記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1007/s12551-020-00698-1

記述言語：その他   掲載種別：研究論文（学術雑誌）  

DOI： 10.3390/ijms21010147

記述言語：英語  

DOI： 10.1038/s41598-019-48323-w

記述言語：その他   掲載種別：研究論文（学術雑誌）  

DOI： 10.3390/antib8030039

記述言語：その他   掲載種別：研究論文（学術雑誌）  

DOI： 10.1007/s10858-018-0169-2

記述言語：その他   掲載種別：研究論文（学術雑誌）  

DOI： 10.3390/molecules22101619

記述言語：英語   掲載種別：研究論文（学術雑誌）   出版者・発行元：Journal of bacteriology  

Members of the kingdom Nanobdellati, previously known as DPANN archaea, are characterized by ultrasmall cell sizes and reduced genomes. They primarily thrive through ectosymbiotic interactions with specific hosts in diverse environments. Recent successful cultivations have emphasized the importance of adhesion to host cells for understanding the ecophysiology of Nanobdellati. Cell adhesion is often mediated by cell surface carbohydrates, and in archaea, this may be facilitated by the glycosylated S-layer protein that typically coats their cell surface. In this study, we conducted glycoproteomic analyses on two co-cultures of Nanobdellati with their host archaea, as well as on pure cultures of both host and non-host archaea. Nanobdellati exhibited various glycoproteins, including archaellins and hypothetical proteins, with glycans that were structurally distinct from those of their hosts. This indicated that Nanobdellati autonomously synthesize their glycans for protein modifications probably using host-derived substrates, despite the high energy cost. Glycan modifications on Nanobdellati proteins consistently occurred on asparagine residues within the N-X-S/T sequon, consistent with patterns observed across archaea, bacteria, and eukaryotes. In both host and non-host archaea, S-layer proteins were commonly modified with hexose, N-acetylhexosamine, and sulfonated deoxyhexose. However, the N-glycan structures of host archaea, characterized by distinct sugars such as deoxyhexose, nonulosonate sugar, and pentose at the nonreducing ends, were implicated in enabling Nanobdellati to differentiate between host and non-host cells. Interestingly, the specific sugar, xylose, was eliminated from the N-glycan in a host archaeon when co-cultured with Nanobdella. These findings enhance our understanding of the role of protein glycosylation in archaeal interactions.IMPORTANCENanobdellati archaea, formerly known as DPANN, are phylogenetically diverse, widely distributed, and obligately ectosymbiotic. The molecular mechanisms by which Nanobdellati recognize and adhere to their specific hosts remain largely unexplored. Protein glycosylation, a fundamental biological mechanism observed across all domains of life, is often crucial for various cell-cell interactions. This study provides the first insights into the glycoproteome of Nanobdellati and their host and non-host archaea. We discovered that Nanobdellati autonomously synthesize glycans for protein modifications, probably utilizing substrates derived from their hosts. Additionally, we identified distinctive glycosylation patterns that suggest mechanisms through which Nanobdellati differentiate between host and non-host cells. This research significantly advances our understanding of the molecular basis of microbial interactions in extreme environments.

DOI： 10.1128/jb.00205-24

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DOI： 10.1101/2024.05.11.593658

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記述言語：その他   掲載種別：研究論文（学術雑誌）   出版者・発行元：International Immunology  

Abstract

IgG molecules that bind antigen on the membrane of target cells spontaneously form hexameric rings, thus recruiting C1 to initiate the complement pathway. However, our previous report indicated that a mouse IgG mutant lacking the Cγ1 domain activates the pathway independently of antigen presence through its monomeric interaction with C1q via the CL domain, as well as Fc. In this study, we investigated the potential interaction between C1q and human CL isoforms. Quantitative single molecule observations using high-speed atomic force microscopy revealed that human Cκ exhibited comparable C1q binding capabilities with its mouse counterpart, surpassing the Cλ types, which have a higher isoelectric point than the Cκ domains. Nuclear magnetic resonance and mutation experiments indicated that the human and mouse Cκ domains share a common primary binding site for C1q, centered on Glu194, a residue conserved in the Cκ domains but absent in the Cλ domains. Additionally, the Cγ1 domain, with its high isoelectric point, can cause electrostatic repulsion to the C1q head and impede the C1q-interaction adjustability of the Cκ domain in Fab. The removal of the Cγ1 domain is considered to eliminate these factors and thus promote Cκ interaction with C1q with the potential risk of uncontrolled activation of the complement pathway in vivo in the absence of antigen. However, this research underscores the presence of potential subsites in Fab for C1q binding, offering promising targets for antibody engineering to refine therapeutic antibody design.

DOI： 10.1093/intimm/dxae017

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記述言語：英語   掲載種別：研究論文（学術雑誌）   出版者・発行元：公益社団法人 日本薬学会  

This study employed high-speed atomic force microscopy to quantitatively analyze the interactions between therapeutic antibodies and Fcγ receptors (FcγRs). Antibodies are essential components of the immune system and are integral to biopharmaceuticals. The focus of this study was on immunoglobulin G molecules, which are crucial for antigen binding via the Fab segments and cytotoxic functions through their Fc portions. We conducted real-time, label-free observations of the interactions of rituximab and mogamulizumab with the recombinant FcγRIIIa and FcγRIIa. The dwell times of FcγR binding were measured at the single-molecule level, which revealed an extended interaction duration of mogamulizumab with FcγRIIIa compared with that of rituximab. This is linked to enhanced antibody-dependent cellular cytotoxicity that is attributed to the absence of the core fucosylation of Fc-linked N-glycan. This study also emphasizes the crucial role of the Fab segments in the interaction with FcγRIIa as well as that with FcγRIIIa. This approach provided quantitative insight into therapeutic antibody interactions and exemplified kinetic proofreading, where cellular discrimination relies on ligand residence times. Observing the dwell times of antibodies on the effector molecules has emerged as a robust indicator of therapeutic antibody efficacy. Ultimately, these findings pave the way for the development of refined therapeutic antibodies with tailored interactions with specific FcγRs. This research contributes to the advancement of biopharmaceutical antibody design and optimizing antibody-based treatments for enhanced efficacy and precision.

DOI： 10.1248/bpb.b23-00751

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記述言語：英語   出版者・発行元：(公社)日本薬学会  

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記述言語：英語   掲載種別：研究論文（学術雑誌）   出版者・発行元：BBA Advances  

Archaeal cells are typically enveloped by glycosylated S-layer proteins. Archaeal protein glycosylation provides valuable insights not only into their adaptation to their niches but also into their evolutionary trajectory. Notably, thermophilic Thermoproteota modify proteins with N-glycans that include two GlcNAc units at the reducing end, resembling the "core structure" preserved across eukaryotes. Recently, Asgard archaea, now classified as members of the phylum Promethearchaeota, have offered unprecedented opportunities for understanding the role of archaea in eukaryogenesis. Despite the presence of genes indicative of protein N-glycosylation in this archaeal group, these have not been experimentally investigated. Here we performed a glycoproteome analysis of the firstly isolated Asgard archaeon Promethearchaeum syntrophicum. Over 700 different proteins were identified through high-resolution LC-MS/MS analysis, however, there was no evidence of either the presence or glycosylation of putative S-layer proteins. Instead, N-glycosylation in this archaeon was primarily observed in an extracellular solute-binding protein, possibly related to chemoreception or transmembrane transport of oligopeptides. The glycan modification occurred on an asparagine residue located within the conserved N-X-S/T sequon, consistent with the pattern found in other archaea, bacteria, and eukaryotes. Unexpectedly, three structurally different N-glycans lacking the conventional core structure were identified in this archaeon, presenting unique compositions that included atypical sugars. Notably, one of these sugars was likely HexNAc modified with a threonine residue, similar to modifications previously observed in mesophilic methanogens within the Methanobacteriati. Our findings advance our understanding of Asgard archaea physiology and evolutionary dynamics.

DOI： 10.1016/j.bbadva.2024.100118

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記述言語：日本語   出版者・発行元：公益社団法人 日本生物工学会  

DOI： 10.34565/seibutsukogaku.101.7_347

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記述言語：その他   掲載種別：研究論文（学術雑誌）   出版者・発行元：International Journal of Molecular Sciences  

In multidomain proteins, individual domains connected by flexible linkers are dynamically rearranged upon ligand binding and sensing changes in environmental factors, such as pH and temperature. Here, we characterize dynamic domain rearrangements of Lys48-linked ubiquitin (Ub) chains as models of multidomain proteins in which molecular surfaces mediating intermolecular interactions are involved in intramolecular domain–domain interactions. Using NMR and other biophysical techniques, we characterized dynamic conformational interconversions of diUb between open and closed states regarding solvent exposure of the hydrophobic surfaces of each Ub unit, which serve as binding sites for various Ub-interacting proteins. We found that the hydrophobic Ub-Ub interaction in diUb was reinforced by cysteine substitution of Lys48 of the distal Ub unit because of interaction between the cysteinyl thiol group and the C-terminal segment of the proximal Ub unit. In contrast, the replacement of the isopeptide linker with an artificial ethylenamine linker minimally affected the conformational distributions. Furthermore, we demonstrated that the mutational modification allosterically impacted the exposure of the most distal Ub unit in triUb. Thus, the conformational interconversion of Ub chains offers a unique design framework in Ub-based protein engineering not only for developing biosensing probes but also for allowing new opportunities for the allosteric regulation of multidomain proteins.

DOI： 10.3390/ijms24076075

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記述言語：英語   掲載種別：研究論文（学術雑誌）   出版者・発行元：Protein Science  

The characterization of residual structures persistent in unfolded proteins is an important issue in studies of protein folding, because the residual structures present, if any, may form a folding initiation site and guide the subsequent folding reactions. Here, we studied the residual structures of the isolated B domain (BDPA) of staphylococcal protein A in 6 M guanidinium chloride. BDPA is a small three-helix-bundle protein, and until recently its folding/unfolding reaction has been treated as a simple two-state process between the native and the fully unfolded states. We employed a dimethylsulfoxide (DMSO)-quenched hydrogen/deuterium (H/D)-exchange 2D NMR techniques with the use of spin desalting columns, which allowed us to investigate the H/D-exchange behavior of individually identified peptide amide (NH) protons. We obtained H/D-exchange protection factors of the 21 NH protons that form an α-helical hydrogen bond in the native structure, and the majority of these NH protons were significantly protected with a protection factor of 2.0-5.2 in 6 M guanidinium chloride, strongly suggesting that these weakly protected NH protons form much stronger hydrogen bonds under native folding conditions. The results can be used to deduce the structure of an early folding intermediate, when such an intermediate is shown by other methods. Among three native helical regions, the third helix in the C-terminal side was highly protected and stabilized by side-chain salt bridges, probably acting as the folding initiation site of BDPA. The present results are discussed in relation to previous experimental and computational findings on the folding mechanisms of BDPA. This article is protected by copyright. All rights reserved.

DOI： 10.1002/pro.4569

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記述言語：その他   掲載種別：研究論文（学術雑誌）   出版者・発行元：mAbs  

The interaction between IgG and Fc gamma receptor IIIa (FcγRIIIa) is essential for mediating immune responses. Recent studies have shown that the antigen binding fragment (Fab) and Fc are involved in IgG-FcγRIII interactions. Here, we conducted bio-layer interferometry (BLI) and isothermal titration calorimetry to measure the kinetic and thermodynamic parameters that define the role of Fab in forming the IgG-FcγRIII complex using several marketed therapeutic antibodies. Moreover, hydrogen/deuterium exchange mass spectrometry (HDX-MS) and crosslinking mass spectrometry (XL-MS) were used to clarify the interaction sites and structural changes upon formation of these IgG-FcγRIII complexes. The results showed that Fab in IgG facilitates the interaction via slower dissociation and a larger enthalpy gain. However, a larger entropy loss led to only a marginal change in the equilibrium dissociation constant. Combined HDX-MS and XL-MS analysis revealed that the CL domain of Fab in IgG was in close proximity to FcγRIIIa, indicating that this domain specifically interacts with the extracellular membrane-distal domain (D1) and membrane-proximal domain (D2) of FcγRIIIa. Together with previous studies, these results demonstrate that IgG-FcγRIII interactions are predominantly mediated by the binding of Fc to D2, and the Fab-FcγRIII interaction stabilizes complex formation. These interaction schemes were essentially fucosylation-independent, with Fc-D2 interactions enhanced by afucosylation and the contribution of Fab slightly reduced. Furthermore, the influence of antigen binding on IgG-FcγRIII interactions was also investigated. Combined BLI and HDX-MS results indicate that structural alterations in Fab caused by antigen binding facilitate stabilization of IgG-FcγRIII interactions. This report provides a comprehensive understanding of the interaction between IgG and FcγRIII.

DOI： 10.1080/19420862.2022.2038531

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記述言語：英語   掲載種別：研究論文（学術雑誌）   出版者・発行元：Trends in Glycoscience and Glycotechnology  

The three-dimensional glycan structures dynamically fluctuate in aqueous solutions. The dynamics of these molecular structures govern the interactions with sugar-recognizing molecules and are deeply involved in regulating the functions of sugar-bearing proteins. In glycotechnology and drug discovery targeting the glycan recognition systems, it is crucial to quantitatively understand the conformation of glycans bound to target molecules and the three-dimensional structural dynamics of unbound glycans. By modifying the conformational space of unbound glycans, it is possible to improve their affinity for lectins. Furthermore, the glycans constituting a glycoprotein also influence the conformational dynamics of the protein part. Therefore, in the molecular design of glycoproteins aiming for higher functionality, it is essential to consider the existence of an intramolecular interaction network where the glycan chains and the protein are integrated. Approaches from the perspective of experimental science, computational science, and information science will become increasingly important to decipher the biological information carried by the four-dimensional structures of glycans.

DOI： 10.4052/tigg.2042.1e

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記述言語：英語   掲載種別：研究論文（学術雑誌）   出版者・発行元：Molecules  

Hydrogen/deuterium (H/D) exchange combined with two-dimensional (2D) NMR spectroscopy has been widely used for studying the structure, stability, and dynamics of proteins. When we apply the H/D-exchange method to investigate non-native states of proteins such as equilibrium and kinetic folding intermediates, H/D-exchange quenching techniques are indispensable, because the exchange reaction is usually too fast to follow by 2D NMR. In this article, we will describe the dimethylsulfoxide (DMSO)-quenched H/D-exchange method and its applications in protein science. In this method, the H/D-exchange buffer is replaced by an aprotic DMSO solution, which quenches the exchange reaction. We have improved the DMSO-quenched method by using spin desalting columns, which are used for medium exchange from the H/D-exchange buffer to the DMSO solution. This improvement has allowed us to monitor the H/D exchange of proteins at a high concentration of salts or denaturants. We describe methodological details of the improved DMSO-quenched method and present a case study using the improved method on the H/D-exchange behavior of unfolded human ubiquitin in 6 M guanidinium chloride.

DOI： 10.3390/molecules27123748

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記述言語：英語   掲載種別：研究論文（学術雑誌）   出版者・発行元：European Journal of Organic Chemistry  

Mincle, a C-type lectin receptor (CLR), senses certain lipid conjugates, leading to the activation of the innate immune system. The lipid conjugate ligands include glyco-, glycero-, and mannitol lipids. Recently, a fungal β-mannosyloxymannitol glycolipid demonstrating a novel architecture, “44-2,” was isolated from the fungus Malassezia and displayed potent Mincle-mediated signaling activity. For this study, we synthesized the diastereomeric pair of mannosyloxymannitol glycolipids and their analogues and analyzed the structure-activity relationships of Mincle-mediated signaling. The results suggest that the dimannosyl-fatty acid moiety in the mannosyloxymannitol glycolipid-type structure plays a major role in the molecular recognition of Mincle.

DOI： 10.1002/ejoc.202200109

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その他リンク： https://onlinelibrary.wiley.com/doi/full-xml/10.1002/ejoc.202200109

記述言語：英語   掲載種別：研究論文（学術雑誌）   出版者・発行元：Chemical Science  

<jats:p>In the photoactivation strategies with bioactive molecules, one-photon visible or two-photon near-infrared light-sensitive caged compounds are desirable tools for biological applications because they offer reduced phototoxicity and deep tissue penetration....</jats:p>

DOI： 10.1039/d2sc02364d

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記述言語：英語   掲載種別：研究論文（学術雑誌）   出版者・発行元：Molecules  

The human immunodeficiency virus type-1 Reverse Transcriptase (HIV-1 RT) plays a pivotal role in essential viral replication and is the main target for antiviral therapy. The anti-HIV-1 RT drugs address resistance-associated mutations. This research focused on isolating the potential specific DNA aptamers against K103N/Y181C double mutant HIV-1 RT. Five DNA aptamers showed low IC50 values against both the KY-mutant HIV-1 RT and wildtype (WT) HIV-1 RT. The kinetic binding affinity forms surface plasmon resonance of both KY-mutant and WT HIV-1 RTs in the range of 0.06-2 μM and 0.15-2 μM, respectively. Among these aptamers, the KY44 aptamer was chosen to study the interaction of HIV-1 RTs-DNA aptamer complex by NMR experiments. The NMR results indicate that the aptamer could interact with both WT and KY-mutant HIV-1 RT at the NNRTI drug binding pocket by inducing a chemical shift at methionine residues. Furthermore, KY44 could inhibit pseudo-HIV particle infection in HEK293 cells with nearly 80&#37; inhibition and showed low cytotoxicity on HEK293 cells. These together indicated that the KY44 aptamer could be a potential inhibitor of both WT and KY-mutant HIV-RT.

DOI： 10.3390/molecules27010285

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記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1038/s41598-021-00724-6

記述言語：英語   掲載種別：研究論文（学術雑誌）  

Secretory-abundant heat-soluble (SAHS) proteins are unique heat-soluble proteins of Tardigrada and are believed to play an essential role in anhydrobiosis, a latent state of life induced by desiccation. To investigate the dynamic properties, molecular dynamics (MD) simulations of a SAHS protein, RvSAHS1, were performed in solution and under dehydrating conditions. For comparison purposes, MD simulations of a human liver-type fatty-acid binding protein (LFABP) were performed in solution. Furthermore, high-speed atomic force microscopy observations were conducted to ascertain the results of the MD simulations. Three properties of RvSAHS1 were found as follows. (1) The entrance region of RvSAHS1 is more flexible and can be more extensive in solutions compared with that of a human LFABP because there is no salt bridge between the βD and βE strands. (2) The intrinsically disordered domain in the N-terminal region significantly fluctuates and can form an amphiphilic α-helix. (3) The size of the entrance region gets smaller along with dehydration, keeping the β-barrel structure. Overall, the obtained results provide atomic-level dynamics of SAHS proteins.

DOI： 10.1021/acs.jpcb.1c04850

記述言語：その他  

DOI： 10.1016/b978-0-12-819475-1.00044-4

記述言語：その他   掲載種別：研究論文（学術雑誌）  

DOI： 10.14456/JCST.2021.8

記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1002/anie.202102774

記述言語：その他   掲載種別：研究論文（学術雑誌）  

DOI： 10.1039/d0cp06448c

記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1093/jb/mvab012

記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1002/cbic.202000633

記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1016/j.bpj.2020.10.003

記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.3390/biom10111482

記述言語：その他   掲載種別：研究論文（学術雑誌）  

DOI： 10.3390/ijms21155351

記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1002/anie.202006600

記述言語：英語   掲載種別：研究論文（学術雑誌）  

Amyloid fibrils are self-assembled and ordered proteinaceous supramolecules structurally characterized by the cross-β spine. Amyloid formation is known to be related to various diseases typified by neurogenerative disorders and involved in a variety of functional roles. Whereas common mechanisms for amyloid formation have been postulated across diverse systems, the mesoscopic morphology of the fibrils is significantly affected by the type of solution condition in which it grows. Amyloid formation is also thought to share a phenomenological similarity with protein crystallization. Although many studies have demonstrated the effect of gravity on protein crystallization, its effect on amyloid formation has not been reported. In this study, we conducted an experiment at the International Space Station (ISS) to characterize fibril formation of 40-residue amyloid β (Aβ(1-40)) under microgravity conditions. Our comparative analyses revealed that the Aβ(1-40) fibrilization progresses much more slowly on the ISS than on the ground, similarly to protein crystallization. Furthermore, microgravity promoted the formation of distinct morphologies of Aβ(1-40) fibrils. Our findings demonstrate that the ISS provides an ideal experimental environment for detailed investigations of amyloid formation mechanisms by eliminating the conventionally uncontrollable factors derived from gravity.

DOI： 10.1038/s41526-020-0107-y

記述言語：英語  

DOI： 10.1007/s12551-020-00671-y

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DOI： 10.1007/s12551-020-00691-8

記述言語：その他   掲載種別：研究論文（学術雑誌）  

DOI： 10.1038/s41598-019-48911-w

記述言語：その他   掲載種別：研究論文（学術雑誌）  

DOI： 10.1038/s41598-019-50722-y

記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1021/acs.biochem.9b00594

記述言語：その他   掲載種別：研究論文（学術雑誌）  

DOI： 10.3390/ijms20092308

記述言語：その他   掲載種別：研究論文（学術雑誌）  

DOI： 10.1080/19420862.2018.1544454

記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1007/s12104-018-9809-4

記述言語：その他   掲載種別：研究論文（学術雑誌）  

DOI： 10.1007/978-981-13-2158-0_11

記述言語：その他   掲載種別：研究論文（学術雑誌）  

DOI： 10.3390/scipharm86010005

記述言語：その他   掲載種別：研究論文（学術雑誌）  

DOI： 10.1038/s41598-017-13845-8

記述言語：その他   掲載種別：研究論文（学術雑誌）  

DOI： 10.1371/journal.pone.0187022

記述言語：その他   掲載種別：研究論文（学術雑誌）  

DOI： 10.1016/j.bbrep.2017.08.004

記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1038/s41598-017-10246-9

記述言語：英語  

DOI： 10.3389/fimmu.2017.00632

記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1002/asia.201700202

記述言語：英語  

DOI： 10.1002/cbic.201600595

記述言語：英語  

DOI： 10.1016/j.pnmrs.2016.02.002

記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1074/jbc.M114.566174

記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1038/ncomms3211

記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1126/scisignal.2002056

記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1074/jbc.M110.152561

記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1093/protein/gzq006

記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.4049/jimmunol.0803471

記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1124/jpet.107.121640

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開催年月日： 2012年

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開催年月日： 2012年

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開催年月日： 2012年

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開催年月日： 2012年

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開催年月日： 2012年

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開催年月日： 2011年

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開催年月日： 2010年

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開催年月日： 2010年

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開催年月日： 2010年

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開催年月日： 2009年

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開催年月日： 2009年

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開催年月日： 2008年

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開催年月日： 2008年

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開催年月日： 2008年

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記述言語：日本語  

記述言語：日本語  

記述言語：英語  

記述言語：日本語   出版者・発行元：(株)羊土社  

Fcγ受容体をはじめとするエフェクター分子は抗体のFc領域の共通部位に結合する.抗体医薬の高機能化においてこうした部位を標的とした分子改変が進められている.一方,Fc領域は糖鎖修飾を受けており,糖鎖の構造がエフェクター機能に大きな影響を与える.さらに最近の研究により,抗体分子の定常部にエフェクター分子との相互作用を規定する部位が新たに見出されており,分子中に張り巡らされたアロステリックネットワークの存在も浮き彫りになってきた.こうした知見は,抗体の高機能化に重要な示唆を与える.(著者抄録)

J-GLOBAL

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記述言語：日本語  

記述言語：日本語  

記述言語：日本語  

記述言語：英語  

記述言語：日本語  

記述言語：英語