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Autophagy, ISSN 1554-8627, 05/2015, Volume 11, Issue 5, pp. 812 - 832
By monitoring the fragmentation of a GST-BHMT (a protein fusion of glutathionine S-transferase N-terminal to betaine-homocysteine S-methyltransferase) reporter... 
GST-BHMT, a fusion protein of glutathionine S-transferase N-terminal to betaine-homocysteine S-methyltransferase | ATF4, activating transcription factor 4 | MTORC1, MTOR complex 1 | LSCS, linker-specific cleavage site | selective macroautophagy | RPS6KB1, ribosomal protein S6 kinase, 70kDa, polypeptide 1 | UPR, unfolded protein response | ATG7, autophagy-related 7 | ULK1, unc-51 like autophagy activating kinase 1 | TSC1/2, tuberous sclerosis 1/2 | BCL2, B-cell CLL/lymphoma 2 | XBP1, X-box binding protein 1 | ACACA/B, acetyl-CoA carboxylase α/β | BECN1, Beclin 1, autophagy-related | MTOR, mechanistic target of rapamycin (serine/threonine kinase) | 1 | SQSTM1, sequestosome 1 | HA, hemagglutinin | BHMT, betaine-homocysteine S-methyltransferase | GST-BHMT | DDIT3, DNA-damage-inducible transcript 3 | ATF6, activating transcription factor 6 | EBSS, Earle's Balanced Salt Solution | Cvt, cytoplasm-to-vacuole-targeting | RM, rich medium | proteasome inhibition | GST, glutathionine S-transferase | FRAG | MAP1LC3, microtubule-associated protein 1 light chain 3 | PRKAA, protein kinase, AMP-activated, α catalytic subunit | an autophagy-mediated cleavage product of the GST-BHMT reporter | NBR1, neighbor of BRCA1 gene 1 | ERN1, endoplasmic reticulum to nucleus signaling 1 | P4HB, prolyl 4-hydroxylase, β polypeptide | MAP2K7, mitogen-activated protein kinase kinase 7 | Baf A1, bafilomycin A | UPS, ubiquitin proteasome system | PRKAA/AMPK | EIF4EBP1, eukaryotic translation initiation factor 4E binding protein 1 | ACTB, actin, β | HSPA5, heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa) | MTOR | BHMT | EIF2AK3, eukaryotic translation initiation factor 2-α, kinase 3 | RHEB, Ras homolog enriched in brain | MAPK8, mitogen-activated protein kinase 8 | cargo receptors SQSTM1/p62 and NBR1 | ER, endoplasmic reticulum | CTNNB1, catenin (cadherin-associated protein), β 1, 88kDa | SIGNALING PATHWAYS | ER STRESS | KINASE | ENDOPLASMIC-RETICULUM STRESS | SELECTIVE AUTOPHAGY | CELL BIOLOGY | UNFOLDED PROTEIN RESPONSE | MONITORING AUTOPHAGY | FUSION PROTEIN | BETAINE HOMOCYSTEINE METHYLTRANSFERASE | MAINTAINS ENERGY | AMP-Activated Protein Kinases - metabolism | TOR Serine-Threonine Kinases - metabolism | Sequestosome-1 Protein | Humans | Recombinant Fusion Proteins - metabolism | Autophagy - drug effects | Lysosomes - metabolism | Ubiquitination - drug effects | Protein Processing, Post-Translational - drug effects | Protein Binding - drug effects | HEK293 Cells | Membrane Proteins - metabolism | Betaine-Homocysteine S-Methyltransferase - metabolism | Protein-Serine-Threonine Kinases - metabolism | Beclin-1 | Lysosomes - drug effects | Protein Structure, Tertiary | Endoplasmic Reticulum Stress - drug effects | Endoribonucleases - metabolism | Proteasome Inhibitors - pharmacology | Mitogen-Activated Protein Kinase 8 - metabolism | Glutathione Transferase - metabolism | Apoptosis Regulatory Proteins - metabolism | Leupeptins - pharmacology | Proteins - metabolism | Signal Transduction - drug effects | HeLa Cells | Proteasome Endopeptidase Complex - metabolism | Adaptor Proteins, Signal Transducing - metabolism | Protein Multimerization - drug effects
Journal Article
Cell, ISSN 0092-8674, 2006, Volume 126, Issue 2, pp. 269 - 283
The PML tumor suppressor controls key pathways for growth suppression, induction of apoptosis, and cellular senescence. PML loss occurs frequently in human... 
APOPTOSIS | ACTIVATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROTEIN-KINASE CK2 | DNA-DAMAGE | GROWTH | SENESCENCE | NUCLEAR-BODY FORMATION | EXPRESSION | CARCINOMA | P53 | CELL BIOLOGY | NIH 3T3 Cells | Protein Subunits | Transcription Factors - chemistry | Humans | Transcriptional Activation | Ubiquitin - metabolism | Neoplasm Proteins - antagonists & inhibitors | Casein Kinase II - genetics | Tumor Suppressor Proteins - chemistry | p38 Mitogen-Activated Protein Kinases - metabolism | Neoplasm Proteins - genetics | Genes, Tumor Suppressor | Amino Acid Sequence | Tumor Suppressor Proteins - metabolism | Lung Neoplasms - enzymology | Enzyme Inhibitors - pharmacology | Mice, Transgenic | Neoplasm Proteins - chemistry | Nuclear Proteins - chemistry | Serine - metabolism | Leupeptins - pharmacology | Tumor Suppressor Proteins - physiology | Cell Line, Tumor | Mice | Carcinoma, Non-Small-Cell Lung - enzymology | Enzyme Activation | Proteasome Endopeptidase Complex - metabolism | Sequence Deletion | Phosphorylation | Tumor Suppressor Proteins - antagonists & inhibitors | Neoplasm Proteins - physiology | Molecular Sequence Data | Lung Neoplasms - pathology | Neoplasm Proteins - metabolism | Tumor Suppressor Proteins - genetics | Nuclear Proteins - genetics | Carcinoma, Non-Small-Cell Lung - pathology | Lung Neoplasms - genetics | Protein Structure, Tertiary | Cell Line | Green Fluorescent Proteins - metabolism | Transcription Factors - physiology | Carcinoma, Non-Small-Cell Lung - genetics | RNA, Small Interfering - pharmacology | Casein Kinase II - antagonists & inhibitors | Nuclear Proteins - metabolism | Transcription Factors - antagonists & inhibitors | Transcription Factors - genetics | Serine - chemistry | Transcription Factors - metabolism | Triazoles - pharmacology | Animals | Hemagglutinins - chemistry | Nuclear Proteins - antagonists & inhibitors | Nuclear Proteins - physiology | Casein Kinase II - metabolism | Cell Line, Transformed | Promyelocytic Leukemia Protein | Sorbitol - pharmacology | Amino Acid Substitution | Apoptosis | Genetic research | Tumor suppressor genes | Research | Protein kinases | Oncogenes | Prevention | Casein | Health aspects | Analysis | Lung cancer | Cancer
Journal Article
JOURNAL OF BIOLOGICAL CHEMISTRY, ISSN 0021-9258, 08/2017, Volume 292, Issue 32, pp. 13258 - 13270
The beta-secretase (BACE1) initiates processing of the amyloid precursor protein (APP) into A beta peptides, which have been implicated as central players in... 
BACE1 | CLEAVING ENZYME | DOMAIN | WILSON-DISEASE | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | SEQUENCE | AMYLOID-PRECURSOR-PROTEIN | MICE | MODEL | INFLUENZA-VIRUS HEMAGGLUTININ | Amyloid Precursor Protein Secretases - genetics | Humans | Protein Multimerization | Bacterial Proteins - chemistry | Alanine - chemistry | Green Fluorescent Proteins - genetics | Aspartic Acid Endopeptidases - genetics | Recombinant Fusion Proteins - metabolism | Biological Transport | RNA Interference | Copper - metabolism | HEK293 Cells | Fluorescence Resonance Energy Transfer | Luminescent Proteins - chemistry | Protein Interaction Domains and Motifs | Green Fluorescent Proteins - chemistry | Aspartic Acid Endopeptidases - chemistry | Green Fluorescent Proteins - metabolism | Mutagenesis, Site-Directed | Aspartic Acid Endopeptidases - antagonists & inhibitors | Bacterial Proteins - genetics | Models, Molecular | Cysteine - chemistry | Recombinant Fusion Proteins - chemistry | Amyloid Precursor Protein Secretases - chemistry | Protein Folding | Point Mutation | Amyloid Precursor Protein Secretases - metabolism | Aspartic Acid Endopeptidases - metabolism | Bacterial Proteins - metabolism | Cytosol - metabolism | Luminescent Proteins - genetics | Protein Conformation | Amyloid Precursor Protein Secretases - antagonists & inhibitors | Microscopy, Fluorescence | Amino Acid Substitution | Luminescent Proteins - metabolism | single-molecule biophysics | stoichiometry | protein cross-linking | beta-secretase 1 (BACE1) | copper transport | Cell Biology
Journal Article
Journal Article
PLoS Pathogens, ISSN 1553-7366, 05/2015, Volume 11, Issue 5, p. e1004896
Clostridium perfringens epsilon-toxin (ETX) is a potent pore-forming toxin responsible for a central nervous system (CNS) disease in ruminant animals with... 
NERVOUS-SYSTEM | MDCK CELLS | MICROBIOLOGY | PLASMA-MEMBRANE | INTESTINAL INFECTIONS | DARBY CANINE KIDNEY | VIROLOGY | PORE-FORMING TOXIN | APICAL SORTING MACHINERY | RAFT-ASSOCIATED PROTEIN | HUMAN T-LYMPHOCYTES | PARASITOLOGY | INFLUENZA-VIRUS HEMAGGLUTININ | Injections, Intravenous | Cricetulus | Myelin and Lymphocyte-Associated Proteolipid Proteins - metabolism | Humans | Bacterial Toxins - toxicity | Recombinant Fusion Proteins - metabolism | Tissue Distribution | Protein Precursors - toxicity | Bacterial Toxins - genetics | Clostridium perfringens - metabolism | Protein Interaction Domains and Motifs | Cell Death - drug effects | Binding Sites | Clostridium perfringens - pathogenicity | Recombinant Fusion Proteins - administration & dosage | CHO Cells | Recombinant Proteins - metabolism | Protein Precursors - genetics | Protein Precursors - administration & dosage | Mice, Inbred C57BL | Rats | Recombinant Proteins - chemistry | Recombinant Fusion Proteins - toxicity | Recombinant Fusion Proteins - chemistry | Recombinant Proteins - administration & dosage | Mice, Knockout | Protein Precursors - metabolism | Toxicokinetics | Bacterial Toxins - metabolism | Animals | Myelin and Lymphocyte-Associated Proteolipid Proteins - chemistry | Recombinant Proteins - toxicity | Ligands | Mutagenesis, Insertional | Myelin and Lymphocyte-Associated Proteolipid Proteins - genetics
Journal Article
BBA - Molecular Cell Research, ISSN 0167-4889, 10/2011, Volume 1813, Issue 10, pp. 1906 - 1916
The first and third extracellular loops (ECL) of G protein-coupled receptors (GPCRs) have been implicated in ligand binding and receptor function. This study... 
G protein-coupled receptor | Extracellular loop | Receptor activation | Juxtamembrane domain | Receptor activity-modifying protein | CGRP | AMINO-TERMINUS | ACTIVATION | COMPLEX | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROTEIN-COUPLED RECEPTORS | AGONIST BINDING | PEPTIDE | FAMILY | CELL BIOLOGY | SECRETIN RECEPTOR | B GPCRS | HORMONE-RECEPTOR | Calcitonin Receptor-Like Protein - physiology | Protein Interaction Domains and Motifs - physiology | Humans | Cercopithecus aethiops | Molecular Sequence Data | Receptor Activity-Modifying Protein 1 - chemistry | Calcitonin Gene-Related Peptide - chemistry | Calcitonin Gene-Related Peptide - physiology | Cattle | Protein Interaction Domains and Motifs - genetics | Protein Structure, Secondary - physiology | Cell Membrane - metabolism | Calcitonin Gene-Related Peptide - metabolism | Cyclic AMP - metabolism | Amino Acid Sequence | Mutagenesis, Site-Directed | Calcitonin Receptor-Like Protein - chemistry | Models, Molecular | Receptor Activity-Modifying Protein 1 - metabolism | Calcitonin Gene-Related Peptide - genetics | Mutant Proteins - metabolism | Mutant Proteins - physiology | Calcitonin Receptor-Like Protein - metabolism | Protein Structure, Secondary - genetics | Animals | Models, Biological | Calcitonin Receptor-Like Protein - genetics | Mutant Proteins - chemistry | Protein Binding | COS Cells | Amino Acid Substitution | Lectins | Vasoactive intestinal peptides | Parathyroid hormone | Membrane proteins
Journal Article