7q4m - Revision history

OCA at 07:42, 8 March 2023

OCA — Wed, 08 Mar 2023 07:42:16 GMT

←Older revision		Revision as of 07:42, 8 March 2023
Line 8:		Line 8:
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/A4_HUMAN A4_HUMAN]] Defects in APP are the cause of Alzheimer disease type 1 (AD1) [MIM:[https://omim.org/entry/104300 104300]]. AD1 is a familial early-onset form of Alzheimer disease. It can be associated with cerebral amyloid angiopathy. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death.<ref>PMID:8476439</ref> <ref>PMID:15201367</ref> <ref>PMID:1671712</ref> <ref>PMID:1908231</ref> <ref>PMID:1678058</ref> <ref>PMID:1944558</ref> <ref>PMID:1925564</ref> <ref>PMID:1415269</ref> <ref>PMID:1303239</ref> <ref>PMID:1302033</ref> <ref>PMID:1303275</ref> <ref>PMID:8267572</ref> <ref>PMID:8290042</ref> <ref>PMID:8577393</ref> <ref>PMID:9328472</ref> <ref>PMID:9754958</ref> <ref>PMID:10097173</ref> <ref>PMID:10631141</ref> <ref>PMID:10665499</ref> <ref>PMID:10867787</ref> <ref>PMID:11063718</ref> <ref>PMID:11311152</ref> <ref>PMID:11528419</ref> <ref>PMID:12034808</ref> <ref>PMID:15365148</ref> <ref>PMID:15668448</ref> Defects in APP are the cause of cerebral amyloid angiopathy APP-related (CAA-APP) [MIM:[https://omim.org/entry/605714 605714]]. A hereditary localized amyloidosis due to amyloid-beta A4 peptide(s) deposition in the cerebral vessels. The principal clinical characteristics are recurrent cerebral and cerebellar hemorrhages, recurrent strokes, cerebral ischemia, cerebral infarction, and progressive mental deterioration. Patients develop cerebral hemorrhage because of the severe cerebral amyloid angiopathy. Parenchymal amyloid deposits are rare and largely in the form of pre-amyloid lesions or diffuse plaque-like structures. They are Congo red negative and lack the dense amyloid cores commonly present in Alzheimer disease. Some affected individuals manifest progressive aphasic dementia, leukoencephalopathy, and occipital calcifications.<ref>PMID:10821838</ref> <ref>PMID:2111584</ref> <ref>PMID:11409420</ref> <ref>PMID:12654973</ref> <ref>PMID:16178030</ref>	+	[https://www.uniprot.org/uniprot/A4_HUMAN A4_HUMAN] Defects in APP are the cause of Alzheimer disease type 1 (AD1) [MIM:[https://omim.org/entry/104300 104300]. AD1 is a familial early-onset form of Alzheimer disease. It can be associated with cerebral amyloid angiopathy. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death.<ref>PMID:8476439</ref> <ref>PMID:15201367</ref> <ref>PMID:1671712</ref> <ref>PMID:1908231</ref> <ref>PMID:1678058</ref> <ref>PMID:1944558</ref> <ref>PMID:1925564</ref> <ref>PMID:1415269</ref> <ref>PMID:1303239</ref> <ref>PMID:1302033</ref> <ref>PMID:1303275</ref> <ref>PMID:8267572</ref> <ref>PMID:8290042</ref> <ref>PMID:8577393</ref> <ref>PMID:9328472</ref> <ref>PMID:9754958</ref> <ref>PMID:10097173</ref> <ref>PMID:10631141</ref> <ref>PMID:10665499</ref> <ref>PMID:10867787</ref> <ref>PMID:11063718</ref> <ref>PMID:11311152</ref> <ref>PMID:11528419</ref> <ref>PMID:12034808</ref> <ref>PMID:15365148</ref> <ref>PMID:15668448</ref> Defects in APP are the cause of cerebral amyloid angiopathy APP-related (CAA-APP) [MIM:[https://omim.org/entry/605714 605714]. A hereditary localized amyloidosis due to amyloid-beta A4 peptide(s) deposition in the cerebral vessels. The principal clinical characteristics are recurrent cerebral and cerebellar hemorrhages, recurrent strokes, cerebral ischemia, cerebral infarction, and progressive mental deterioration. Patients develop cerebral hemorrhage because of the severe cerebral amyloid angiopathy. Parenchymal amyloid deposits are rare and largely in the form of pre-amyloid lesions or diffuse plaque-like structures. They are Congo red negative and lack the dense amyloid cores commonly present in Alzheimer disease. Some affected individuals manifest progressive aphasic dementia, leukoencephalopathy, and occipital calcifications.<ref>PMID:10821838</ref> <ref>PMID:2111584</ref> <ref>PMID:11409420</ref> <ref>PMID:12654973</ref> <ref>PMID:16178030</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/A4_HUMAN A4_HUMAN]] Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), respectively. Beta-amyloid 42 is a more effective reductant than beta-amyloid 40. Beta-amyloid peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with Also bind GPC1 in lipid rafts.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain (By similarity).<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref>	+	[https://www.uniprot.org/uniprot/A4_HUMAN A4_HUMAN] Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), respectively. Beta-amyloid 42 is a more effective reductant than beta-amyloid 40. Beta-amyloid peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with Also bind GPC1 in lipid rafts.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain (By similarity).<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 26:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Arseni, D]]	+	[[Category: Arseni D]]
-	[[Category: Falcon, B]]	+	[[Category: Falcon B]]
-	[[Category: Garringer~~, H J~~]]	+	[[Category: Garringer HJ]]
-	[[Category: Gelpi, E]]	+	[[Category: Gelpi E]]
-	[[Category: Ghetti, B]]	+	[[Category: Ghetti B]]
-	[[Category: Goedert, M]]	+	[[Category: Goedert M]]
-	[[Category: Huang, M]]	+	[[Category: Huang M]]
-	[[Category: Kotecha, A]]	+	[[Category: Kotecha A]]
-	[[Category: Kovacs~~, G G~~]]	+	[[Category: Kovacs GG]]
-	[[Category: Lavenir, I]]	+	[[Category: Lavenir I]]
-	[[Category: Lovestam~~, S K.A~~]]	+	[[Category: Lovestam SKA]]
-	[[Category: Macdonald, J]]	+	[[Category: Macdonald J]]
-	[[Category: Murzin~~, A G~~]]	+	[[Category: Murzin AG]]
-	[[Category: Newell~~, K L~~]]	+	[[Category: Newell KL]]
-	[[Category: Peak-Chew~~, S Y~~]]	+	[[Category: Peak-Chew SY]]
-	[[Category: Scheres~~, H W~~]]	+	[[Category: Scheres SHW]]
-	[[Category: Schweighauser, M]]	+	[[Category: Schweighauser M]]
-	[[Category: Vidal, R]]	+	[[Category: Vidal R]]
-	[[Category: Yang, Y]]	+	[[Category: Yang Y]]
-	[[Category: Zhang, W]]	+	[[Category: Zhang W]]
-	~~[[Category: Abeta42]]~~	+
-	~~[[Category: Amyloid filament]]~~	+
-	~~[[Category: Cryo-em]]~~	+
-	~~[[Category: Human brain]]~~	+
-	~~[[Category: Protein fibril~~]]	+

OCA at 07:12, 27 January 2022

OCA — Thu, 27 Jan 2022 07:12:11 GMT

←Older revision		Revision as of 07:12, 27 January 2022
Line 1:		Line 1:

	==Type II beta-amyloid 42 Filaments from Human Brain==		==Type II beta-amyloid 42 Filaments from Human Brain==
-	<StructureSection load='7q4m' size='340' side='right'caption='[[7q4m]]' scene=''>	+	<StructureSection load='7q4m' size='340' side='right'caption='[[7q4m]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Q4M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q4M FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7q4m]] is a 10 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=7Q4M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q4M FirstGlance]. <br>
-	</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=7q4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q4m OCA], [https://pdbe.org/7q4m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q4m RCSB], [https://www.ebi.ac.uk/pdbsum/7q4m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q4m ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></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=7q4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q4m OCA], [https://pdbe.org/7q4m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q4m RCSB], [https://www.ebi.ac.uk/pdbsum/7q4m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q4m ProSAT]</span></td></tr>
	</table>		</table>
		+	== Disease ==
		+	[[https://www.uniprot.org/uniprot/A4_HUMAN A4_HUMAN]] Defects in APP are the cause of Alzheimer disease type 1 (AD1) [MIM:[https://omim.org/entry/104300 104300]]. AD1 is a familial early-onset form of Alzheimer disease. It can be associated with cerebral amyloid angiopathy. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death.<ref>PMID:8476439</ref> <ref>PMID:15201367</ref> <ref>PMID:1671712</ref> <ref>PMID:1908231</ref> <ref>PMID:1678058</ref> <ref>PMID:1944558</ref> <ref>PMID:1925564</ref> <ref>PMID:1415269</ref> <ref>PMID:1303239</ref> <ref>PMID:1302033</ref> <ref>PMID:1303275</ref> <ref>PMID:8267572</ref> <ref>PMID:8290042</ref> <ref>PMID:8577393</ref> <ref>PMID:9328472</ref> <ref>PMID:9754958</ref> <ref>PMID:10097173</ref> <ref>PMID:10631141</ref> <ref>PMID:10665499</ref> <ref>PMID:10867787</ref> <ref>PMID:11063718</ref> <ref>PMID:11311152</ref> <ref>PMID:11528419</ref> <ref>PMID:12034808</ref> <ref>PMID:15365148</ref> <ref>PMID:15668448</ref> Defects in APP are the cause of cerebral amyloid angiopathy APP-related (CAA-APP) [MIM:[https://omim.org/entry/605714 605714]]. A hereditary localized amyloidosis due to amyloid-beta A4 peptide(s) deposition in the cerebral vessels. The principal clinical characteristics are recurrent cerebral and cerebellar hemorrhages, recurrent strokes, cerebral ischemia, cerebral infarction, and progressive mental deterioration. Patients develop cerebral hemorrhage because of the severe cerebral amyloid angiopathy. Parenchymal amyloid deposits are rare and largely in the form of pre-amyloid lesions or diffuse plaque-like structures. They are Congo red negative and lack the dense amyloid cores commonly present in Alzheimer disease. Some affected individuals manifest progressive aphasic dementia, leukoencephalopathy, and occipital calcifications.<ref>PMID:10821838</ref> <ref>PMID:2111584</ref> <ref>PMID:11409420</ref> <ref>PMID:12654973</ref> <ref>PMID:16178030</ref>
		+	== Function ==
		+	[[https://www.uniprot.org/uniprot/A4_HUMAN A4_HUMAN]] Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), respectively. Beta-amyloid 42 is a more effective reductant than beta-amyloid 40. Beta-amyloid peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with Also bind GPC1 in lipid rafts.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain (By similarity).<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis.<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref> N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).<ref>PMID:9168929</ref> <ref>PMID:11544248</ref> <ref>PMID:11943163</ref> <ref>PMID:19225519</ref> <ref>PMID:19901339</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	[Figure: see text].
		+
		+	Cryo-EM structures of amyloid-beta 42 filaments from human brains.,Yang Y, Arseni D, Zhang W, Huang M, Lovestam S, Schweighauser M, Kotecha A, Murzin AG, Peak-Chew SY, Macdonald J, Lavenir I, Garringer HJ, Gelpi E, Newell KL, Kovacs GG, Vidal R, Ghetti B, Ryskeldi-Falcon B, Scheres SHW, Goedert M Science. 2022 Jan 14;375(6577):167-172. doi: 10.1126/science.abm7285. Epub 2022, Jan 13. PMID:35025654<ref>PMID:35025654</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7q4m" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Arseni D]]	+	[[Category: Arseni, D]]
-	[[Category: Falcon B]]	+	[[Category: Falcon, B]]
-	[[Category: Garringer HJ]]	+	[[Category: Garringer, H J]]
-	[[Category: Gelpi E]]	+	[[Category: Gelpi, E]]
-	[[Category: Ghetti B]]	+	[[Category: Ghetti, B]]
-	[[Category: Goedert M]]	+	[[Category: Goedert, M]]
-	[[Category: Huang M]]	+	[[Category: Huang, M]]
-	[[Category: Kotecha A]]	+	[[Category: Kotecha, A]]
-	[[Category: Kovacs GG]]	+	[[Category: Kovacs, G G]]
-	[[Category: Lavenir I]]	+	[[Category: Lavenir, I]]
-	[[Category: Lovestam ~~SKA~~]]	+	[[Category: Lovestam, S K.A]]
-	[[Category: Macdonald J]]	+	[[Category: Macdonald, J]]
-	[[Category: Murzin AG]]	+	[[Category: Murzin, A G]]
-	[[Category: Newell KL]]	+	[[Category: Newell, K L]]
-	[[Category: Peak-Chew SY]]	+	[[Category: Peak-Chew, S Y]]
-	[[Category: Scheres HW]]	+	[[Category: Scheres, H W]]
-	[[Category: Schweighauser M]]	+	[[Category: Schweighauser, M]]
-	[[Category: Vidal R]]	+	[[Category: Vidal, R]]
-	[[Category: Yang Y]]	+	[[Category: Yang, Y]]
-	[[Category: Zhang W]]	+	[[Category: Zhang, W]]
		+	[[Category: Abeta42]]
		+	[[Category: Amyloid filament]]
		+	[[Category: Cryo-em]]
		+	[[Category: Human brain]]
		+	[[Category: Protein fibril]]

OCA at 12:37, 24 November 2021

OCA — Wed, 24 Nov 2021 12:37:40 GMT

←Older revision		Revision as of 12:37, 24 November 2021
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 7q4m ~~is ON HOLD~~	+	==Type II beta-amyloid 42 Filaments from Human Brain==
-		+	<StructureSection load='7q4m' size='340' side='right'caption='[[7q4m]]' scene=''>
-	~~Authors~~: ~~Yang, Y~~.~~, Arseni, D~~.~~, Zhang, W~~.~~, Huang, M~~.~~, Lovestam, S~~.K.A.~~, Schweighauser, M~~.~~, Kotecha, A~~., ~~Murzin, A~~.G.~~, Peak~~-~~Chew~~, ~~S.Y~~., ~~Macdonald, J~~.~~, Lavenir, I~~.~~, Garringer, H.J~~., ~~Gelpi, E~~.~~, Newell, K~~.L., ~~Kovacs, G~~.~~G., Vidal, R., Ghetti, B., Falcon, B., Scheres, H.W., Goedert, M~~.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Q4M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q4M FirstGlance]. <br>
-	~~Description: Type II beta-amyloid 42 Filaments from Human Brain~~	+	</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=7q4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q4m OCA], [https://pdbe.org/7q4m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q4m RCSB], [https://www.ebi.ac.uk/pdbsum/7q4m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q4m ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
-	[[Category: ~~Goedert, M~~]]	+	__TOC__
-	[[Category: ~~Garringer, H.J~~]]	+	</StructureSection>
-	[[Category: ~~Yang, Y~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Zhang, W~~]]	+	[[Category: Arseni D]]
-	[[Category: ~~Gelpi, E~~]]	+	[[Category: Falcon B]]
-	[[Category: ~~Macdonald, J~~]]	+	[[Category: Garringer HJ]]
-	[[Category: ~~Falcon, B~~]]	+	[[Category: Gelpi E]]
-	[[Category: ~~Kovacs, G.G~~]]	+	[[Category: Ghetti B]]
-	[[Category: ~~Schweighauser, M~~]]	+	[[Category: Goedert M]]
-	[[Category: Lavenir, I]]	+	[[Category: Huang M]]
-	[[Category: ~~Kotecha, A~~]]	+	[[Category: Kotecha A]]
-	[[Category: ~~Arseni, D~~]]	+	[[Category: Kovacs GG]]
-	[[Category: ~~Ghetti, B~~]]	+	[[Category: Lavenir I]]
-	[[Category: ~~Peak-Chew, S.Y~~]]	+	[[Category: Lovestam SKA]]
-	[[Category: ~~Scheres, H.W~~]]	+	[[Category: Macdonald J]]
-	[[Category: ~~Huang, M~~]]	+	[[Category: Murzin AG]]
-	[[Category: ~~Lovestam, S.K.A~~]]	+	[[Category: Newell KL]]
-	[[Category: Vidal, R]]	+	[[Category: Peak-Chew SY]]
-	[[Category: ~~Newell, K.L~~]]	+	[[Category: Scheres HW]]
-	[[Category: ~~Murzin, A.G~~]]	+	[[Category: Schweighauser M]]
		+	[[Category: Vidal R]]
		+	[[Category: Yang Y]]
		+	[[Category: Zhang W]]

OCA: Protected "7q4m" [edit=sysop:move=sysop]

OCA — Wed, 10 Nov 2021 05:10:56 GMT

Protected "7q4m" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:10, 10 November 2021

OCA: New page: '''Unreleased structure''' The entry 7q4m is ON HOLD Authors: Yang, Y., Arseni, D., Zhang, W., Huang, M., Lovestam, S.K.A., Schweighauser, M., Kotecha, A., Murzin, A.G., Peak-Chew, S.Y....

OCA — Wed, 10 Nov 2021 05:10:56 GMT

New page: '''Unreleased structure''' The entry 7q4m is ON HOLD Authors: Yang, Y., Arseni, D., Zhang, W., Huang, M., Lovestam, S.K.A., Schweighauser, M., Kotecha, A., Murzin, A.G., Peak-Chew, S.Y....

New page

'''Unreleased structure'''

The entry 7q4m is ON HOLD

Authors: Yang, Y., Arseni, D., Zhang, W., Huang, M., Lovestam, S.K.A., Schweighauser, M., Kotecha, A., Murzin, A.G., Peak-Chew, S.Y., Macdonald, J., Lavenir, I., Garringer, H.J., Gelpi, E., Newell, K.L., Kovacs, G.G., Vidal, R., Ghetti, B., Falcon, B., Scheres, H.W., Goedert, M.

Description: Type II beta-amyloid 42 Filaments from Human Brain
[[Category: Unreleased Structures]]
[[Category: Goedert, M]]
[[Category: Garringer, H.J]]
[[Category: Yang, Y]]
[[Category: Zhang, W]]
[[Category: Gelpi, E]]
[[Category: Macdonald, J]]
[[Category: Falcon, B]]
[[Category: Kovacs, G.G]]
[[Category: Schweighauser, M]]
[[Category: Lavenir, I]]
[[Category: Kotecha, A]]
[[Category: Arseni, D]]
[[Category: Ghetti, B]]
[[Category: Peak-Chew, S.Y]]
[[Category: Scheres, H.W]]
[[Category: Huang, M]]
[[Category: Lovestam, S.K.A]]
[[Category: Vidal, R]]
[[Category: Newell, K.L]]
[[Category: Murzin, A.G]]