| Type |
Details |
Score |
| Publication |
| First Author: |
Clark CS |
| Year: |
1984 |
| Journal: |
J Occup Med |
| Title: |
Enteric parasites in workers occupationally exposed to sewage. |
| Volume: |
26 |
| Issue: |
4 |
| Pages: |
273-5 |
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| Publication |
| First Author: |
Suzuki T |
| Year: |
2009 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
PKC eta regulates occludin phosphorylation and epithelial tight junction integrity. |
| Volume: |
106 |
| Issue: |
1 |
| Pages: |
61-6 |
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| Publication |
| First Author: |
Naito Y |
| Year: |
2006 |
| Journal: |
J Biochem |
| Title: |
Phospholipase C isoforms are localized at the cleavage furrow during cytokinesis. |
| Volume: |
140 |
| Issue: |
6 |
| Pages: |
785-91 |
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| Publication |
| First Author: |
Mittelstaedt T |
| Year: |
2010 |
| Journal: |
Biol Chem |
| Title: |
RIM proteins and their role in synapse function. |
| Volume: |
391 |
| Issue: |
6 |
| Pages: |
599-606 |
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•
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| Publication |
| First Author: |
Han Y |
| Year: |
2011 |
| Journal: |
Neuron |
| Title: |
RIM determines Ca²+ channel density and vesicle docking at the presynaptic active zone. |
| Volume: |
69 |
| Issue: |
2 |
| Pages: |
304-16 |
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| Publication |
| First Author: |
Schoch S |
| Year: |
2006 |
| Journal: |
EMBO J |
| Title: |
Redundant functions of RIM1alpha and RIM2alpha in Ca(2+)-triggered neurotransmitter release. |
| Volume: |
25 |
| Issue: |
24 |
| Pages: |
5852-63 |
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| Publication |
| First Author: |
Roepman R |
| Year: |
2005 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Interaction of nephrocystin-4 and RPGRIP1 is disrupted by nephronophthisis or Leber congenital amaurosis-associated mutations. |
| Volume: |
102 |
| Issue: |
51 |
| Pages: |
18520-5 |
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| Publication |
| First Author: |
Schauder CM |
| Year: |
2014 |
| Journal: |
Nature |
| Title: |
Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer. |
| Volume: |
510 |
| Issue: |
7506 |
| Pages: |
552-5 |
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•
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| Publication |
| First Author: |
Martiny-Baron G |
| Year: |
2007 |
| Journal: |
Pharmacol Res |
| Title: |
Classical PKC isoforms in cancer. |
| Volume: |
55 |
| Issue: |
6 |
| Pages: |
477-86 |
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•
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| Publication |
| First Author: |
Keranen LM |
| Year: |
1995 |
| Journal: |
Curr Biol |
| Title: |
Protein kinase C is regulated in vivo by three functionally distinct phosphorylations. |
| Volume: |
5 |
| Issue: |
12 |
| Pages: |
1394-1403 |
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| Publication |
| First Author: |
Newton AC |
| Year: |
2010 |
| Journal: |
Am J Physiol Endocrinol Metab |
| Title: |
Protein kinase C: poised to signal. |
| Volume: |
298 |
| Issue: |
3 |
| Pages: |
E395-402 |
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| Protein Domain |
| Type: |
Family |
| Description: |
This entry represents phosphoinositol-specific phospholipase C (PLC) from eukaryotes. Proteins in this entry include PLC-beta, gamma, delta, epsilon, eta, zeta and inactive phospholipase C-like protein 2 (PLC-L2). Phosphoinositol-specific phospholipase C (PLC; () plays an important role in signal transduction processes [], mediating the cellular actions of a variety of hormones, neurotransmitters and growth factors. Upon agonist-dependent activation, PLC catalyses the hydrolysis of membrane phosphatidylinositol 4,5-bisphosphate (PIP2), generating the second messengers inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG). IP3 binds specific intracellular receptors to trigger Ca2+mobilisation, while DAG mediates activation of a family of protein kinase C isozymes. This catalytic process is tightly regulated by reversible phosphorylation and binding of regulatory proteins [, , ]. Based on molecular size, immunoreactivity and amino acid sequence, several subtypes have been classified. Overall, sequence identity between sub-types is low, yet all isoforms share a split TIM barrel containing two conserved domains, designated X and Y []. The core eukaryotic PLC enzyme is composed of a pleckstrin homology (PH) domain, four tandem EF hand domains, a split TIM barrel, and a C2 domain []. The presence of an insert in the TIM barrel led to the naming of the N- and C-terminal halves of the TIM barrel as 'X-box' and 'Y-box'. The order of these two regions is always the same (NH2-X-Y-COOH), but the spacing is variable. In most isoforms, the distance between these two regions is only 50-100 residues, for example, in PLC-beta subtypes, X and Y domains are separated by a stretch of 70-120 amino acids rich in Ser, Thr and acidic residues (their C terminus is rich in basic residues). However, in PLC-gammas, there is an insert of more than 400 residues containing a PH domain, two SH2 domains, and one SH3 domain. The two conserved X and Y domains have been shown to be important for the catalytic activity. C-terminal to the Y-box, there is a C2 domain, possibly involved in Ca-dependent membrane attachment. |
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| Protein Domain |
| Type: |
Family |
| Description: |
These proteins belong to MEROPS peptidase family S1 (chymotrypsin family, clan PA(S)), subfamily S1A.This family contains two mammalian proteins, complement C2 and complement factor B, which, respectively, have analogous roles in the classical and alternative pathways of complement activation. These proteins are composed of three regions, an N-terminal three-module complement control protein domain, a von Willebrand factor A domain, and a C-terminal serine protease domain. Briefly, they are activated by cleavage and function as the serine protease components of the C3/C5 convertases, which play similar roles in these pathways although composed of different proteins. Homologs in non-mammalian species are often more or less equally related to mammalian C2 and B and may be designated as complement B/C2. Strongylocentrotus purpuratus (Purple sea urchin) has an atypical factor B with a five-module complement control protein domain.The structures of the von Willebrand factor A and serine protease domains from human complement factor B () have been analysed [, ]. The A domain forms the classical vWF A domain fold, which consists of a central β-sheet flanked on both sides by amphipathic alpha helices. It contains an integrin-like MIDAS (metal ion-dependent adhesion site) motif that adopts the open conformation typical of integrin-ligand complexes, with an acidic residue from another A domain (provided by a fortuitous crystal contact) completing the coordination of the metal ion. Although a closed conformation was not observed, modelling studies suggest that the A domain could adopt this conformation, implying that as with integrins, ligand-binding may induce conformational changes which transduce a signal to other domains in the protein []. The serine protease domain forms a chymotrypsin fold with several novel features []. Like other serine proteases it forms two β-sheets, composed of six β-strands each, surrounded by surface helices and loops. However, several novel deletions and insertions occur within these surface helices and loops, and differences in active site conformation also exist. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Metallothioneins (MT) are small proteins that bind heavy metals, such as zinc, copper, cadmium, nickel, etc. They have a high content of cysteine residues that bind the metal ions through clusters of thiolate bonds [, ]. An empirical classification into three classes has been proposed by Fowler and coworkers []and Kojima []. Members of class I are defined to include polypeptides related in the positions of their cysteines to equine MT-1B, and include mammalian MTs as well as from crustaceans and molluscs. Class II groups MTs from a variety of species, including sea urchins,fungi, insects and cyanobacteria. Class III MTs are atypical polypeptides composed of gamma-glutamylcysteinyl units [].This original classification system has been found to be limited, in the sense that it does not allow clear differentiation of patterns of structural similarities, either between or within classes. Subsequently, a new classification was proposed on the basis of sequence similarity derived from phylogenetic relationships, which basically proposes an MT family for each main taxonomic group of organisms []. Crustacean MTs belong to family 3. They are small proteins, with 18 totally conserved cysteines. The members of this family are recognised by the sequence pattern P-[GD]-P-C-C-x(3,4)-C-x-C located at the Nterm. The taxonomic range of the members extends to crustaceans. Known characteristics of this family are: 58 to 60 AAs; variants exist with and without the N-terminal Met. Protein sequence is divided into two structural domains, containing each 9 Cys binding 3 bivalent metal ions. Family 3 includes subfamilies: c1, c2, c. All sequences are very similar. c1 and c2 are forming two distinct monophyletic groups in the AA phylogenetic tree. c are crustacean MTs different from c1 and c2 based on phylogenetic analyses. |
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•
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| Protein Domain |
| Type: |
Family |
| Description: |
Cytochromes c (cytC) can be defined as electron-transfer proteins having one or several haem c groups, bound to the protein by one or, more generally, two thioether bonds involving sulfhydryl groups of cysteine residues. The fifth haem iron ligand is always provided by a histidine residue. CytC possess a wide range of properties and function in a large number of different redox processes.Ambler []recognised four classes of cytC. Class I includes the low-spin soluble cytC of mitochondria and bacteria, with the haem-attachment site towards the N terminus, and the sixth ligand provided by a methionine residue about 40 residues further on towards the C terminus []. On the basis of sequence similarity, class I cytC were further subdivided into five classes, IA to IE. Class IB includes the eukaryotic mitochondrial cyt C and prokaryotic 'short' cyt C2 exemplified by Rhodopila globiformis cyt C2; Class IA includes 'long' cyt C2, such as Rhodospirillum rubrum cyt C2 and Aquaspirillum itersonii cyt C-550, which have several extra loops by comparison with Class IB cyt C.Class I cytC has a characterised fold which comprises 5 α-helices arranged in a unique tertiary structure and a conserved N-terminal sequence -Cys-Xxx-Xxx-Cys-His- where the cysteines mediate the covalent cross-linking of the heme to the protein and the His [].The 3D structures of a considerable number of class IA and IB cytC have been determined. The proteins consist of 3-6 α-helices; the three most conserved 'core' helices form a 'basket' around the haem group, with one haem edge exposed to the solvent. Most class I cytC have conserved aromatic residues clustered around the haem and axial ligands. |
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•
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| Protein Domain |
| Type: |
Domain |
| Description: |
Rho guanosine triphosphatases (GTPases) are critical regulators of cell motility, polarity, adhesion, cytoskeletal organisation, proliferation, geneexpression, and apoptosis. Conversion of these biomolecular switches to the activated GTP-bound state is controlled by two families of guanine nucleotide exchanges factors (GEFs). DH-PH proteins are a large group of Rho GEFs comprising a catalytic Dbl homology (DH) domain with anadjacent pleckstrin homology (PH) domain within the context of functionally diverse signalling modules. The evolutionarily distinct and smaller family of DOCK (dedicator of cytokinesis) or CDM (CED-5, DOCK1180, Myoblast city) proteins activate either Rac or Cdc42 to control cell migration, morphogenesis, and phagocytosis. DOCK proteins share the DOCK-type C2 domain (also termed the DOCK-homology region (DHR)-1 or CDM-zizimin homology 1 (CZH1) domain and the DOCKER domain (also termed the DHR-2 or CZH2 domain) [, , , , , , ].The DOCK-type C2 domain is located toward the N terminus []. The DOCKER domain is a GEF catalytic domain of ~400 residues situated within the C terminus. The structure of the DOCKER domain differs from that of other GEF catalytic domains. It is organised into three lobes of roughly equal size (lobes A, B, and C), with the Rho-family binding site and catalytic centre generated entirely from lobes B and C. Lobe A is formed from an antiparallel array of alpha helices. Through extensive contacts with lobe B, lobe A stabilises the DHR2 domain. Lobe B adopts an unusual architecture of two antiparallel beta sheets disposed in a loosely packed orthogonal arrangement, whereas lobe C comprises a four-helix bundle [, ].This entry represents the DOCKER domain. |
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•
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| Protein Domain |
| Type: |
Family |
| Description: |
Synaptotagmin-like protein 2 (SYTL2) belongs to the synaptotagmin-like protein family, which contains a N-terminal RabBD (Rab-binding) domain and two C-terminal C2 domains. RabBD domain mediates interaction with RAB27A and recruitment on to vesicular structures in cytotoxic T-lymphocytes (CTL) [, ]. The C2 domain mediates binding to phosphatidylserine (PS) and phosphatidylinositol 4,5-bisphosphate (PIP2) and localisation to the cell membrane [, ]. SYTL2 has several isoforms produced by alternative splicing, and different isoforms may have different functions.In humans, SYTL2 isoform 1 acts as a RAB27A effector protein and plays a role in cytotoxic granule exocytosis in lymphocytes. It is required for cytotoxic granule docking at the immunologic synapse. Isoform 4 binds phosphatidylserine (PS) and phosphatidylinositol-4,5-bisphosphate (PIP2) and promotes the recruitment of glucagon-containing granules to the cell membrane in pancreatic alpha cells. Its binding to PS is inhibited by Ca2+ while binding to PIP2 is Ca2+ insensitive [, , ]. In mice, SYTL2 isoform 1 may play a role in melanosome transport and vesicle trafficking. It controls melanosome distribution in the cell periphery and regulates melanocyte morphology [, ]. Isoform 1 also acts as a positive mediator of mucus secretion by the surface mucus cells of the stomach. It mediates basal mucus secretion by gastric surface cells by promoting the proper granule biognesis and docking of mucus granules with the apical plasma membrane []. Isoform 11 acts as a RAB27A effector protein and plays a role in cytotoxic granule exocytosis in lymphocytes. It is required for cytotoxic granule docking at the immunologic synapse. Isoform 1 may play a role in melanosome transport and vesicle trafficking. It controls melanosome distribution in the cell periphery and regulates melanocyte morphology. |
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| Publication |
| First Author: |
Keller C |
| Year: |
2004 |
| Journal: |
Genes Dev |
| Title: |
Pax3:Fkhr interferes with embryonic Pax3 and Pax7 function: implications for alveolar rhabdomyosarcoma cell of origin. |
| Volume: |
18 |
| Issue: |
21 |
| Pages: |
2608-13 |
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•
•
•
•
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| Publication |
| First Author: |
de Sousa e Melo F |
| Year: |
2017 |
| Journal: |
Nature |
| Title: |
A distinct role for Lgr5+ stem cells in primary and metastatic colon cancer. |
| Volume: |
543 |
| Issue: |
7647 |
| Pages: |
676-680 |
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•
•
•
•
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| Publication |
| First Author: |
Burzyn D |
| Year: |
2013 |
| Journal: |
Cell |
| Title: |
A special population of regulatory T cells potentiates muscle repair. |
| Volume: |
155 |
| Issue: |
6 |
| Pages: |
1282-95 |
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•
•
•
•
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| Publication |
| First Author: |
Flanigan TJ |
| Year: |
2014 |
| Journal: |
Genes Brain Behav |
| Title: |
Abnormal vibrissa-related behavior and loss of barrel field inhibitory neurons in 5xFAD transgenics. |
| Volume: |
13 |
| Issue: |
5 |
| Pages: |
488-500 |
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•
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| Publication |
| First Author: |
Dumortier A |
| Year: |
2010 |
| Journal: |
PLoS One |
| Title: |
Atopic dermatitis-like disease and associated lethal myeloproliferative disorder arise from loss of Notch signaling in the murine skin. |
| Volume: |
5 |
| Issue: |
2 |
| Pages: |
e9258 |
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•
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| Publication |
| First Author: |
Krebs P |
| Year: |
2011 |
| Journal: |
Blood |
| Title: |
Disruption of MyD88 signaling suppresses hemophagocytic lymphohistiocytosis in mice. |
| Volume: |
117 |
| Issue: |
24 |
| Pages: |
6582-8 |
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•
•
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| Publication |
| First Author: |
Li G |
| Year: |
2013 |
| Journal: |
Stem Cells |
| Title: |
IL-4 receptor blockade abrogates satellite cell: rhabdomyosarcoma fusion and prevents tumor establishment. |
| Volume: |
31 |
| Issue: |
11 |
| Pages: |
2304-12 |
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•
•
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| Publication |
| First Author: |
Nakhai H |
| Year: |
2008 |
| Journal: |
Development |
| Title: |
Conditional ablation of Notch signaling in pancreatic development. |
| Volume: |
135 |
| Issue: |
16 |
| Pages: |
2757-65 |
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•
•
•
•
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| Publication |
| First Author: |
Kunze B |
| Year: |
2020 |
| Journal: |
Gastroenterology |
| Title: |
Notch Signaling Mediates Differentiation in Barrett's Esophagus and Promotes Progression to Adenocarcinoma. |
| Volume: |
159 |
| Issue: |
2 |
| Pages: |
575-590 |
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•
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| Publication |
| First Author: |
Tian H |
| Year: |
2011 |
| Journal: |
Nature |
| Title: |
A reserve stem cell population in small intestine renders Lgr5-positive cells dispensable. |
| Volume: |
478 |
| Issue: |
7368 |
| Pages: |
255-9 |
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•
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| First Author: |
Yang A |
| Year: |
2018 |
| Journal: |
Cancer Discov |
| Title: |
Autophagy Sustains Pancreatic Cancer Growth through Both Cell-Autonomous and Nonautonomous Mechanisms. |
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| Publication |
| First Author: |
Rubin BP |
| Year: |
2011 |
| Journal: |
Cancer Cell |
| Title: |
Evidence for an unanticipated relationship between undifferentiated pleomorphic sarcoma and embryonal rhabdomyosarcoma. |
| Volume: |
19 |
| Issue: |
2 |
| Pages: |
177-91 |
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| Publication |
| First Author: |
Schouwey K |
| Year: |
2011 |
| Journal: |
Oncogene |
| Title: |
RBP-Jκ-dependent Notch signaling enhances retinal pigment epithelial cell proliferation in transgenic mice. |
| Volume: |
30 |
| Issue: |
3 |
| Pages: |
313-22 |
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•
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| First Author: |
Mazur PK |
| Year: |
2010 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Notch2 is required for progression of pancreatic intraepithelial neoplasia and development of pancreatic ductal adenocarcinoma. |
| Volume: |
107 |
| Issue: |
30 |
| Pages: |
13438-43 |
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Lau LS |
| Year: |
2014 |
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PLoS Pathog |
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CD8+ T cells from a novel T cell receptor transgenic mouse induce liver-stage immunity that can be boosted by blood-stage infection in rodent malaria. |
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10 |
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5 |
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| First Author: |
Xiang B |
| Year: |
2021 |
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Arterioscler Thromb Vasc Biol |
| Title: |
Calcium Ion Chelation Preserves Platelet Function During Cold Storage. |
| Volume: |
41 |
| Issue: |
1 |
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Levine AG |
| Year: |
2014 |
| Journal: |
Nat Immunol |
| Title: |
Continuous requirement for the TCR in regulatory T cell function. |
| Volume: |
15 |
| Issue: |
11 |
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Fernandez Vallone V |
| Year: |
2016 |
| Journal: |
Development |
| Title: |
Trop2 marks transient gastric fetal epithelium and adult regenerating cells after epithelial damage. |
| Volume: |
143 |
| Issue: |
9 |
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Vogl C |
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J Cell Sci |
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Unconventional molecular regulation of synaptic vesicle replenishment in cochlear inner hair cells. |
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Huang S |
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2018 |
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PLoS Biol |
| Title: |
Jagged1/Notch2 controls kidney fibrosis via Tfam-mediated metabolic reprogramming. |
| Volume: |
16 |
| Issue: |
9 |
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Jadhav U |
| Year: |
2017 |
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Cell Stem Cell |
| Title: |
Dynamic Reorganization of Chromatin Accessibility Signatures during Dedifferentiation of Secretory Precursors into Lgr5+ Intestinal Stem Cells. |
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21 |
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Nature |
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J Neurosci |
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Doc2 Proteins Are Not Required for the Increased Spontaneous Release Rate in Synaptotagmin-1-Deficient Neurons. |
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Neuron |
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Excitatory and Inhibitory Neurons Utilize Different Ca2+ Sensors and Sources to Regulate Spontaneous Release. |
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Guiberson NGL |
| Year: |
2024 |
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Brain |
| Title: |
Disease-linked mutations in Munc18-1 deplete synaptic Doc2. |
| Volume: |
147 |
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6 |
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2185-2202 |
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Exp Cell Res |
| Title: |
Signaling by distinct classes of phosphoinositide 3-kinases. |
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Chem Biol |
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Ready, set, go! How protein kinase C manages dynamic signaling. |
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4 |
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Buonanno A |
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1986 |
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J Biol Chem |
| Title: |
A universal oligonucleotide probe for acetylcholine receptor genes. Selection and sequencing of cDNA clones for the mouse muscle beta subunit. |
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35 |
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16451-8 |
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James PL |
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| Journal: |
J Biol Chem |
| Title: |
A highly conserved insulin-like growth factor-binding protein (IGFBP-5) is expressed during myoblast differentiation. |
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Biol Reprod |
| Title: |
Molecular cloning and characterization of P47, a novel boar sperm-associated zona pellucida-binding protein homologous to a family of mammalian secretory proteins. |
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Williamson DJ |
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| Journal: |
Mol Cell Biol |
| Title: |
hnRNP C is required for postimplantation mouse development but Is dispensable for cell viability. |
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•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
461
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
461
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
502
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
402
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
461
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
564
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
149
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
149
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
527
 |
| Fragment?: |
false |
|
•
•
•
•
•
|