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Hammer, Gianna

Overview:

The study of microbial communities that reside on and within the human body (the microbiome) is considered one of the hottest areas of science today. It is now well appreciated that the microbiome has remarkable influence on diverse aspects of human health and disease. To understand how the microbiome exerts such influence, our lab seeks to define the mechanisms by which cells of the immune system interact with microbes that reside in the intestine. To the immune system, co-existence with microbes is a remarkable paradox: while immune cells are skilled operatives fixated on eliminating microbial invaders, these same cells are somehow restrained from attacking microbial commensals. This restraint is critical to prevent inflammatory bowel disease (IBD).
Our research seeks to understand the pathogenesis of inflammatory bowel disease, and understand interactions between host and the microbiome. In particular, we study the roles of dendritic cells. Dendritic cells are exquisitely sensitive to microbes, and after engaging microbes or microbial products, dendritic cells are reprogrammed into inflammatory cells with potent ability to activate other immune cells. Because of their potent influence over the immune system, dendritic cells are in a prime position to relay signals from the microbiome, and we have found that dendritic cells are key players in pathogenesis of inflammatory bowel disease. To prevent IBD, dendritic cells require the NF-kB suppressor, A20. A20 suppresses multiple disease-associated signaling pathways, including TNF, NOD2 and Toll-like receptors. Using biochemistry and in vivo analyses, we are interrogating the roles of these receptors and signaling pathways in regulating the responses of dendritic cells to the intestinal microbiome. Additionally, we seek to identify new signaling pathways by which DCs interact with microbial communities of the intestine.

Positions:

Assistant Professor of Immunology

Immunology
School of Medicine

Member of the Duke Cancer Institute

Duke Cancer Institute
School of Medicine

Education:

Ph.D. 2006

Ph.D. — University of California at Berkeley

News:

Grants:

Role of osteopontin in innate immunity during infections and inflammation

Administered By
Immunology
AwardedBy
National Institutes of Health
Role
Collaborator
Start Date
February 15, 2011
End Date
February 28, 2022

Duke Training Grant in Digestive Diseases and Nutrition

Administered By
Medicine, Gastroenterology
AwardedBy
National Institutes of Health
Role
Mentor
Start Date
July 01, 1988
End Date
June 30, 2021

Identification of anti-commensal T cells, their pathological function, and their commensal antigen specificities in inflammatory bowel disease using a novel in vivo reporter system

Administered By
Immunology
AwardedBy
Pew Charitable Trusts
Role
Principal Investigator
Start Date
August 01, 2015
End Date
July 31, 2020

Role of Dendritic Cell-mediated T Cell Activation in Salt-sensitive Hypertension

Administered By
Medicine, Nephrology
AwardedBy
National Institutes of Health
Role
Collaborator
Start Date
April 01, 2016
End Date
March 31, 2020

IL-27 in skin host defense and regeneration

Administered By
Dermatology
AwardedBy
National Institutes of Health
Role
Collaborator
Start Date
August 15, 2017
End Date
July 31, 2019

The role of dendritic cell-mediated T cell activation in hypertension

Administered By
Medicine, Nephrology
AwardedBy
National Institutes of Health
Role
Collaborator
Start Date
July 01, 2017
End Date
June 30, 2019

Basic Immunology Training Program

Administered By
Immunology
AwardedBy
National Institutes of Health
Role
Mentor
Start Date
July 01, 2002
End Date
June 30, 2019

Microbiota induced upregulation of PDL1 on intestinal dendritic cells in intestinal tumorig

Administered By
Immunology
AwardedBy
V Foundation for Cancer Research
Role
Principal Investigator
Start Date
November 01, 2016
End Date
October 31, 2018

Dendritic cell orchestration of colitogenic T cells in inflammatory bowel disease

Administered By
Immunology
AwardedBy
University of North Carolina - Chapel Hill
Role
Principal Investigator
Start Date
December 01, 2013
End Date
November 30, 2015
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Awards:

Pew Scholar. Pew Charitable Trusts.

Type
National
Awarded By
Pew Charitable Trusts
Date
January 01, 2015

Publications:

IL-27 signaling is essential for IL-15 production and mediates contact hypersensitivity

Authors
Pontius, L; Suwanpradid, J; Kwock, J; Yang, B; Maycock, J; Kedl, R; Hammer, G; MacLeod, AS
MLA Citation
Pontius, L, Suwanpradid, J, Kwock, J, Yang, B, Maycock, J, Kedl, R, Hammer, G, and MacLeod, AS. "IL-27 signaling is essential for IL-15 production and mediates contact hypersensitivity." May 2017.
Source
wos-lite
Published In
Journal of Investigative Dermatology
Volume
137
Issue
5
Publish Date
2017
Start Page
S105
End Page
S105

Inflammatory Th1 and Th17 in the Intestine Are Each Driven by Functionally Specialized Dendritic Cells with Distinct Requirements for MyD88.

Normal dynamics between microbiota and dendritic cells (DCs) support modest numbers of T cells, yet these do not cause inflammation. The DCs that induce inflammatory T cells and the signals that drive this process remain unclear. Here, we demonstrate that small intestine DCs lacking the signaling attenuator A20 induce inflammatory T cells and that the signals perceived and antigen-presenting cell (APC) functions are unique for different DC subsets. Thus, although CD103+CD11b- DCs exclusively instruct IFNγ+ T cells, CD103+CD11b+ DCs exclusively instruct IL-17+ T cells. Surprisingly, APC functions of both DC subsets are upregulated in a MyD88-independent fashion. In contrast, CD103-CD11b+ DCs instruct both IFNγ+ and IL-17+ T cells, and only the IL-17-inducing APC functions require MyD88. In disease pathogenesis, both CD103-CD11b+ and CD103+CD11b+ DCs expand pathologic Th17 cells. Thus, in disease pathogenesis, specific DCs instruct specific inflammatory T cells.

Authors
Liang, J; Huang, H-I; Benzatti, FP; Karlsson, AB; Zhang, JJ; Youssef, N; Ma, A; Hale, LP; Hammer, GE
MLA Citation
Liang, J, Huang, H-I, Benzatti, FP, Karlsson, AB, Zhang, JJ, Youssef, N, Ma, A, Hale, LP, and Hammer, GE. "Inflammatory Th1 and Th17 in the Intestine Are Each Driven by Functionally Specialized Dendritic Cells with Distinct Requirements for MyD88." Cell reports 17.5 (October 2016): 1330-1343.
Website
http://hdl.handle.net/10161/13002
PMID
27783947
Source
epmc
Published In
Cell Reports
Volume
17
Issue
5
Publish Date
2016
Start Page
1330
End Page
1343
DOI
10.1016/j.celrep.2016.09.091

Microbiota upregulate distinct APC functions in each intestinal dendritic cell subset, in a Myd88-independent fashion

Authors
Hammer, G; Liang, J; Huang, H-I; Benzatti, F; Karlsson, A; Hale, LP
MLA Citation
Hammer, G, Liang, J, Huang, H-I, Benzatti, F, Karlsson, A, and Hale, LP. "Microbiota upregulate distinct APC functions in each intestinal dendritic cell subset, in a Myd88-independent fashion." May 1, 2016.
Source
wos-lite
Published In
Journal of immunology (Baltimore, Md. : 1950)
Volume
196
Publish Date
2016

Autophagy enhances NFκB activity in specific tissue macrophages by sequestering A20 to boost antifungal immunity.

Immune responses must be well restrained in a steady state to avoid excessive inflammation. However, such restraints are quickly removed to exert antimicrobial responses. Here we report a role of autophagy in an early host antifungal response by enhancing NFκB activity through A20 sequestration. Enhancement of NFκB activation is achieved by autophagic depletion of A20, an NFκB inhibitor, in F4/80(hi) macrophages in the spleen, peritoneum and kidney. We show that p62, an autophagic adaptor protein, captures A20 to sequester it in the autophagosome. This allows the macrophages to release chemokines to recruit neutrophils. Indeed, mice lacking autophagy in myeloid cells show higher susceptibility to Candida albicans infection due to impairment in neutrophil recruitment. Thus, at least in the specific aforementioned tissues, autophagy appears to break A20-dependent suppression in F4/80(hi) macrophages, which express abundant A20 and contribute to the initiation of efficient innate immune responses.

Authors
Kanayama, M; Inoue, M; Danzaki, K; Hammer, G; He, Y-W; Shinohara, ML
MLA Citation
Kanayama, M, Inoue, M, Danzaki, K, Hammer, G, He, Y-W, and Shinohara, ML. "Autophagy enhances NFκB activity in specific tissue macrophages by sequestering A20 to boost antifungal immunity." Nature Communications 6 (January 22, 2015): 5779-.
Website
http://hdl.handle.net/10161/9376
PMID
25609235
Source
epmc
Published In
Nature Communications
Volume
6
Publish Date
2015
Start Page
5779
DOI
10.1038/ncomms6779

Cutting edge: ABIN-1 protects against psoriasis by restricting MyD88 signals in dendritic cells.

Psoriasis is a chronic, inflammatory skin disease caused by a combination of environmental and genetic factors. The Tnip1 gene encodes A20 binding and inhibitor of NF-κB-1 (ABIN-1) protein and is strongly associated with susceptibility to psoriasis in humans. ABIN-1, a widely expressed ubiquitin-binding protein, restricts TNF- and TLR-induced signals. In this study, we report that mice lacking ABIN-1 specifically in dendritic cells (DCs), ABIN-1(fl) CD11c-Cre mice, exhibit perturbed immune homeostasis. ABIN-1-deficient DCs display exaggerated NF-κB and MAPK signaling and produce more IL-23 than do normal cells in response to TLR ligands. Challenge of ABIN-1(fl) CD11c-Cre mice with topical TLR7 ligand leads to greater numbers of Th17 and TCRγδ T cells and exacerbated development of psoriaform lesions. These phenotypes are reversed by DC-specific deletion of the TLR adaptor MyD88. These studies link ABIN-1 with IL-23 and IL-17, and they provide cellular and molecular mechanisms by which ABIN-1 regulates susceptibility to psoriasis.

Authors
Callahan, JA; Hammer, GE; Agelides, A; Duong, BH; Oshima, S; North, J; Advincula, R; Shifrin, N; Truong, H-A; Paw, J; Barrera, J; DeFranco, A; Rosenblum, MD; Malynn, BA; Ma, A
MLA Citation
Callahan, JA, Hammer, GE, Agelides, A, Duong, BH, Oshima, S, North, J, Advincula, R, Shifrin, N, Truong, H-A, Paw, J, Barrera, J, DeFranco, A, Rosenblum, MD, Malynn, BA, and Ma, A. "Cutting edge: ABIN-1 protects against psoriasis by restricting MyD88 signals in dendritic cells." Journal of immunology (Baltimore, Md. : 1950) 191.2 (July 2013): 535-539.
PMID
23785118
Source
epmc
Published In
Journal of immunology (Baltimore, Md. : 1950)
Volume
191
Issue
2
Publish Date
2013
Start Page
535
End Page
539
DOI
10.4049/jimmunol.1203335

Dimerization and ubiquitin mediated recruitment of A20, a complex deubiquitinating enzyme.

A20 is an anti-inflammatory protein linked to multiple human autoimmune diseases and lymphomas. A20 possesses a deubiquitinating motif and a zinc finger, ZF4, that binds ubiquitin and supports its E3 ubiquitin ligase activity. To understand how these activities mediate A20's physiological functions, we generated two lines of gene-targeted mice, abrogating either A20's deubiquitinating activity (Tnfaip3(OTU) mice) or A20's ZF4 (Tnfaip3(ZF4) mice). Both Tnfaip3(OTU) and Tnfaip3(ZF4) mice exhibited increased responses to TNF and sensitivity to colitis. A20's C103 deubiquitinating motif restricted both K48- and K63-linked ubiquitination of receptor interacting protein 1 (RIP1). A20's ZF4 was required for recruiting A20 to ubiquitinated RIP1. A20(OTU) proteins and A20(ZF4) proteins complemented each other to regulate RIP1 ubiquitination and NFκB signaling normally in compound mutant Tnfaip3(OTU/ZF4) cells. This complementation involved homodimerization of A20 proteins, and we have defined an extensive dimerization interface in A20. These studies reveal how A20 proteins collaborate to restrict TNF signaling.

Authors
Lu, TT; Onizawa, M; Hammer, GE; Turer, EE; Yin, Q; Damko, E; Agelidis, A; Shifrin, N; Advincula, R; Barrera, J; Malynn, BA; Wu, H; Ma, A
MLA Citation
Lu, TT, Onizawa, M, Hammer, GE, Turer, EE, Yin, Q, Damko, E, Agelidis, A, Shifrin, N, Advincula, R, Barrera, J, Malynn, BA, Wu, H, and Ma, A. "Dimerization and ubiquitin mediated recruitment of A20, a complex deubiquitinating enzyme." Immunity 38.5 (May 2013): 896-905.
PMID
23602765
Source
epmc
Published In
Immunity
Volume
38
Issue
5
Publish Date
2013
Start Page
896
End Page
905
DOI
10.1016/j.immuni.2013.03.008

Molecular control of steady-state dendritic cell maturation and immune homeostasis.

Dendritic cells (DCs) are specialized sentinels responsible for coordinating adaptive immunity. This function is dependent upon coupled sensitivity to environmental signs of inflammation and infection to cellular maturation-the programmed alteration of DC phenotype and function to enhance immune cell activation. Although DCs are thus well equipped to respond to pathogens, maturation triggers are not unique to infection. Given that immune cells are exquisitely sensitive to the biological functions of DCs, we now appreciate that multiple layers of suppression are required to restrict the environmental sensitivity, cellular maturation, and even life span of DCs to prevent aberrant immune activation during the steady state. At the same time, steady-state DCs are not quiescent but rather perform key functions that support homeostasis of numerous cell types. Here we review these functions and molecular mechanisms of suppression that control steady-state DC maturation. Corruption of these steady-state operatives has diverse immunological consequences and pinpoints DCs as potent drivers of autoimmune and inflammatory disease.

Authors
Hammer, GE; Ma, A
MLA Citation
Hammer, GE, and Ma, A. "Molecular control of steady-state dendritic cell maturation and immune homeostasis." Annual review of immunology 31 (January 17, 2013): 743-791. (Review)
PMID
23330953
Source
epmc
Published In
Annual Review of Immunology
Volume
31
Publish Date
2013
Start Page
743
End Page
791
DOI
10.1146/annurev-immunol-020711-074929

Expression of A20 by dendritic cells preserves immune homeostasis and prevents colitis and spondyloarthritis.

Dendritic cells (DCs), which are known to support immune activation during infection, may also regulate immune homeostasis in resting animals. Here we show that mice lacking the ubiquitin-editing molecule A20 specifically in DCs spontaneously showed DC activation and population expansion of activated T cells. Analysis of DC-specific epistasis in compound mice lacking both A20 and the signaling adaptor MyD88 specifically in DCs showed that A20 restricted both MyD88-independent signals, which drive activation of DCs and T cells, and MyD88-dependent signals, which drive population expansion of T cells. In addition, mice lacking A20 specifically in DCs spontaneously developed lymphocyte-dependent colitis, seronegative ankylosing arthritis and enthesitis, conditions stereotypical of human inflammatory bowel disease (IBD). Our findings indicate that DCs need A20 to preserve immune quiescence and suggest that A20-dependent DC functions may underlie IBD and IBD-associated arthritides.

Authors
Hammer, GE; Turer, EE; Taylor, KE; Fang, CJ; Advincula, R; Oshima, S; Barrera, J; Huang, EJ; Hou, B; Malynn, BA; Reizis, B; DeFranco, A; Criswell, LA; Nakamura, MC; Ma, A
MLA Citation
Hammer, GE, Turer, EE, Taylor, KE, Fang, CJ, Advincula, R, Oshima, S, Barrera, J, Huang, EJ, Hou, B, Malynn, BA, Reizis, B, DeFranco, A, Criswell, LA, Nakamura, MC, and Ma, A. "Expression of A20 by dendritic cells preserves immune homeostasis and prevents colitis and spondyloarthritis." Nature immunology 12.12 (October 23, 2011): 1184-1193.
PMID
22019834
Source
epmc
Published In
Nature Immunology
Volume
12
Issue
12
Publish Date
2011
Start Page
1184
End Page
1193
DOI
10.1038/ni.2135

Construction and destruction of MHC class I in the peptide-loading complex.

Authors
Hammer, GE; Shastri, N
MLA Citation
Hammer, GE, and Shastri, N. "Construction and destruction of MHC class I in the peptide-loading complex." Nature immunology 8.8 (August 2007): 793-794.
PMID
17641657
Source
epmc
Published In
Nature Immunology
Volume
8
Issue
8
Publish Date
2007
Start Page
793
End Page
794
DOI
10.1038/ni0807-793

The final touches make perfect the peptide-MHC class I repertoire.

Major histocompatibility complex (MHC) class I molecules present short, perfectly cleaved peptides on the cell surface for immune surveillance by CD8(+) T cells. The pathway for generating these peptides begins in the cytoplasm, and the peptide-MHC I (pMHC I) repertoire is finalized in the endoplasmic reticulum. Recent studies show that the peptides for MHC I are customized by the ER aminopeptidase associated with antigen processing and by dynamic interactions within the MHC peptide-loading complex. Failure to customize the pMHC I repertoire has profound immunological consequences.

Authors
Hammer, GE; Kanaseki, T; Shastri, N
MLA Citation
Hammer, GE, Kanaseki, T, and Shastri, N. "The final touches make perfect the peptide-MHC class I repertoire." Immunity 26.4 (April 2007): 397-406. (Review)
PMID
17459809
Source
epmc
Published In
Immunity
Volume
26
Issue
4
Publish Date
2007
Start Page
397
End Page
406
DOI
10.1016/j.immuni.2007.04.003

In the absence of aminopeptidase ERAAP, MHC class I molecules present many unstable and highly immunogenic peptides.

Immunosurveillance by cytotoxic T cells requires that cells generate a diverse spectrum of peptides for presentation by major histocompatibility complex (MHC) class I molecules. Those peptides are generated by proteolysis, which begins in the cytoplasm and continues in the endoplasmic reticulum by the unique aminopeptidase ERAAP. The overall extent to which trimming by ERAAP modifies the peptide pool and the immunological consequences of ERAAP deficiency are unknown. Here we show that the peptide-MHC repertoire of ERAAP-deficient mice was missing many peptides. Furthermore, ERAAP-deficient cells presented many unstable and structurally unique peptide-MHC complexes, which elicited potent CD8+ T cell and B cell responses. Thus, ERAAP is a 'quintessential editor' of the peptide-MHC repertoire and, paradoxically, its absence enhances immunogenicity.

Authors
Hammer, GE; Gonzalez, F; James, E; Nolla, H; Shastri, N
MLA Citation
Hammer, GE, Gonzalez, F, James, E, Nolla, H, and Shastri, N. "In the absence of aminopeptidase ERAAP, MHC class I molecules present many unstable and highly immunogenic peptides." Nature immunology 8.1 (January 2007): 101-108.
PMID
17128277
Source
epmc
Published In
Nature Immunology
Volume
8
Issue
1
Publish Date
2007
Start Page
101
End Page
108
DOI
10.1038/ni1409

ERAAP synergizes with MHC class I molecules to make the final cut in the antigenic peptide precursors in the endoplasmic reticulum.

The major histocompatibility complex class I molecules display peptides (pMHC I) on the cell surface for immune surveillance by CD8(+) T cells. These peptides are generated by proteolysis of intracellular polypeptides by the proteasome in the cytoplasm and then in the endoplasmic reticulum (ER) by the ER aminopeptidase associated with antigen processing (ERAAP). To define the unknown mechanism of ERAAP function in vivo, we analyzed naturally processed peptides in cells with or without appropriate MHC I and ERAAP. In the absence of MHC I, ERAAP degraded the antigenic precursors in the ER. However, MHC I molecules could bind proteolytic intermediates and were essential for generation of the final peptide by ERAAP. Thus, ERAAP synergizes with MHC I to generate the final pMHC I repertoire.

Authors
Kanaseki, T; Blanchard, N; Hammer, GE; Gonzalez, F; Shastri, N
MLA Citation
Kanaseki, T, Blanchard, N, Hammer, GE, Gonzalez, F, and Shastri, N. "ERAAP synergizes with MHC class I molecules to make the final cut in the antigenic peptide precursors in the endoplasmic reticulum." Immunity 25.5 (November 2006): 795-806.
PMID
17088086
Source
epmc
Published In
Immunity
Volume
25
Issue
5
Publish Date
2006
Start Page
795
End Page
806
DOI
10.1016/j.immuni.2006.09.012

ERAAP and MHC class I molecules collaborate to generate the exact length of antigenic peptides in the endoplasmic reticulum

Authors
Kanaseki, T; Blanchard, N; Hammer, GE; Gonzalez, F; Shastri, N
MLA Citation
Kanaseki, T, Blanchard, N, Hammer, GE, Gonzalez, F, and Shastri, N. "ERAAP and MHC class I molecules collaborate to generate the exact length of antigenic peptides in the endoplasmic reticulum." April 1, 2006.
Source
wos-lite
Published In
Journal of immunology (Baltimore, Md. : 1950)
Volume
176
Publish Date
2006
Start Page
S54
End Page
S54

The aminopeptidase ERAAP shapes the peptide repertoire displayed by major histocompatibility complex class I molecules.

Major histocompatibility complex (MHC) class I molecules present thousands of peptides to allow CD8(+) T cells to detect abnormal intracellular proteins. The antigen-processing pathway for generating peptides begins in the cytoplasm, and the MHC molecules are loaded in the endoplasmic reticulum. However, the nature of peptide pool in the endoplasmic reticulum and the proteolytic events that occur in this compartment are unclear. We addressed these issues by generating mice lacking the endoplasmic reticulum aminopeptidase associated with antigen processing (ERAAP). We found that loss of ERAAP disrupted the generation of naturally processed peptides in the endoplasmic reticulum, decreased the stability of peptide-MHC class I complexes and diminished CD8(+) T cell responses. Thus, trimming of antigenic peptides by ERAAP in the endoplasmic reticulum is essential for the generation of the normal repertoire of processed peptides.

Authors
Hammer, GE; Gonzalez, F; Champsaur, M; Cado, D; Shastri, N
MLA Citation
Hammer, GE, Gonzalez, F, Champsaur, M, Cado, D, and Shastri, N. "The aminopeptidase ERAAP shapes the peptide repertoire displayed by major histocompatibility complex class I molecules." Nature immunology 7.1 (January 2006): 103-112.
PMID
16299505
Source
epmc
Published In
Nature Immunology
Volume
7
Issue
1
Publish Date
2006
Start Page
103
End Page
112
DOI
10.1038/ni1286

Viral and bacterial infections induce expression of multiple NK cell receptors in responding CD8(+) T cells.

NK cells express several families of receptors that play central roles in target cell recognition. These NK cell receptors are also expressed by certain memory phenotype CD8(+) T cells, and in some cases are up-regulated in T cells responding to viral infection. To determine how the profile of NK receptor expression changes in murine CD8(+) T cells as they respond to intracellular pathogens, we used class I tetramer reagents to directly examine Ag-specific T cells during lymphocytic choriomeningitis virus and Listeria monocytogenes infections. We found that the majority of pathogen-specific CD8(+) T cells initiated expression of the inhibitory CD94/NKG2A heterodimer, the KLRG1 receptor, and a novel murine NK cell marker (10D7); conversely, very few Ag-specific T cells expressed Ly49 family members. The up-regulation of these receptors was independent of IL-15 and persisted long after clearance of the pathogen. The expression of CD94/NKG2A was rapidly initiated in naive CD8(+) T cells responding to peptide Ags in vitro and on many of the naive T cells that proliferate when transferred into lymphopenic (Rag-1(-/-)) hosts. Thus, CD94/NKG2A expression is a common consequence of CD8(+) T cell activation. Binding of the CD94/NKG2A receptor by its ligand (Qa-1(b)) did not significantly inhibit CD8(+) T cell effector functions. However, expression of CD94 and NKG2A transgenes partially inhibited early events of T cell activation. These subtle effects suggest that CD94/NKG2A-mediated inhibition of T cells may be limited to particular circumstances or may synergize with other receptors that are similarly up-regulated.

Authors
McMahon, CW; Zajac, AJ; Jamieson, AM; Corral, L; Hammer, GE; Ahmed, R; Raulet, DH
MLA Citation
McMahon, CW, Zajac, AJ, Jamieson, AM, Corral, L, Hammer, GE, Ahmed, R, and Raulet, DH. "Viral and bacterial infections induce expression of multiple NK cell receptors in responding CD8(+) T cells." Journal of immunology (Baltimore, Md. : 1950) 169.3 (August 2002): 1444-1452.
PMID
12133970
Source
epmc
Published In
Journal of immunology (Baltimore, Md. : 1950)
Volume
169
Issue
3
Publish Date
2002
Start Page
1444
End Page
1452
DOI
10.4049/jimmunol.169.3.1444
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