Reference health

Unique carbohydrate–carbohydrate interactions are required for high affinity binding between FcγRIII and antibodies lacking core fucose

https://doi.org/10.1073/pnas.1108455108
CiteStamped reference-health badge
36/36 checkable references clean · checked 2026-07-24

Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.

4 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.

The 36 checked references that resolve
resolves10.1016/j.tips.2009.04.007
Recombinant antibody therapeutics: the impact of glycosylation on mechanisms of action
resolves10.1038/nri2206
Fcγ receptors as regulators of immune responses
resolves10.1016/S0165-2478(02)00019-6
Interaction sites on human IgG-Fc for FcγR: current models
resolves10.1038/35018508
The 3.2-Å crystal structure of the human IgG1 Fc fragment–FcγRIII complex
resolves10.1016/S0022-2836(02)01250-0
Structural Analysis of Human IgG-Fc Glycoforms Reveals a Correlation Between Glycosylation and Structural Integrity
resolves10.1073/pnas.0702936104
Agalactosylated IgG antibodies depend on cellular Fc receptors for <i>in vivo</i> activity
resolves10.1126/science.1129594
Anti-Inflammatory Activity of Immunoglobulin G Resulting from Fc Sialylation
resolves10.1073/pnas.0810163105
Identification of a receptor required for the anti-inflammatory activity of IVIG
resolves10.1074/jbc.M202069200
Lack of Fucose on Human IgG1 N-Linked Oligosaccharide Improves Binding to Human FcγRIII and Antibody-dependent Cellular Toxicity
resolves10.1126/science.1118948
Divergent Immunoglobulin G Subclass Activity Through Selective Fc Receptor Binding
resolves10.1038/74704
Inhibitory Fc receptors modulate in vivo cytoxicity against tumor targets
resolves10.1182/blood.V99.3.754
Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcγRIIIa gene
resolves10.1038/6179
Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity
resolves10.1074/jbc.M210665200
The Absence of Fucose but Not the Presence of Galactose or Bisecting N-Acetylglucosamine of Human IgG1 Complex-type Oligosaccharides Shows the Critical Role of Enhancing Antibody-dependent Cellular Cytotoxicity
resolves10.1093/glycob/cwn110
The N-linked oligosaccharide at Fc RIIIa Asn-45: an inhibitory element for high Fc RIIIa binding affinity to IgG glycoforms lacking core fucosylation
resolves10.1016/j.jmb.2007.02.034
Structural Comparison of Fucosylated and Nonfucosylated Fc Fragments of Human Immunoglobulin G1
resolves10.1016/j.str.2007.01.011
Glycoprotein Structural Genomics: Solving the Glycosylation Problem
resolves10.4049/jimmunol.159.8.3849
Cell type-specific glycoforms of Fc gamma RIIIa (CD16): differential ligand binding
resolves10.1074/jbc.M100350200
The Structure of a Human Type III Fcγ Receptor in Complex with Fc
resolves10.1083/jcb.200309005
Carbohydrate–carbohydrate interaction provides adhesion force and specificity for cellular recognition
resolves10.1016/j.jmb.2004.01.007
Fucose Depletion from Human IgG1 Oligosaccharide Enhances Binding Enthalpy and Association Rate Between IgG1 and FcγRIIIa
resolves10.1073/pnas.1014515107
FcγRIV deletion reveals its central role for IgG2a and IgG2b activity in vivo
resolves10.1046/j.1365-2249.2002.01864.x
Hypogalactosylation of serum IgG in patients with ANCA-associated systemic vasculitis
resolves10.1146/annurev.immunol.25.022106.141702
The Impact of Glycosylation on the Biological Function and Structure of Human Immunoglobulins
resolves10.1021/pr1012653
Cell Type-Specific and Site Directed <i>N</i>-Glycosylation Pattern of FcγRIIIa
resolves10.1182/blood-2009-06-225979
Increasing the efficacy of CD20 antibody therapy through the engineering of a new type II anti-CD20 antibody with enhanced direct and immune effector cell–mediated B-cell cytotoxicity
resolves10.1182/blood-2010-09-305847
Epitope characterization and crystal structure of GA101 provide insights into the molecular basis for type I/II distinction of CD20 antibodies
resolves10.1093/glycob/cwg079
Detailed glycan analysis of serum glycoproteins of patients with congenital disorders of glycosylation indicates the specific defective glycan processing step and provides an insight into pathogenesis
resolves10.1021/pr800651j
Regulated Glycosylation Patterns of IgG during Alloimmune Responses against Human Platelet Antigens
resolves10.1002/bit.20777
Modulation of therapeutic antibody effector functions by glycosylation engineering: Influence of Golgi enzyme localization domain and co‐expression of heterologous β1, 4‐<i>N</i>‐acetylglucosaminyltransferase III and Golgi α‐mannosidase II
resolves10.1107/S0907444909047374
Integration, scaling, space-group assignment and post-refinement
resolves10.1107/S0021889807021206
<i>Phaser</i>crystallographic software
resolves10.1107/S0907444994003112
The CCP4 suite: programs for protein crystallography
resolves10.1107/S0907444904016427
Refinement of severely incomplete structures with maximum likelihood in<i>BUSTER–TNT</i>
resolves10.1107/S0907444910007493
Features and development of <i>Coot</i>
resolves10.1002/bip.360320811
Peptide mechanics: A force field for peptides and proteins working with entire residues as smallest units
The 4 references without a DOI — listed, not checked
no DOI — not checkedG Cartron, et al., Promising efficacy with the new anti-CD20 antibody GA101 in heavily pre-treated NHL patients—First results from a phase II study in patients with relapsed/refractory DLBCL and MCL. Blood (ASH Annual Meeting Abtracts) 116, 2878 (2010).
no DOI — not checkedGA Salles, et al., Promising efficacy with the New anti-CD20 antibody GA101 in heavily pre-treated NHL patients—Updated results with encouraging progression free survival (PFS) data from a phase II study in patients with relapsed/refractory indolent NHL (iNHL). Blood (ASH Annual Meeting Abtracts) 116, 2868 (2010).
no DOI — not checkedC Ferrara, F Stuart, P Sondermann, P Brünker, P Umaña, The carbohydrate at FcgammaRIIIa Asn-162. An element required for high affinity binding to non-fucosylated IgG glycoforms. J Biol Chem 281, 5032–5036 (2005).
no DOI — not checkedWarren DeLano The PyMOL Molecular Graphics System Version 1.2r3pre (Schrödinger LLC Palo Alto CA 2002).
What this badge says. CiteStamped means the CHECKABLE references of this work were clean at the dated check: each resolved to a known work in a public registry, and none carried a retraction notice at that time. It says nothing about the quality, findings, or importance of the work itself, and nothing about references deposited without a DOI.

checked 2026-07-24 — re-checked daily as this page is visited; titles and statuses come from Crossref and DataCite and are not part of the signed record

Embed this badge

Both snippets point at the live badge image and link back to this page. The badge re-renders from the daily check, so an embed never goes stale by more than a day of visits.

<a href="https://citestamp.com/citestamped/10.1073/pnas.1108455108"><img src="https://citestamp.com/citestamped/10.1073/pnas.1108455108/badge.svg" alt="CiteStamped reference-health badge" width="460" height="64"></a>
[![CiteStamped reference-health badge](https://citestamp.com/citestamped/10.1073/pnas.1108455108/badge.svg)](https://citestamp.com/citestamped/10.1073/pnas.1108455108)