| Type |
Details |
Score |
| Publication |
| First Author: |
Zhang L |
| Year: |
2024 |
| Journal: |
Commun Biol |
| Title: |
Glutamate oxaloacetate transaminase 1 is dispensable in macrophage differentiation and anti-pathogen response. |
| Volume: |
7 |
| Issue: |
1 |
| Pages: |
817 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Martinez-Terroba E |
| Year: |
2024 |
| Journal: |
Sci Immunol |
| Title: |
Overexpression of Malat1 drives metastasis through inflammatory reprogramming of the tumor microenvironment. |
| Volume: |
9 |
| Issue: |
96 |
| Pages: |
eadh5462 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Reizel Y |
| Year: |
2015 |
| Journal: |
Genes Dev |
| Title: |
Gender-specific postnatal demethylation and establishment of epigenetic memory. |
| Volume: |
29 |
| Issue: |
9 |
| Pages: |
923-33 |
|
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•
•
|
| Publication |
| First Author: |
Samara C |
| Year: |
2013 |
| Journal: |
Front Cell Neurosci |
| Title: |
Neuronal activity in the hub of extrasynaptic Schwann cell-axon interactions. |
| Volume: |
7 |
|
| Pages: |
228 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Ray S |
| Year: |
2015 |
| Journal: |
G3 (Bethesda) |
| Title: |
An Examination of Dynamic Gene Expression Changes in the Mouse Brain During Pregnancy and the Postpartum Period. |
| Volume: |
6 |
| Issue: |
1 |
| Pages: |
221-33 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Lavin Y |
| Year: |
2014 |
| Journal: |
Cell |
| Title: |
Tissue-resident macrophage enhancer landscapes are shaped by the local microenvironment. |
| Volume: |
159 |
| Issue: |
6 |
| Pages: |
1312-26 |
|
•
•
•
•
•
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| Publication |
| First Author: |
M Real F |
| Year: |
2020 |
| Journal: |
Science |
| Title: |
The mole genome reveals regulatory rearrangements associated with adaptive intersexuality. |
| Volume: |
370 |
| Issue: |
6513 |
| Pages: |
208-214 |
|
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•
•
•
•
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| Publication |
| First Author: |
Sun L |
| Year: |
2013 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Long noncoding RNAs regulate adipogenesis. |
| Volume: |
110 |
| Issue: |
9 |
| Pages: |
3387-92 |
|
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•
•
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| Publication |
| First Author: |
Bonthuis PJ |
| Year: |
2015 |
| Journal: |
Cell Rep |
| Title: |
Noncanonical Genomic Imprinting Effects in Offspring. |
| Volume: |
12 |
| Issue: |
6 |
| Pages: |
979-91 |
|
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•
•
•
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| Publication |
| First Author: |
Shi X |
| Year: |
2024 |
| Journal: |
Sci Adv |
| Title: |
Compromised macrophages contribute to progression of MASH to hepatocellular carcinoma in FGF21KO mice. |
| Volume: |
10 |
| Issue: |
43 |
| Pages: |
eado9311 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Binns MM |
| Year: |
1985 |
| Journal: |
J Gen Virol |
| Title: |
Cloning and sequencing of the gene encoding the spike protein of the coronavirus IBV. |
| Volume: |
66 ( Pt 4) |
|
| Pages: |
719-26 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Godeke GJ |
| Year: |
2000 |
| Journal: |
J Virol |
| Title: |
Assembly of spikes into coronavirus particles is mediated by the carboxy-terminal domain of the spike protein. |
| Volume: |
74 |
| Issue: |
3 |
| Pages: |
1566-71 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Chang KW |
| Year: |
2000 |
| Journal: |
Virology |
| Title: |
Coronavirus-induced membrane fusion requires the cysteine-rich domain in the spike protein. |
| Volume: |
269 |
| Issue: |
1 |
| Pages: |
212-24 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Belouzard S |
| Year: |
2009 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites. |
| Volume: |
106 |
| Issue: |
14 |
| Pages: |
5871-6 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Lu G |
| Year: |
2015 |
| Journal: |
Trends Microbiol |
| Title: |
Bat-to-human: spike features determining 'host jump' of coronaviruses SARS-CoV, MERS-CoV, and beyond. |
| Volume: |
23 |
| Issue: |
8 |
| Pages: |
468-78 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Schwartz C |
| Year: |
2019 |
| Journal: |
Allergy |
| Title: |
Spontaneous atopic dermatitis in mice with a defective skin barrier is independent of ILC2 and mediated by IL-1β. |
| Volume: |
74 |
| Issue: |
10 |
| Pages: |
1920-1933 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Zhou W |
| Year: |
2022 |
| Journal: |
Nature |
| Title: |
ZBTB46 defines and regulates ILC3s that protect the intestine. |
| Volume: |
609 |
| Issue: |
7925 |
| Pages: |
159-165 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Godinho-Silva C |
| Year: |
2019 |
| Journal: |
Nature |
| Title: |
Light-entrained and brain-tuned circadian circuits regulate ILC3s and gut homeostasis. |
| Volume: |
574 |
| Issue: |
7777 |
| Pages: |
254-258 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Papaioannou NE |
| Year: |
2021 |
| Journal: |
Nat Commun |
| Title: |
Environmental signals rather than layered ontogeny imprint the function of type 2 conventional dendritic cells in young and adult mice. |
| Volume: |
12 |
| Issue: |
1 |
| Pages: |
464 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Pierson W |
| Year: |
2013 |
| Journal: |
Nat Immunol |
| Title: |
Antiapoptotic Mcl-1 is critical for the survival and niche-filling capacity of Foxp3⁺ regulatory T cells. |
| Volume: |
14 |
| Issue: |
9 |
| Pages: |
959-65 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kuno A |
| Year: |
2022 |
| Journal: |
PLoS Biol |
| Title: |
DAJIN enables multiplex genotyping to simultaneously validate intended and unintended target genome editing outcomes. |
| Volume: |
20 |
| Issue: |
1 |
| Pages: |
e3001507 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
2201
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
2126
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
2126
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
2151
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Zhang W |
| Year: |
2018 |
| Journal: |
Biochem Biophys Res Commun |
| Title: |
Structural characterization of the HCoV-229E fusion core. |
| Volume: |
497 |
| Issue: |
2 |
| Pages: |
705-712 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Yan L |
| Year: |
2018 |
| Journal: |
Acta Crystallogr D Struct Biol |
| Title: |
Crystal structure of the post-fusion core of the Human coronavirus 229E spike protein at 1.86 Å resolution. |
| Volume: |
74 |
| Issue: |
Pt 9 |
| Pages: |
841-851 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
304
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
110
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
109
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
170
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
211
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
179
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
170
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
167
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
251
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
170
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
165
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
170
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
110
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
170
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
167
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Millet JK |
| Year: |
2015 |
| Journal: |
Virus Res |
| Title: |
Host cell proteases: Critical determinants of coronavirus tropism and pathogenesis. |
| Volume: |
202 |
|
| Pages: |
120-34 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Coutard B |
| Year: |
2020 |
| Journal: |
Antiviral Res |
| Title: |
The spike glycoprotein of the new coronavirus 2019-nCoV contains a furin-like cleavage site absent in CoV of the same clade. |
| Volume: |
176 |
|
| Pages: |
104742 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Shulla A |
| Year: |
2009 |
| Journal: |
J Biol Chem |
| Title: |
Role of spike protein endodomains in regulating coronavirus entry. |
| Volume: |
284 |
| Issue: |
47 |
| Pages: |
32725-34 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
The type I glycoprotein S of Coronavirus, trimers of which constitute the typical viral spikes, is assembled into virions through noncovalent interactions with the M protein. The spike glycoprotein is translated as a large polypeptide that is subsequently cleaved to S1 () and S2 []. The cleavage of S can occur at two distinct sites: S2 or S2' []. The spike is present in two very different forms: pre-fusion (the form on mature virions) and post-fusion (the form after membrane fusion has been completed). The spike is cleaved sequentially by host proteases at two sites: first at the S1/S2 boundary (i.e. S1/S2 site) and second within S2 (i.e. S2' site). After the cleavages, S1 dissociates from S2, allowing S2 to transition to the post-fusion structure []. Both chimeric S proteins appeared to cause cell fusion when expressed individually, suggesting that they were biologically fully active []. The spike is a type I membrane glycoprotein that possesses a conserved transmembrane anchor and an unusual cysteine-rich (cys) domain that bridges the putative junction of the anchor and the cytoplasmic tail [].SARS-CoV S is largely uncleaved after biosynthesis. It can be later processed by endosomal cathepsin L, trypsin, thermolysin, and elastase, which are shown to induce syncytia formation and virus entry. Other proteases that are of potential biological relevance in potentiating SARS-CoV S include TMPRSS2, TMPRSS11a, and HAT which are localized on the cell surface and are highly expressed in the human airway []. The furin-like S2' cleavage site at KR/SF with P1 and P2 basic residues and a P2' hydrophobic Phe downstream of the IFP is identical between the SARS-CoV-2 and SARS-CoV. One or more furin-like enzymes would cleave the S2' site at KR/SF [, ]. Deletion of SARS-CoV-2 furin cleavage site suggests that it may not be required for viral entry but may affect replication kinetics and altered sites have been still seen proteolytically cleaved. Several substitutions within the S2' cleavage domain of SARS-COV-2 have been reported, including P812L/S/T, S813I/G, F817L, I818S/V, but further experimental study of their consequences and the replication properties of the altered viruses are required to understand the role of furin cleavage in SARS-CoV-2 infection and virulence []. The S2 subunit normally contains multiple key components, including one or more fusion peptides (FP), a second proteolytic site (S2') and two conserved heptad repeats (HRs), driving membrane penetration and virus-cell fusion. The HRs can trimerize into a coiled-coil structure built of three HR1-HR2 helical hairpins presenting as a canonical six-helix bundle and drag the virus envelope and the host cell bilayer into close proximity, preparing for fusion to occur []. The fusion core is composed of HR1 and HR2 and at least three membranotropic regions that are denoted as the fusion peptide (FP), internal fusion peptide (IFP), and pretransmembrane domain (PTM). The HR regions are further flanked by the three membranotropic components. Both FP and IFP are located upstream of HR1, while PTM is distally downstream of HR2 and directly precedes the transmembrane domain of SARS-CoV S. All of these three components are able to partition into the phospholipid bilayer to disturb membrane integrity. []. During the pandemic, many conservative amino acid changes in FP segment of SARS-CoV-2 have been reported (i.e., L821I, L822F, K825R, V826L, T827I, L828P, A829T, D830G/A, A831V/S/T, G832C/S, F833S, I834T), although their impact is not known as the active conformation and mode of insertion of SARS-CoV-2 fusion peptide have not been experimentally characterised. Differences in HR1 sequences between SARS-CoV and SARS-CoV-2 suggest that SARS-CoV-2 HR2 makes stronger interactions with HR1. However, the substitutions observed in the solvent accessible surface of the HR1 domain (e.g., D936Y, S943P, S939F) of SARS-CoV-2 do not seem to be involved in stabilizing interactions with HR2. Substitutions in HR2 (e.g., K1073N, V1176F) or the TM or cytoplasmic tail domains have also been observed, but further experimental work is required to determine the effects of these changes [].This entry represents the cysteine rich intravirion region found at the C-terminal of coronavirus spike proteins (S) []. These cysteine residues are targets for palmitoylation, necessary for efficiently S incorporation into virions and S-mediated membrane fusions. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
The type I glycoprotein S of Coronavirus, trimers of which constitute the typical viral spikes, is assembled into virions through noncovalent interactions with the M protein. The spike glycoprotein is translated as a large polypeptide that is subsequently cleaved to S1 () and S2 []. The cleavage of S can occur at two distinct sites: S2 or S2' []. The spike is present in two very different forms: pre-fusion (the form on mature virions) and post-fusion (the form after membrane fusion has been completed). The spike is cleaved sequentially by host proteases at two sites: first at the S1/S2 boundary (i.e. S1/S2 site) and second within S2 (i.e. S2' site). After the cleavages, S1 dissociates from S2, allowing S2 to transition to the post-fusion structure []. Both chimeric S proteins appeared to cause cell fusion when expressed individually, suggesting that they were biologically fully active []. The spike is a type I membrane glycoprotein that possesses a conserved transmembrane anchor and an unusual cysteine-rich (cys) domain that bridges the putative junction of the anchor and the cytoplasmic tail [].SARS-CoV S is largely uncleaved after biosynthesis. It can be later processed by endosomal cathepsin L, trypsin, thermolysin, and elastase, which are shown to induce syncytia formation and virus entry. Other proteases that are of potential biological relevance in potentiating SARS-CoV S include TMPRSS2, TMPRSS11a, and HAT which are localized on the cell surface and are highly expressed in the human airway []. The furin-like S2' cleavage site at KR/SF with P1 and P2 basic residues and a P2' hydrophobic Phe downstream of the IFP is identical between the SARS-CoV-2 and SARS-CoV. One or more furin-like enzymes would cleave the S2' site at KR/SF [, ]. Deletion of SARS-CoV-2 furin cleavage site suggests that it may not be required for viral entry but may affect replication kinetics and altered sites have been still seen proteolytically cleaved. Several substitutions within the S2' cleavage domain of SARS-COV-2 have been reported, including P812L/S/T, S813I/G, F817L, I818S/V, but further experimental study of their consequences and the replication properties of the altered viruses are required to understand the role of furin cleavage in SARS-CoV-2 infection and virulence []. The S2 subunit normally contains multiple key components, including one or more fusion peptides (FP), a second proteolytic site (S2') and two conserved heptad repeats (HRs), driving membrane penetration and virus-cell fusion. The HRs can trimerize into a coiled-coil structure built of three HR1-HR2 helical hairpins presenting as a canonical six-helix bundle and drag the virus envelope and the host cell bilayer into close proximity, preparing for fusion to occur []. The fusion core is composed of HR1 and HR2 and at least three membranotropic regions that are denoted as the fusion peptide (FP), internal fusion peptide (IFP), and pretransmembrane domain (PTM). The HR regions are further flanked by the three membranotropic components. Both FP and IFP are located upstream of HR1, while PTM is distally downstream of HR2 and directly precedes the transmembrane domain of SARS-CoV S. All of these three components are able to partition into the phospholipid bilayer to disturb membrane integrity. []. During the pandemic, many conservative amino acid changes in FP segment of SARS-CoV-2 have been reported (i.e., L821I, L822F, K825R, V826L, T827I, L828P, A829T, D830G/A, A831V/S/T, G832C/S, F833S, I834T), although their impact is not known as the active conformation and mode of insertion of SARS-CoV-2 fusion peptide have not been experimentally characterised. Differences in HR1 sequences between SARS-CoV and SARS-CoV-2 suggest that SARS-CoV-2 HR2 makes stronger interactions with HR1. However, the substitutions observed in the solvent accessible surface of the HR1 domain (e.g., D936Y, S943P, S939F) of SARS-CoV-2 do not seem to be involved in stabilizing interactions with HR2. Substitutions in HR2 (e.g., K1073N, V1176F) or the TM or cytoplasmic tail domains have also been observed, but further experimental work is required to determine the effects of these changes [].This entry represents the heptad repeat 1 (HR1) from coronavirus Spike glycoprotein, S2 subunit. This region forms a long trimeric helical coiled-coil structure with peptides from the HR2 region packing in an oblique antiparallel manner on the grooves of the HR1 trimer in a mixed extended and helical conformation. Packing of the helical parts of HR2 on the HR1 trimer grooves and formation of a six-helical bundle plays an important role in the formation of a stable post-fusion structure. In contrast to their extended helical conformations in the post-fusion state, the HR1 motifs within S2 form several shorter helices in their pre-fusion state [, ]. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
The type I glycoprotein S of Coronavirus, trimers of which constitute the typical viral spikes, is assembled into virions through noncovalent interactions with the M protein. The spike glycoprotein is translated as a large polypeptide that is subsequently cleaved to S1 () and S2 []. The cleavage of S can occur at two distinct sites: S2 or S2' []. The spike is present in two very different forms: pre-fusion (the form on mature virions) and post-fusion (the form after membrane fusion has been completed). The spike is cleaved sequentially by host proteases at two sites: first at the S1/S2 boundary (i.e. S1/S2 site) and second within S2 (i.e. S2' site). After the cleavages, S1 dissociates from S2, allowing S2 to transition to the post-fusion structure []. Both chimeric S proteins appeared to cause cell fusion when expressed individually, suggesting that they were biologically fully active []. The spike is a type I membrane glycoprotein that possesses a conserved transmembrane anchor and an unusual cysteine-rich (cys) domain that bridges the putative junction of the anchor and the cytoplasmic tail [].SARS-CoV S is largely uncleaved after biosynthesis. It can be later processed by endosomal cathepsin L, trypsin, thermolysin, and elastase, which are shown to induce syncytia formation and virus entry. Other proteases that are of potential biological relevance in potentiating SARS-CoV S include TMPRSS2, TMPRSS11a, and HAT which are localized on the cell surface and are highly expressed in the human airway []. The furin-like S2' cleavage site at KR/SF with P1 and P2 basic residues and a P2' hydrophobic Phe downstream of the IFP is identical between the SARS-CoV-2 and SARS-CoV. One or more furin-like enzymes would cleave the S2' site at KR/SF [, ]. Deletion of SARS-CoV-2 furin cleavage site suggests that it may not be required for viral entry but may affect replication kinetics and altered sites have been still seen proteolytically cleaved. Several substitutions within the S2' cleavage domain of SARS-COV-2 have been reported, including P812L/S/T, S813I/G, F817L, I818S/V, but further experimental study of their consequences and the replication properties of the altered viruses are required to understand the role of furin cleavage in SARS-CoV-2 infection and virulence []. The S2 subunit normally contains multiple key components, including one or more fusion peptides (FP), a second proteolytic site (S2') and two conserved heptad repeats (HRs), driving membrane penetration and virus-cell fusion. The HRs can trimerize into a coiled-coil structure built of three HR1-HR2 helical hairpins presenting as a canonical six-helix bundle and drag the virus envelope and the host cell bilayer into close proximity, preparing for fusion to occur []. The fusion core is composed of HR1 and HR2 and at least three membranotropic regions that are denoted as the fusion peptide (FP), internal fusion peptide (IFP), and pretransmembrane domain (PTM). The HR regions are further flanked by the three membranotropic components. Both FP and IFP are located upstream of HR1, while PTM is distally downstream of HR2 and directly precedes the transmembrane domain of SARS-CoV S. All of these three components are able to partition into the phospholipid bilayer to disturb membrane integrity. []. During the pandemic, many conservative amino acid changes in FP segment of SARS-CoV-2 have been reported (i.e., L821I, L822F, K825R, V826L, T827I, L828P, A829T, D830G/A, A831V/S/T, G832C/S, F833S, I834T), although their impact is not known as the active conformation and mode of insertion of SARS-CoV-2 fusion peptide have not been experimentally characterised. Differences in HR1 sequences between SARS-CoV and SARS-CoV-2 suggest that SARS-CoV-2 HR2 makes stronger interactions with HR1. However, the substitutions observed in the solvent accessible surface of the HR1 domain (e.g., D936Y, S943P, S939F) of SARS-CoV-2 do not seem to be involved in stabilizing interactions with HR2. Substitutions in HR2 (e.g., K1073N, V1176F) or the TM orcytoplasmic tail domains have also been observed, but further experimental work is required to determine the effects of these changes [].This entry represents the heptad repeat 2 (HR2) from coronavirus Spike glycoprotein, S2 subunit. It adopts a mixed conformation: the central part fold into a nine-turn α-helix, while the residues on either side of the helix adopt an extended conformation. Packing of the helical parts of HR2 on the HR1 trimer grooves and formation of a six-helical bundle plays an important role in the formation of a stable post-fusion structure [, ]. |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Sarojini S |
| Year: |
2011 |
| Journal: |
DNA Cell Biol |
| Title: |
Interferon-induced tetherin restricts vesicular stomatitis virus release in neurons. |
| Volume: |
30 |
| Issue: |
12 |
| Pages: |
965-74 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mariathasan S |
| Year: |
2004 |
| Journal: |
Nature |
| Title: |
Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. |
| Volume: |
430 |
| Issue: |
6996 |
| Pages: |
213-8 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Srivastava D |
| Year: |
2012 |
| Journal: |
J Mol Biol |
| Title: |
The three-dimensional structural basis of type II hyperprolinemia. |
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