(Q37104697)

English

SDF2L1, a component of the endoplasmic reticulum chaperone complex, differentially interacts with {alpha}-, {beta}-, and {theta}-defensin propeptides

scientific article published on 24 December 2008

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

SDF2L1, a component of the endoplasmic reticulum chaperone complex, differentially interacts with {alpha}-, {beta}-, and {theta}-defensin propeptides (English)

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

endoplasmic reticulum

0 references

molecular chaperones

0 references

author name string

Prasad Tongaonkar

1

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

Michael E Selsted

2

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

language of work or name

0 references

publication date

24 December 2008

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

284

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

9

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

5602-5609

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

1 reference

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Mixed-disulfide folding intermediates between thyroglobulin and endoplasmic reticulum resident oxidoreductases ERp57 and protein disulfide isomerase.

1 reference

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Mammalian defensins in the antimicrobial immune response

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Antibacterial activity and specificity of the six human {alpha}-defensins

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1 reference

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Theta defensins protect cells from infection by herpes simplex virus by inhibiting viral adhesion and entry

1 reference

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Human epithelial beta-defensins 2 and 3 inhibit HIV-1 replication

1 reference

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A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins

1 reference

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Paneth cell trypsin is the processing enzyme for human defensin-5.

1 reference

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Murine and human SDF2L1 is an endoplasmic reticulum stress-inducible gene and encodes a new member of the Pmt/rt protein family

1 reference

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Mechanisms for induction of acquired host immunity by neutrophil peptide defensins

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Multiple molecular chaperones interact with apolipoprotein B during its maturation. The network of endoplasmic reticulum-resident chaperones (ERp72, GRP94, calreticulin, and BiP) interacts with apolipoprotein b regardless of its lipidation state

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Mutational analysis of the ligand binding site of the inositol 1,4,5-trisphosphate receptor

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Identification of defensin-1, defensin-2, and CAP37/azurocidin as T-cell chemoattractant proteins released from interleukin-8-stimulated neutrophils

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14 September 2017

Several endoplasmic reticulum stress proteins, including ERp72, interact with thyroglobulin during its maturation

1 reference

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Direct inactivation of viruses by human granulocyte defensins

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Posttranslational processing of defensins in immature human myeloid cells

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Structural analysis of human beta-defensin-1 and its significance in urinary tract infection

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Defensins act as potent adjuvants that promote cellular and humoral immune responses in mice to a lymphoma idiotype and carrier antigens

1 reference

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Human alpha-defensin 1 (HNP-1) inhibits adenoviral infection in vitro

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Identifiers

10.1074/JBC.M806664200

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

18 August 2017

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