Results 251 to 260 of about 76,339 (318)

Asymmetrically glycosylated IgG1 antibodies are universal and drive human disease. [PDF]

Nat Commun
Azzam T, Bournazos S, Gunduz H, Adams T, Flowers MW, Niejadlik EG, Duong V, Brown TJ, Roberts AM, Sastre DE, Avci FY, Lam WA, Cantaert T, Roberts BR, Diamond B, Ravetch JV, Du JJ, Sundberg EJ.   +17 more
europepmc   +1 more source

Beyond monoclonal antibodies: constraints and the case for alternative PD-1/PD-L1-targeting formats. [PDF]

Front Immunol
Porozova NO, Petukhova NV, Gureev MA, Moiseev IS, Eliseev IE, Fedorova LV, Porozov YB.   +6 more
europepmc   +1 more source

Effects of rhEPO-Fc on chronic renal anemia in Chinese patients undergoing maintenance hemodialysis: a multicenter, randomized, open-label, and phase 3 study. [PDF]

Ren Fail
Gan L, Gao X, Yao J, Xiong X, Peng Q, Long G, Xiong F, Li Y, Chen Q, Qin Y, Xu Q, Chen W, Xu J, Zheng H, Yang L, Yi X, Cao N, Shen Y, Liu B, Zhu Q, Zhang P, Wu H, Shi J, Li Y, Li Y, Wang B, Chang W, Yu W, Wen R, Liu C, Jiang H, Li R, Ou J, Jiang X, Zhang A, Yang A, Yu Y, Peng J, Xu K, Wan X, Wang Y, Shi Y, Wang P, Liu P, Feng X, Xu H, Yang C, Li X, Wang J, Zhang W, Zuo L.   +50 more
europepmc   +1 more source

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FC-like fragments in peptic digests of human immunoglobulin G.

The Journal of Immunology, 1968
When the products of digestion of human immunoglobulin G with pepsin are compared to those obtained with papain, one major difference appears to involve the recovery of the Fc fragment.
R. Heimer, S. Schnoll
semanticscholar   +3 more sources

Chemical characterisation of the Fab and Fc fragments from surface immunoglobulin

Nature, 1980
Immunoglobulin (Ig) molecules of the M and D classes are present on the membranes of B lymphocytes (sIg), where they serve as antigen receptors1–6. sIg is a biosynthetically stable membrane protein which requires either denaturing conditions or detergents to free it from other membrane constituents1,7–9.
R. Parkhouse, J. Lifter, Y. S. Choi
semanticscholar   +3 more sources

Investigation of the cooperative structure of Fc fragments from myeloma immunoglobulin G.

Biochemistry, 1998
The cooperative structure of Fc fragments prepared from myeloma human IgG1 was studied using scanning microcalorimetry and fluorescence at pH 4.2-8.0. It was shown that the first to be melted are CH2 domains whose interaction with each other is rather weak, while that with CH3 domains is strong.
V. Tischenko, V. Abramov, V. Zav'yalov
semanticscholar   +3 more sources

Structural comparison of fucosylated and nonfucosylated Fc fragments of human immunoglobulin G1.

Journal of Molecular Biology, 2007
Removal of the fucose residue from the oligosaccharides attached to Asn297 of human immunoglobulin G1 (IgG1) results in a significant enhancement of antibody-dependent cellular cytotoxicity (ADCC) via improved IgG1 binding to Fcgamma receptor IIIa. To provide structural insight into the mechanisms of affinity enhancement, we determined the crystal ...
S. Matsumiya, Y. Yamaguchi, J. Saito, M. Nagano, H. Sasakawa, S. Otaki, M. Satoh, K. Shitara, Koichi Kato   +8 more
semanticscholar   +3 more sources

Identity of the Fc fragments of pathological and normal human immunoglobulin M.

Biochemistry, 1974
G. Florent, D. Lehman, D. Lockhart, F. Putnam   +3 more
semanticscholar   +3 more sources

Impairment by glycation of immunoglobulin G Fc fragment function

Scandinavian Journal of Clinical and Laboratory Investigation, 1990
Incubation of human immunoglobulin G (IgG) with glucose in vitro leads to the formation of glycated IgG concomitant with marked changes in functional properties of the Fc fragment. After 22 days of incubation in the absence and presence of 13.9, 27.7 and 55.5 mmol/l glucose, respectively, protein A binding was reduced by 42, 66 and 83%, depending on ...
R, Dolhofer-Bliesener, K D, Gerbitz
openaire   +2 more sources

Fc and Fab Fragments from IgG2 Human Immunoglobulins Characterized

Nature New Biology, 1972
Papain digestion of 7S immunoglobulin G (IgG) produces two 3.5S Fab fragments and one 3.5S Fc fragment1–8. The Fab fragment contains one light chain and one Fd fragment and is still able to combine specifically univalently with antigen. The Fc fragment is a dimer of the carboxyl terminal half of the heavy chain.
A C, Wang, H H, Fudenberg
openaire   +2 more sources