5j5e - Revision history

OCA at 09:41, 27 September 2023

2023-09-27T09:41:48Z

←Older revision		Revision as of 09:41, 27 September 2023
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	<StructureSection load='5j5e' size='340' side='right'caption='[[5j5e]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='5j5e' size='340' side='right'caption='[[5j5e]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5j5e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J5E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5j5e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J5E FirstGlance]. <br>
-	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~ERAP1~~, ~~APPILS, ARTS1, KIAA0525, UNQ584/PRO1154 (~~[~~https://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=9606 HUMAN])~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.8Å</td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5j5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j5e OCA], [https://pdbe.org/5j5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j5e RCSB], [https://www.ebi.ac.uk/pdbsum/5j5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j5e ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5j5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j5e OCA], [https://pdbe.org/5j5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j5e RCSB], [https://www.ebi.ac.uk/pdbsum/5j5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j5e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ERAP1_HUMAN ERAP1_HUMAN]] Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney.<ref>PMID:15908954</ref> <ref>PMID:16286653</ref> <ref>PMID:21478864</ref>	+	[https://www.uniprot.org/uniprot/ERAP1_HUMAN ERAP1_HUMAN] Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney.<ref>PMID:15908954</ref> <ref>PMID:16286653</ref> <ref>PMID:21478864</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Gandhi, A]]	+	[[Category: Gandhi A]]
-	[[Category: Guo, H C]]	+	[[Category: Guo H-C]]
-	[[Category: Sui, L]]	+	[[Category: Sui L]]
-	~~[[Category: Aminopeptidase]]~~	+
-	~~[[Category: Hydrolase~~]]	+

OCA at 10:13, 19 May 2021

2021-05-19T10:13:24Z

OCA at 16:21, 11 December 2019

2019-12-11T16:21:06Z

←Older revision		Revision as of 16:21, 11 December 2019
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	==crystal structure of antigen-ERAP1 domain complex==		==crystal structure of antigen-ERAP1 domain complex==
-	<StructureSection load='5j5e' size='340' side='right' caption='[[5j5e]], [[Resolution\|resolution]] 2.80Å' scene=''>	+	<StructureSection load='5j5e' size='340' side='right'caption='[[5j5e]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5j5e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J5E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J5E FirstGlance]. <br>		<table><tr><td colspan='2'>[[5j5e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J5E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J5E FirstGlance]. <br>
Line 18:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 5j5e" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5j5e" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Aminopeptidase 3D structures\|Aminopeptidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 23:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Gandhi, A]]		[[Category: Gandhi, A]]
	[[Category: Guo, H C]]		[[Category: Guo, H C]]

OCA at 17:50, 15 November 2017

2017-11-15T17:50:26Z

←Older revision		Revision as of 17:50, 15 November 2017
Line 3:		Line 3:
	<StructureSection load='5j5e' size='340' side='right' caption='[[5j5e]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='5j5e' size='340' side='right' caption='[[5j5e]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5j5e]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J5E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J5E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5j5e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J5E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J5E FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5j5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j5e OCA], [http://pdbe.org/5j5e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j5e RCSB], [http://www.ebi.ac.uk/pdbsum/5j5e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j5e ProSAT]</span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ERAP1, APPILS, ARTS1, KIAA0525, UNQ584/PRO1154 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5j5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j5e OCA], [http://pdbe.org/5j5e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j5e RCSB], [http://www.ebi.ac.uk/pdbsum/5j5e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j5e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 21:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Gandhi, A]]		[[Category: Gandhi, A]]
	[[Category: Guo, H C]]		[[Category: Guo, H C]]

OCA at 11:35, 12 April 2017

2017-04-12T11:35:29Z

←Older revision		Revision as of 11:35, 12 April 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5j5e is ~~ON HOLD~~	+	==crystal structure of antigen-ERAP1 domain complex==
		+	<StructureSection load='5j5e' size='340' side='right' caption='[[5j5e]], [[Resolution\|resolution]] 2.80Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5j5e]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J5E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J5E FirstGlance]. <br>
		+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5j5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j5e OCA], [http://pdbe.org/5j5e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j5e RCSB], [http://www.ebi.ac.uk/pdbsum/5j5e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j5e ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ERAP1_HUMAN ERAP1_HUMAN]] Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney.<ref>PMID:15908954</ref> <ref>PMID:16286653</ref> <ref>PMID:21478864</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Endoplasmic reticulum aminopeptidase 1 (ERAP1) is an essential component of the immune system, because it trims peptide precursors and generates the N--restricted epitopes. To examine ERAP1's unique properties of length- and sequence-dependent processing of antigen precursors, we report a 2.3 A resolution complex structure of the ERAP1 regulatory domain. Our study reveals a binding conformation of ERAP1 to the carboxyl terminus of a peptide, and thus provides direct evidence for the molecular ruler mechanism.

-	~~Authors~~:	+	Structural insights into the molecular ruler mechanism of the endoplasmic reticulum aminopeptidase ERAP1.,Gandhi A, Lakshminarasimhan D, Sun Y, Guo HC Sci Rep. 2011;1:186. Epub 2011 Dec 13. PMID:22355701<ref>PMID:22355701</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5j5e" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Gandhi, A]]
		+	[[Category: Guo, H C]]
		+	[[Category: Sui, L]]
		+	[[Category: Aminopeptidase]]
		+	[[Category: Hydrolase]]

OCA at 07:51, 5 April 2017

2017-04-05T07:51:16Z

←Older revision		Revision as of 07:51, 5 April 2017
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5j5e is ON HOLD ~~until Paper Publication~~	+	The entry 5j5e is ON HOLD

-	Authors: ~~Sui, L., Gandhi, A., Guo, H.-C.~~	+	Authors:

-	Description: ~~crystal structure of antigen-ERAP1 domain complex~~	+	Description:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Sui, L]]
-	[[Category: Gandhi, A]]
-	[[Category: Guo, H.-C]]

OCA: Protected "5j5e" [edit=sysop:move=sysop]

2016-05-11T01:29:13Z

Protected "5j5e" [edit=sysop:move=sysop]

←Older revision

Revision as of 01:29, 11 May 2016

OCA: New page: '''Unreleased structure''' The entry 5j5e is ON HOLD until Paper Publication Authors: Sui, L., Gandhi, A., Guo, H.-C. Description: crystal structure of antigen-ERAP1 domain complex [[C...

2016-05-11T01:29:12Z

New page: '''Unreleased structure''' The entry 5j5e is ON HOLD until Paper Publication Authors: Sui, L., Gandhi, A., Guo, H.-C. Description: crystal structure of antigen-ERAP1 domain complex [[C...

New page

'''Unreleased structure'''

The entry 5j5e is ON HOLD until Paper Publication

Authors: Sui, L., Gandhi, A., Guo, H.-C.

Description: crystal structure of antigen-ERAP1 domain complex
[[Category: Unreleased Structures]]
[[Category: Sui, L]]
[[Category: Gandhi, A]]
[[Category: Guo, H.-C]]

←Older revision		Revision as of 10:13, 19 May 2021
Line 3:		Line 3:
	<StructureSection load='5j5e' size='340' side='right'caption='[[5j5e]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='5j5e' size='340' side='right'caption='[[5j5e]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5j5e]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J5E OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5J5E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5j5e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J5E FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ERAP1, APPILS, ARTS1, KIAA0525, UNQ584/PRO1154 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ERAP1, APPILS, ARTS1, KIAA0525, UNQ584/PRO1154 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5j5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j5e OCA], [~~http~~://pdbe.org/5j5e PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5j5e RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5j5e PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5j5e ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5j5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j5e OCA], [https://pdbe.org/5j5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j5e RCSB], [https://www.ebi.ac.uk/pdbsum/5j5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j5e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ERAP1_HUMAN ERAP1_HUMAN]] Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney.<ref>PMID:15908954</ref> <ref>PMID:16286653</ref> <ref>PMID:21478864</ref>	+	[[https://www.uniprot.org/uniprot/ERAP1_HUMAN ERAP1_HUMAN]] Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney.<ref>PMID:15908954</ref> <ref>PMID:16286653</ref> <ref>PMID:21478864</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
-	Endoplasmic reticulum aminopeptidase 1 (ERAP1) is ~~an essential component~~ of ~~the immune system, because it trims~~ peptide precursors ~~and generates~~ the N--restricted epitopes. To ~~examine~~ ERAP1's unique ~~properties of length~~- and ~~sequence~~-dependent ~~processing~~ of ~~antigen precursors~~, we report a 2.~~3 A~~ resolution ~~complex~~ structure of the ERAP1 regulatory domain. ~~Our study~~ reveals ~~a binding conformation~~ of ERAP1 to the carboxyl ~~terminus~~ of ~~a peptide~~, and ~~thus provides direct evidence for~~ the ~~molecular ruler mechanism~~.	+	Endoplasmic reticulum aminopeptidase 1 (ERAP1) is involved in the final processing of peptide precursors to generate the N-termini of MHC class I-restricted epitopes. ERAP1 thus influences immunodominance and cytotoxic immune responses by controlling the peptide repertoire available for cell surface presentation by MHC molecules. To enable this critical role in antigen processing, ERAP1 trims peptides by a unique molecular ruler mechanism that turns on/off hydrolysis activity in a peptide-length and -sequence dependent manner. Thus unlike other aminopeptidases, ERAP1 could recognize both the N- and C-termini of peptides in order to read the substrate's length. To exemplify and validate this molecular ruler mechanism, we have carried out crystallographic studies on molecular recognition of antigenic peptide's C-terminus by ERAP1. In this report, we have determined a 2.8A-resolution crystal structure of an intermolecular complex between the ERAP1 regulatory domain and a natural epitope's C-terminus displayed in a fusion protein. It reveals the structural details of peptide's C-termini recognition by ERAP1. ERAP1 uses specificity pockets on the regulatory domain to bind the peptide's carboxyl end and side chain of the C-terminal anchoring residue. At the same time, flexibility in length and sequence at the middle of peptides is accommodated by a kink with minimal interactions with ERAP1.

-	~~Structural insights into the molecular ruler mechanism~~ of the ~~endoplasmic reticulum~~ aminopeptidase ~~ERAP1~~.,Gandhi A~~, Lakshminarasimhan D, Sun Y~~, Guo HC ~~Sci Rep~~. ~~2011~~;1:~~186~~. Epub ~~2011 Dec 13~~. PMID:~~22355701~~<ref>PMID:~~22355701~~</ref>	+	Crystal structure of a polypeptide's C-terminus in complex with the regulatory domain of ER aminopeptidase 1.,Sui L, Gandhi A, Guo HC Mol Immunol. 2016 Dec;80:41-49. doi: 10.1016/j.molimm.2016.10.012. Epub 2016 Nov , 5. PMID:27825049<ref>PMID:27825049</ref>

	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>