J
Jeffrey V. Ravetch
Researcher at Rockefeller University
Publications - 310
Citations - 59480
Jeffrey V. Ravetch is an academic researcher from Rockefeller University. The author has contributed to research in topics: Antibody & Receptor. The author has an hindex of 110, co-authored 296 publications receiving 54829 citations. Previous affiliations of Jeffrey V. Ravetch include Bristol-Myers Squibb & Kettering University.
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Characterization of the promoter of the human gene encoding the high-affinity IgG receptor: transcriptional induction by gamma-interferon is mediated through common DNA response elements
TL;DR: The studies suggest that the combination of X, H, and gamma-IRE elements is a common motif in the pathway of transcriptional induction by this lymphokine, and indicates that the presence of these elements are a general feature of IFN-gamma-responsive genes.
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Distinct contribution of Fc receptors and angiotensin II-dependent pathways in anti-GBM glomerulonephritis
Yusuke Suzuki,Isao Shirato,Isao Shirato,Isao Shirato,Ko Okumura,Ko Okumura,Ko Okumura,Jeffrey V. Ravetch,Jeffrey V. Ravetch,Jeffrey V. Ravetch,Toshiyuki Takai,Toshiyuki Takai,Toshiyuki Takai,Yasuhiko Tomino,Yasuhiko Tomino,Yasuhiko Tomino,Chisei Ra,Chisei Ra,Chisei Ra +18 more
TL;DR: It is demonstrated that FcRs play a pivotal role in Anti-GBM GN, especially in its acute phase, and the existence of FcR and complement-independent but antibody-dependent pathway is clarified.
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Anti-HA Glycoforms Drive B Cell Affinity Selection and Determine Influenza Vaccine Efficacy
Taia T. Wang,Jad Maamary,Gene S. Tan,Stylianos Bournazos,Carl W. Davis,Florian Krammer,Sarah J. Schlesinger,Peter Palese,Rafi Ahmed,Jeffrey V. Ravetch +9 more
TL;DR: It is shown that sFcs drive BCR affinity selection by binding the Type-II FcR CD23, thus upregulating the inhibitory FcγRIIB on activated B cells, resulting in B cell selection for higher affinity BCR.
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Structural characterization of anti-inflammatory Immunoglobulin G Fc proteins
Alysia A. Ahmed,John P. Giddens,Andrew Pincetic,Joseph V. Lomino,Jeffrey V. Ravetch,Lai-Xi Wang,Pamela J. Bjorkman +6 more
TL;DR: Comparison of the structures of asialylated Fc, sialylation Fc and F241A Fc suggests that increased conformational flexibility of the CH2 domain is associated with the switch from pro-inflammatory to anti-inflammatory activity of the Fc.
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Fcγ Receptor Function and the Design of Vaccination Strategies.
TL;DR: This work presents a framework that synthesizes the current understanding of the contribution of FcγR pathways to the induction and regulation of antibody and T cell responses and discusses vaccination strategies to elicit broad and potent immune responses based on the immunomodulatory properties of F cγR interactions.