular cells. Cell surface glycans determine human blood types, allow viral infections and play a key role in tissue inflammation.

Part 2
Since glycans cannot be labeled with genetically-encoded reporters such as GFP, bioorthoganal reactions have been developed to allow their labeling and imaging. In this lecture, Bertozzi describes the chemistry and imaging methodology used to view glycoproteins in cells and whole organisms.

- See more at: http://www.ibiology.org/ibioseminars/biophysics-chemical-biology/carolyn-bertozzi-part-1.html#sthash.v5ME7HKx.dpuf

 

 

Bernard Offmann's insight:

The current URL links to a Podcast on iTunes. You can watch on Youtube at http://www.youtube.com/watch?v=WCbg-kOY_8E

Otherwise check on the original iBio website : http://www.ibiology.org/ibioseminars/biophysics-chemical-biology/carolyn-bertozzi-part-1.html

 

more...
No comment yet.
Rescooped by Bernard Offmann from directed evolution
Scoop.it!

Combinatorial Engineering of Dextransucrase Specificity

Combinatorial Engineering of Dextransucrase Specificity | Glycoinformatics | Scoop.it

We used combinatorial engineering to investigate the relationships between structure and linkage specificity of the dextransucrase DSR-S from Leuconostoc mesenteroides NRRL B-512F, and to generate variants with altered specificity. Sequence and structural analysis of glycoside-hydrolase family 70 enzymes led to eight amino acids (D306, F353, N404, W440, D460, H463, T464 and S512) being targeted, randomized by saturation mutagenesis and simultaneously recombined. Screening of two libraries totaling 3.6.104 clones allowed the isolation of a toolbox comprising 81 variants which synthesize high molecular weight α-glucans with different proportions of α(1→3) linkages ranging from 3 to 20 %. Mutant sequence analysis, biochemical characterization and molecular modelling studies revealed the previously unknown role of peptide 460DYVHT464 in DSR-S linkage specificity. This peptide sequence together with residue S512 contribute to defining +2 subsite topology, which may be critical for the enzyme regiospecificity.


Via Anna Nikulina
more...
No comment yet.
Scooped by Bernard Offmann
Scoop.it!

Structural investigation of multivalent carbohydrate–protein interactions using synthetic biomolecules

Valentin Wittmann

Understanding multivalent carbohydrate–protein interactions at the molecular level requires access to structural details of these important biological recognition processes. Recent developments toward this goal comprise the use of conformationally defined molecular rulers in combination with binding assays, crystallographic investigation of complexes of multivalent ligands and their target proteins, and distance measurements in the nanometer range by EPR spectroscopy.

more...
No comment yet.
Scooped by Bernard Offmann
Scoop.it!

The Carbohydrate-Binding Site in Galectin-3 Is Preorganized To Recognize a Sugarlike Framework of Oxygens: Ultra-High-Resolution Structures and Water Dynamics - Biochemistry (ACS Publications)

The Carbohydrate-Binding Site in Galectin-3 Is Preorganized To Recognize a Sugarlike Framework of Oxygens: Ultra-High-Resolution Structures and Water Dynamics - Biochemistry (ACS Publications) | Glycoinformatics | Scoop.it

Kadhirvel Saraboji, Maria Håkansson, Samuel Genheden, Carl Diehl, Johan Qvist, Ulrich Weininger, Ulf J Nilsson, Hakon Leffler, Ulf Ryde, Mikael Akke, and Derek T Logan

 

The recognition of carbohydrates by proteins is a fundamental aspect of communication within and between living cells. Understanding the molecular basis of carbohydrate–protein interactions is a prerequisite for the rational design of synthetic ligands. Here we report the high- to ultra-high-resolution crystal structures of the carbohydrate recognition domain of galectin-3 (Gal3C) in the ligand-free state (1.08 Å at 100 K, 1.25 Å at 298 K) and in complex with lactose (0.86 Å) or glycerol (0.9 Å). These structures reveal striking similarities in the positions of water and carbohydrate oxygen atoms in all three states, indicating that the binding site of Gal3C is preorganized to coordinate oxygen atoms in an arrangement that is nearly optimal for the recognition of β-galactosides. Deuterium nuclear magnetic resonance (NMR) relaxation dispersion experiments and molecular dynamics simulations demonstrate that all water molecules in the lactose-binding site exchange with bulk water on a time scale of nanoseconds or shorter. Nevertheless, molecular dynamics simulations identify transient water binding at sites that agree well with those observed by crystallography, indicating that the energy landscape of the binding site is maintained in solution. All heavy atoms of glycerol are positioned like the corresponding atoms of lactose in the Gal3C complexes. However, binding of glycerol to Gal3C is insignificant in solution at room temperature, as monitored by NMR spectroscopy or isothermal titration calorimetry under conditions where lactose binding is readily detected. These observations make a case for protein cryo-crystallography as a valuable screening method in fragment-based drug discovery and further suggest that identification of water sites might inform inhibitor design.

Bernard Offmann's insight:

Absolutely awesome paper on recognition of sugars by galectines.

more...
No comment yet.
Scooped by Bernard Offmann
Scoop.it!

GS-align for glycan structure alignment and similarity measurement

Hui Sun Lee, Sunhwan Jo, Srayanta Mukherjee, Sang-Jun Park, Jeffrey Skolnick, Jooyoung Lee, and Wonpil Im


Bioinformatics 2015 31: 2653-2659


Motivation: 

Glycans play critical roles in many biological processes, and their structural diversity is key for specific protein-glycan recognition. Comparative structural studies of biological molecules provide useful insight into their biological relationships. However, most computational tools are designed for protein structure, and despite their importance, there is no currently available tool for comparing glycan structures in a sequence order- and size-independent manner.

 

Results: 

A novel method, GS-align, is developed for glycan structure alignment and similarity measurement. GS-align generates possible alignments between two glycan structures through iterative maximum clique search and fragment superposition. The optimal alignment is then determined by the maximum structural similarity score, GS-score, which is size-independent. Benchmark tests against the Protein Data Bank (PDB) N-linked glycan library and PDB homologous/non-homologous N-glycoprotein sets indicate that GS-align is a robust computational tool to align glycan structures and quantify their structural similarity. GS-align is also applied to template-based glycan structure prediction and monosaccharide substitution matrix generation to illustrate its utility.


Availability and implementation: http://www.glycanstructure.org/gsalign.


Contact: wonpil@ku.edu


Supplementary information: Supplementary data are available at Bioinformatics online.

Bernard Offmann's insight:

Nice paper on a long awaited method to identify glycans. 

more...
No comment yet.
Scooped by Bernard Offmann
Scoop.it!

Three-dimensional representations of complex carbohydrates and polysaccharides—SweetUnityMol: A video game-based computer graphic software

Serge Pérez, Thibault Tubiana, Anne Imberty, and Marc Baaden 

 

Glycobiology 2015 25: 483-491

 

Abstract

A molecular visualization program tailored to deal with the range of 3D structures of complex carbohydrates and polysaccharides, either alone or in their interactions with other biomacromolecules, has been developed using advanced technologies elaborated by the video games industry. All the specific structural features displayed by the simplest to the most complex carbohydrate molecules have been considered and can be depicted. This concerns the monosaccharide identification and classification, conformations, location in single or multiple branched chains, depiction of secondary structural elements and the essential constituting elements in very complex structures. Particular attention was given to cope with the accepted nomenclature and pictorial representation used in glycoscience. This achievement provides a continuum between the most popular ways to depict the primary structures of complex carbohydrates to visualizing their 3D structures while giving the users many options to select the most appropriate modes of representations including new features such as those provided by the use of textures to depict some molecular properties. These developments are incorporated in a stand-alone viewer capable of displaying molecular structures, biomacromolecule surfaces and complex interactions of biomacromolecules, with powerful, artistic and illustrative rendering methods. They result in an open source software compatible with multiple platforms, i.e., Windows, MacOS and Linux operating systems, web pages, and producing publication-quality figures. The algorithms and visualization enhancements are demonstrated using a variety of carbohydrate molecules, from glycan determinants to glycoproteins and complex protein–carbohydrate interactions, as well as very complex mega-oligosaccharides and bacterial polysaccharides and multi-stranded polysaccharide architectures.

Bernard Offmann's insight:

Wow... Simply very cool !!!

more...
No comment yet.
Scooped by Bernard Offmann
Scoop.it!

Controlled glycosylation of plant-produced recombinant proteins

Richard Strasser, Friedrich Altmann and Herta Steinkellner

 

Despite their recognized importance for therapeutic proteins, the production of structurally defined glycans is still a challenging issue. However, an increased understanding of glycosylation pathways, recent advances in analytical tools, and emerging technologies for subcellular targeting using chimeric glycosyltransferases are facilitating the rational design of new glycan biosynthetic pathways. Plants are particularly amenable to glyco-engineering approaches and thus they are increasingly being used for the production of recombinant proteins. Here we summarize the main achievements in the field of in planta glyco-engineering for the production of therapeutically relevant proteins.

 

In Current Opinion in Biotechnology 2014, 30:95–100

 

 
more...
No comment yet.
Scooped by Bernard Offmann
Scoop.it!

An Atypical Orphan Carbohydrate-NRPS Genomic Island Encodes a Novel Lytic Transglycosylase

An Atypical Orphan Carbohydrate-NRPS Genomic Island Encodes a Novel Lytic Transglycosylase | Glycoinformatics | Scoop.it
Summary

Microbial genome sequencing platforms have produced a deluge of orphan biosynthetic pathways suspected of biosynthesizing new small molecules with pharmacological relevance. Genome synteny analysis provides an assessment of genomic island content, which is enriched in natural product gene clusters. Here we identified an atypical orphan carbohydrate-nonribosomal peptide synthetase genomic island in Photorhabdus luminescens using genome synteny analysis. Heterologous expression of the pathway led to the characterization of five oligosaccharide metabolites with lysozyme inhibitory activities. The oligosaccharides harbor a 1,6-anhydro-β-D-N-acetyl-glucosamine moiety, a rare structural feature for natural products. Gene deletion analysis and biochemical reconstruction of oligosaccharide production led to the discovery that a hypothetical protein in the pathway is a lytic transglycosylase responsible for bicyclic sugar formation. The example presented here supports the notion that targeting select genomic islands with reduced reliance on known protein homologies could enhance the discovery of new metabolic chemistry and biology.

 

 
more...
No comment yet.
Scooped by Bernard Offmann
Scoop.it!

Integrative Glycobiology and Future Perspectives

Given the fact that over 50% of proteins in eukaryotes are glycosylated, it should be no surprise that the field of glycoscience is now one of the most important fields of research in science. The NAS report on “Transforming Glycoscience: the roadmap in the future” published in 2013 highlights the significance and importance of glycoscience in the future, and it is now clear that glycoscience will have an impact on both basic science and applied science in the fields of glycobiology and glycotechnology.

 
Bernard Offmann's insight:

Very informative editorial from Naoyuki Taniguchi.

more...
No comment yet.
Scooped by Bernard Offmann
Scoop.it!

Comparative simulation of pneumococcal serogroup 19 polysaccharide repeating units with two carbohydrate force fields

Comparative simulation of pneumococcal serogroup 19 polysaccharide repeating units with two carbohydrate force fields | Glycoinformatics | Scoop.it
Abstract

Streptococcus pneumoniae causes meningitis, pneumonia, and severe invasive disease (IPD) in young children. Although widespread infant immunisation with the PCV7 seven-valent pneumococcal conjugate vaccine has led to a dramatic decrease in IPD, infections due to non-vaccine serotypes, particularly serotype 19A, have increased. As the 19F polysaccharide differs from 19A at a single linkage position, it was assumed that PCV7 (containing 19F) would cross-protect against 19A disease. However, vaccination with PCV7 results in only 26% effectiveness against IPD caused by 19A. We explored the conformations and dynamics of the polysaccharide repeating units from serotypes 19F and 19A, comparing free energy surfaces for glycosidic linkages with 100 ns aqueous Molecular Dynamics simulations of the di- and trisaccharide components. All calculations were performed with both the CHARMM and the GLYCAM carbohydrate force fields to establish whether the choice of model affects the predicted molecular behaviour. Although we identified key differences between the force fields, overall they were in agreement in predicting a 19F repeating unit with a wider range of conformation families than the more restricted 19A trisaccharide. This suggests a probable conformational difference between the 19F and 19A polysaccharides, which may explain the low cross-protection of 19F vaccines against 19A disease.

more...
No comment yet.
Rescooped by Bernard Offmann from Protein folds and folding
Scoop.it!

Glycoprotein folding and quality-control mechanisms in protein-folding diseases

Glycoprotein folding and quality-control mechanisms in protein-folding diseases | Glycoinformatics | Scoop.it

Ferris SP, Kodali VK, Kaufman RJ.

 

ABSTRACT 


Biosynthesis of proteins - from translation to folding to export - encompasses a complex set of events that are exquisitely regulated and scrutinized to ensure the functional quality of the end products. Cells have evolved to capitalize on multiple post-translational modifications in addition to primary structure to indicate the folding status of nascent polypeptides to the chaperones and other proteins that assist in their folding and export. These modifications can also, in the case of irreversibly misfolded candidates, signal the need for dislocation and degradation. The current Review focuses on the glycoprotein quality-control (GQC) system that utilizes protein N-glycosylation and N-glycan trimming to direct nascent glycopolypeptides through the folding, export and dislocation pathways in the endoplasmic reticulum (ER). A diverse set of pathological conditions rooted in defective as well as over-vigilant ER quality-control systems have been identified, underlining its importance in human health and disease. We describe the GQC pathways and highlight disease and animal models that have been instrumental in clarifying our current understanding of these processes.

Bernard Offmann's insight:

Very original review !!

more...
Bernard Offmann's curator insight, March 15, 2014 5:13 PM

Very original review !

Scooped by Bernard Offmann
Scoop.it!

The Challenge and Promise of Glycomics

Glycomics is a broad and emerging scientific discipline focused on defining the structures and functional roles of glycans in biological systems. The staggering complexity of the glycome, minimally defined as the repertoire of glycans expressed in a cell or organism, has resulted in many challenges that must be overcome; these are being addressed by new advances in mass spectrometry as well as by the expansion of genetic and cell biology studies. Conversely, identifying the specific glycan recognition determinants of glycan-binding proteins by employing the new technology of glycan microarrays is providing insights into how glycans function in recognition and signaling within an organism and with microbes and pathogens. The promises of a more complete knowledge of glycomes are immense in that glycan modifications of intracellular and extracellular proteins have critical functions in almost all biological pathways.

Bernard Offmann's insight:

Very interesting review from Richard Cummings.

more...
No comment yet.
Scooped by Bernard Offmann
Scoop.it!

Synthesis of sialic acid-containing saccharides

Avijit K Adak, Ching-Ching Yu, Chien-Fu Liang, Chun-Cheng Lin

Sialic acids are a diverse family of negatively charged monosaccharides with a shared nine-carbon carboxylated backbone, and they often serve as the terminal positions of cell surface glycoproteins and glycolipids. Sialic acids play essential roles in mediating or modulating numerous pathological, biological, and immunological recognition events. Advances in synthesis have provided chemically well-defined and structurally homogeneous sialic acid-containing carbohydrates that are crucial for studying glycobiology. This review highlights recent innovations in the chemical and chemoenzymatic synthesis of difficult α-sialosides, with a particular focus on methods developed for α-selective sialylation in the synthesis of O-linked and S-linked oligosialic acids.

Bernard Offmann's insight:

A very interesting review.

more...
No comment yet.
Scooped by Bernard Offmann
Scoop.it!

Context and complexity: The next big thing in synthetic glycobiology

Todd L Lowary

Complex glycans participate in many essential life processes. Studies of glycan-mediated biological events have traditionally employed structurally defined fragments of the more elaborate natural molecules. However, it is now clear that this approach may sometimes be insufficient and this realization has prompted a desire to synthesize glycans of similar size and complexity to those found in nature. We highlight here recent work describing the synthesis of such molecules.

more...
No comment yet.
Scooped by Bernard Offmann
Scoop.it!

Deciphering the Glycan Preference of Bacterial Lectins by Glycan Array and Molecular Docking with Validation by Microcalorimetry and Crystallography

Deciphering the Glycan Preference of Bacterial Lectins by Glycan Array and Molecular Docking with Validation by Microcalorimetry and Crystallography | Glycoinformatics | Scoop.it

Recent advances in glycobiology revealed the essential role of lectins for deciphering the glycocode by specific recognition of carbohydrates. Integrated multiscale approaches are needed for characterizing lectin specificity: combining on one hand high-throughput analysis by glycan array experiments and systematic molecular docking of oligosaccharide libraries and on the other hand detailed analysis of the lectin/oligosaccharide interaction by x-ray crystallography, microcalorimetry and free energy calculations. The lectins LecB fromPseudomonas aeruginosa and BambL from Burkholderia ambifaria are part of the virulence factors used by the pathogenic bacteria to invade the targeted host. These two lectins are not related but both recognize fucosylated oligosaccharides such as the histo-blood group oligosaccharides of the ABH(O) and Lewis epitopes. The specificities were characterized using semi-quantitative data from glycan array and analyzed by molecular docking with the Glide software. Reliable prediction of protein/oligosaccharide structures could be obtained as validated by existing crystal structures of complexes. Additionally, the crystal structure of BambL/Lewis x was determined at 1.6 Å resolution, which confirms that Lewis x has to adopt a high-energy conformation so as to bind to this lectin. Free energies of binding were calculated using a procedure combining the Glide docking protocol followed by free energy rescoring with the Prime/Molecular Mechanics Generalized Born Surface Area (MM-GBSA) method. The calculated data were in reasonable agreement with experimental free energies of binding obtained by titration microcalorimetry. The established predictive protocol is proposed to rationalize large sets of data such as glycan arrays and to help in lead discovery projects based on such high throughput technology

Bernard Offmann's insight:

Very interesting paper from Anne Imberty and her team about lectin/carbohydrate recognition.

more...
No comment yet.