Results 11 to 20 of about 51,044 (202)

Improvement of the method of obtaining human IgA Fc-fragments

Regulatory Mechanisms in Biosystems, 2015
To address a number of fundamental and applied problems in immunology, molecular and cellular biology and biotechnology it is necessary to obtain Fc-fragments of immunoglobulins.
O. Y. Galkin, Y. V. Gorshunov, V. F. Solovjova   +2 more
doaj   +1 more source

Manufacturability and functionality assessment of different formats of T-cell engaging bispecific antibodies

mAbs, 2023
T-cell-engaging bispecific antibodies (T-bsAbs) are promising immunotherapies for cancer treatment due to their capability of redirecting T-cells toward destroying tumor cells.
Han Ping Loh, Farouq Bin Mahfut, Serene W Chen, Yuhan Huang, Jianxin Huo, Wei Zhang, Kong Peng Lam, Shengli Xu, Yuansheng Yang   +8 more
doaj   +1 more source

Intrachain disulphide bridges in immunoglobulin G heavy chains. The Fc fragment [PDF]

Biochemical Journal, 1968
The disulphide bridges of the Fc fragment (C-terminal half of the heavy chain) have been studied in several human immunoglobulins, containing heavy chains of different antigenic types (γ1, γ2, γ3 and γ4), and in heavy-chain-disease proteins. Two intrachain disulphide bridges were found to be present.
B, Frangione, C, Milstein, E C, Franklin
openaire   +2 more sources

13C NMR study of the mode of interaction in solution of the B fragment of staphylococcal protein A and the Fc fragments of mouse immunoglobulin G [PDF]

, 1923
The mode of interaction of the B domain (FB) of staphylococcal protein A and the Fc fragments of mouse immunoglobulin G (IgG) has been investigated by 13C NMR spectroscopy.
Langone, Burton, Moks, Deisenhofer, Gouda, Sjöholm, Wright, Lancet, Kato, Matsunaga, Kim, Nagasawa, Saito, Torigoe, Dangl, Dangl, Kainosho, Barnett-Fostar, Ey, Schneider, Edelman, Kabat, Igarashi   +22 more
core   +1 more source

Activating FcγR function depends on endosomal-signaling platforms

iScience, 2023
Summary: Cell surface receptor internalization can either terminate signaling or activate alternative endosomal signaling pathways. We investigated here whether endosomal signaling is involved in the function of the human receptors for Fc immunoglobulin ...
Samira Benadda, Mathilde Nugue, Despoina Koumantou, Marcelle Bens, Mariacristina De Luca, Olivier Pellé, Renato C. Monteiro, Irini Evnouchidou, Loredana Saveanu   +8 more
doaj   +1 more source

Determination of Physicochemical Properties of Human Immunoglobulin G- Fc Fragment by Bioinformatic [PDF]

Pars of Jahrom University of Medical Sciences, 2021
Introduction: Immunoglobulins (Igs) are defensive glycoproteins specifically recognize and destroy pathogens. Immunoglobulin G (IgG) is most abundant Ig in serum has important protective role against infections. Fragment of crystallizable (Fc) in IgG has essential role in pathogens destruction.
Soheyla Rohani, Fatemeh Hajighasemi
openaire   +2 more sources

Structure analysis of goose immunoglobulin Y Fc fragment

Central European Journal of Immunology, 2013
Objective: Goose immunoglobulin Y (IgY)-Fc fragment gene is cloned. Material and methods: In order to obtain a certain length (106 bp) of constant domain gene, a pair of primer was designed according to the conserved nucleotide sequence of duck (CAA46322) and chick en (S00390) IgY-Fc fragment that was published by the GenBank.
Lei Jiang, Wei-Shan Chang, Hao Guo, Peng Sun, Xiu-Mei Dai   +4 more
openaire   +1 more source

Immunoglobulin Fc heterodimer platform technology: From design to applications in therapeutic antibodies and proteins

Frontiers in Immunology, 2016
The monospecific and bivalent characteristics of naturally occurring immunoglobulin G (IgG) antibodies depend on homodimerization of the fragment crystallizable (Fc) regions of two identical heavy chains (HCs) and the subsequent assembly of two identical
Ji-Hee Ha, Jung-Eun Kim, Yong-Sung Kim
doaj   +1 more source

The Solution Structures of Two Human IgG1 Antibodies Show Conformational Stability and Accommodate Their C1q and FcγR Ligands. [PDF]

, 2015
The human IgG1 antibody subclass shows distinct properties compared with the IgG2, IgG3, and IgG4 subclasses and is the most exploited subclass in therapeutic antibodies. It is the most abundant subclass, has a half-life as long as that of IgG2 and IgG4,
Abe, Andrusier, Ashish, Ashton, Boehm, Brekke, Bruhns, Brüggemann, Calmettes, Collins, Dall'Acqua, Dangl, Davies, Deisenhofer, Diebolder, Dorai, Feinstein, Furtado, Gaboriaud, Gar Kay Hui, Garcia de la Torre, García De La Torre, Glatter, Gregory, Guddat, Guex, Hamilton, Harris, Harris, Heenan, Hezareh, Hughes-Jones, Idusogie, Isenman, Iwura, Jayesh Gor, Jefferis, Kilár, Klein, Laue, Lilyestrom, Lucy E. Rayner, Lund, Luo, Manning, Marquart, Michaelsen, Narayanan, Paul A. Dalby, Perkins, Perkins, Perkins, Perkins, Phillips, Pilz, Radaev, Radaev, Rayner, Rayner, Remmele, Richard K. Heenan, Richardson, Roux, Saphire, Saphire, Sarma, Schneider, Schneidman-Duhovny, Schuck, Schuck, Semenyuk, Sondermann, Stephen J. Perkins, Strohl, Sun, Tamm, Tao, Thommesen, Wang, Yang   +79 more
core   +1 more source

Fc-Galactosylation of Human Immunoglobulin Gamma Isotypes Improves C1q Binding and Enhances Complement-Dependent Cytotoxicity

Frontiers in Immunology, 2017
Binding of the complement component C1q to the CH2 domain of antigen-bound immunoglobulin gamma (IgG) activates the classical complement pathway and depends on its close proximity to Fc fragments of neighboring antibodies. IgG subclasses contain a highly
Benjamin Peschke, Christian W. Keller, Patrick Weber, Isaak Quast, Isaak Quast, Jan D. Lünemann, Jan D. Lünemann   +6 more
doaj   +1 more source