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regulated intramembrane proteolysis (424) 424
index medicus (276) 276
humans (250) 250
animals (235) 235
biochemistry & molecular biology (183) 183
cell biology (146) 146
proteolysis (125) 125
amyloid precursor protein (122) 122
gamma-secretase (99) 99
signal transduction (96) 96
membrane proteins - metabolism (92) 92
mice (86) 86
proteins (82) 82
alzheimer's disease (80) 80
neurosciences (74) 74
amino acid sequence (71) 71
molecular sequence data (70) 70
alzheimers-disease (69) 69
presenilin (68) 68
intracellular domain (64) 64
amyloid precursor protein secretases - metabolism (63) 63
proteases (63) 63
membrane proteins - genetics (60) 60
cleavage (58) 58
research (56) 56
intramembrane proteolysis (55) 55
article (51) 51
protein structure, tertiary (50) 50
cell line (49) 49
gene-expression (46) 46
physiological aspects (46) 46
microbiology (45) 45
mutation (45) 45
cell membrane - metabolism (43) 43
protein binding (40) 40
γ-secretase (40) 40
amyloid beta-protein precursor - metabolism (39) 39
substrate specificity (39) 39
cell nucleus - metabolism (37) 37
gene expression (37) 37
endopeptidases - metabolism (36) 36
models, biological (36) 36
biochemistry (34) 34
biophysics (34) 34
genetic aspects (34) 34
signal transduction - physiology (33) 33
cells, cultured (32) 32
escherichia-coli (32) 32
expression (32) 32
apoptosis (31) 31
bacterial proteins - metabolism (31) 31
biology (31) 31
protease (31) 31
signal peptide peptidase (31) 31
analysis (30) 30
research article (30) 30
activation (29) 29
cancer (29) 29
notch (29) 29
p75 neurotrophin receptor (29) 29
alzheimer disease - metabolism (28) 28
er stress (28) 28
membrane proteins (28) 28
peptides (28) 28
rats (28) 28
bacterial proteins - genetics (27) 27
endoplasmic reticulum (27) 27
kinases (27) 27
membrane proteins - chemistry (27) 27
multidisciplinary sciences (27) 27
protein (27) 27
transcription factors (27) 27
transcription factors - metabolism (27) 27
endoplasmic reticulum - metabolism (26) 26
nuclear translocation (26) 26
peptide hydrolases - metabolism (26) 26
amyloid beta-protein (25) 25
amyloid precursor protein secretases (25) 25
amyloid precursor protein secretases - genetics (25) 25
aspartic acid endopeptidases - metabolism (25) 25
endoplasmic-reticulum stress (25) 25
necrosis-factor-alpha (25) 25
phosphorylation (25) 25
regulated proteolysis (25) 25
gamma-secretase activity (24) 24
hek293 cells (24) 24
in-vivo (24) 24
ligands (24) 24
beta-secretase (23) 23
binding (23) 23
crystal-structure (23) 23
molecular biology (23) 23
nerve growth-factor (23) 23
site-2 protease (23) 23
transfection (23) 23
transmembrane domain (23) 23
binding sites (22) 22
endoplasmic-reticulum (22) 22
enzymes (22) 22
unfolded protein response (22) 22
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1. Full Text Intramembrane proteolysis at a glance: from signalling to protein degradation
by Kuhnle, N and Dederer, V and Lemberg, MK
JOURNAL OF CELL SCIENCE, ISSN 0021-9533, 08/2019, Volume 132, Issue 16, p. jcs217745
Over the last two decades, a group of unusual proteases, so-called intramembrane proteases, have become increasingly recognized for their unique ability to... 
DENDRITIC CELLS | Site-2 protease | gamma-secretase | SPPL2A | Presenilin | Protein homeostasis | CLEAVAGE | PEPTIDE PEPTIDASE | PARL | ZMPSTE24 | FAMILY | CELL BIOLOGY | THROMBOMODULIN | Regulated intramembrane proteolysis | B-CELL | MECHANISTIC INSIGHTS | Signal peptide peptidase | SPP-like protease | Limited proteolysis | RCE1 | Rhomboid
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2. Full Text Presenilin-dependent regulated intramembrane proteolysis and γ-secretase activity
by McCarthy, J.V and Twomey, C and Wujek, P
Cellular and Molecular Life Sciences, ISSN 1420-682X, 01/2009, Volume 66, Issue 9, pp. 1534 - 1555
Inhibiting the production of amyloid-beta by antagonising gamma-secretase activity is currently being pursued as a therapeutic strategy for Alzheimer's disease... 
Presenilin | Signal transduction | Regulated intramembrane proteolysis | Alzheimer's disease | γ-secretase complexes | P75 NEUROTROPHIN RECEPTOR | signal transduction | BIOCHEMISTRY & MOLECULAR BIOLOGY | AMYLOID-PRECURSOR-PROTEIN | BETA-PEPTIDE PRODUCTION | CELL BIOLOGY | C-TERMINAL FRAGMENT | GLYCOGEN-SYNTHASE KINASE-3-BETA | NONSTEROIDAL ANTIINFLAMMATORY DRUGS | APP INTRACELLULAR DOMAINS | gamma-secretase complexes | regulated intramembrane proteolysis | CLEAVING ENZYME BACE1 | CELL-CELL ADHESION | CALCIUM-BINDING PROTEIN | Presenilins - physiology | Amyloid Precursor Protein Secretases - genetics | Amyloid Precursor Protein Secretases - metabolism | Animals | Amyloid Precursor Protein Secretases - physiology | Models, Biological | Presenilins - metabolism | Substrate Specificity | Signal Transduction - physiology | Presenilins - chemistry
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3. Full Text Trafficking, a key player in regulated intramembrane proteolysis
by Sannerud, Ragna and Annaert, Wim
Seminars in Cell and Developmental Biology, ISSN 1084-9521, 2009, Volume 20, Issue 2, pp. 183 - 190
The term regulated intramembrane proteolysis (RIP) emerged from converging mechanisms aiming to release or activate signaling fragments or transcription... 
Presenilin | Regulated intramembrane proteolysis | Alzheimer's disease | γ-Secretase | Amyloid precursor protein | GAMMA-SECRETASE COMPLEX | P75 NEUROTROPHIN RECEPTOR | ALZHEIMERS-DISEASE | AMYLOID-PRECURSOR-PROTEIN | A-BETA PRODUCTION | DEVELOPMENTAL BIOLOGY | CELL BIOLOGY | gamma-Secretase | LIPID RAFTS | TRANS-GOLGI NETWORK | SORTILIN-RELATED RECEPTOR | GGA PROTEINS | C-TERMINAL FRAGMENTS | Amyloid Precursor Protein Secretases - metabolism | Signal Transduction | Humans | Amyloid beta-Protein Precursor - metabolism | Protein Transport | Peptides | Proteolysis | Proteases | Amyloid beta-protein
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4. Full Text EpCAM-Regulated Intramembrane Proteolysis Induces a Cancer Stem Cell-like Gene Signature in Hepatitis B Virus-infected Hepatocytes
by Mani, Saravana Kumar Kailasam and Zhang, Hao and Diab, Ahmed and Pascuzzi, Pete E and Lefrançois, Lydie and Fares, Nadim and Bancel, Brigitte and Merle, Philippe and Andrisani, Ourania
Journal of Hepatology, ISSN 0168-8278, 2016, Volume 65, Issue 5, pp. 888 - 898
Graphical abstract 
Gastroenterology and Hepatology | SUZ12/polycomb repressive complex 2 | Wnt signaling | BAMBI | Hepatocellular carcinoma | Hepatitis B virus | EpCAM-regulated intramembrane proteolysis | Pluripotency genes (NANOG, OCT4 and SOX2) | CD44 | CD133 | PLURIPOTENCY | SORAFENIB | TUMOR-INITIATING CELLS | HEPATOCELLULAR-CARCINOMA | TARGET GENES | REPLICATION | LIVER CARCINOGENESIS | X PROTEIN | STEM/PROGENITOR CELLS | GASTROENTEROLOGY & HEPATOLOGY | EXPRESSION | Animals | Hepatocytes | Proteolysis | Humans | Mice | Neoplastic Stem Cells | Carcinoma, Hepatocellular | Liver Neoplasms | Epithelial Cell Adhesion Molecule | Hepatitis B | Genetic aspects | Stem cells | Cancer | SUZ12 | polycomb repressive complex 2
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5. Full Text Regulated intramembrane proteolysis of amyloid precursor protein and regulation of expression of putative target genes
by Craessaerts, Katleen and Müller, Ulrike and De Strooper, Bart and Derks, Carmen and Filippov, Mikhail A and Hébert, Sébastien S and Serneels, Lutgarde and Tolia, Alexandra
EMBO reports, ISSN 1469-221X, 07/2006, Volume 7, Issue 7, pp. 739 - 745
γ‐Secretase‐dependent regulated intramembrane proteolysis of amyloid precursor protein (APP) releases the APP intracellular domain (AICD). The question of... 
secretase | regulated intramembrane proteolysis | amyloid precursor protein | Alzheimer's disease | Regulated intramembrane proteolysis | Amyloid precursor protein | Secretase | MECHANISM | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | COMPLEXES | BINDING DOMAIN | APP INTRACELLULAR DOMAIN | CELL BIOLOGY | SIGNAL-TRANSDUCTION | PRESENILINS | NEURONS | PROMOTER | GAMMA-SECRETASE | Protein Structure, Tertiary | Amyloid beta-Protein Precursor - deficiency | Cell Line | Endopeptidases - metabolism | Amyloid beta-Protein Precursor - chemistry | Humans | Gene Expression Regulation | Cercopithecus aethiops | Membranes - metabolism | Amyloid beta-Protein Precursor - genetics | Animals | Aspartic Acid Endopeptidases | Alzheimer Disease - metabolism | Amyloid Precursor Protein Secretases | Amyloid beta-Protein Precursor - metabolism | Mice | Protein Processing, Post-Translational | HeLa Cells | Alzheimer Disease - genetics | COS Cells | Peptide Hydrolases - metabolism | Proteins | Membranes | Gene expression | Proteomics | Scientific Report
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6. Full Text The Metastable XBP1u Transmembrane Domain Defines Determinants for Intramembrane Proteolysis by Signal Peptide Peptidase
by Yücel, Sara Suna and Stelzer, Walter and Lorenzoni, Alessandra and Wozny, Manfred and Langosch, Dieter and Lemberg, Marius K
Cell Reports, ISSN 2211-1247, 03/2019, Volume 26, Issue 11, pp. 3087 - 3099.e11
Unspliced mRNA encodes XBP1u, the transcriptionally inert variant of the unfolded protein response (UPR) transcription factor XBP1s. XBP1u targets its... 
ERAD | GxGD aspartic intramembrane protease | SPP | transmembrane helix dynamics | subsite | HO1 | regulated intramembrane proteolysis | XBP1u | exosite | SUBSTRATE-SPECIFICITY | UNFOLDED PROTEIN RESPONSE | MESSENGER-RNA | ER STRESS | CONFORMATIONAL FLEXIBILITY | ACTIVATOR PXBP1(S) | ENDOPLASMIC-RETICULUM | AMYLOID PRECURSOR PROTEIN | CLEAVAGE | GAMMA-SECRETASE | CELL BIOLOGY
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7. Full Text Making the cut: central roles of intramembrane proteolysis in pathogenic microorganisms
by Urban, Sinisa
Nature Reviews Microbiology, ISSN 1740-1526, 06/2009, Volume 7, Issue 6, pp. 411 - 423
Proteolysis in cellular membranes to liberate effector domains from their transmembrane anchors is a well-studied regulatory mechanism in animal biology and... 
HOST-CELL INVASION | ANTI-SIGMA FACTOR | HEPATITIS-C VIRUS | SIGNAL PEPTIDE PEPTIDASE | ENTEROCOCCUS-FAECALIS | TOXOPLASMA-GONDII | MICROBIOLOGY | PROVIDENCIA-STUARTII | CORE PROTEIN | RHOMBOID PROTEASE | SEX-PHEROMONE | Bacteria - metabolism | Viruses - pathogenicity | Eukaryota - physiology | Viruses - metabolism | Eukaryota - metabolism | Fungi - metabolism | Peptide Hydrolases - chemistry | Cell Membrane - chemistry | Host-Pathogen Interactions | Animals | Membrane Proteins - chemistry | Membrane Proteins - physiology | Models, Biological | Peptide Hydrolases - physiology | Fungi - physiology | Bacteria - pathogenicity | Cell Membrane - metabolism | Membrane Proteins - metabolism | Peptide Hydrolases - metabolism | Pathogenic microorganisms | Proteases | Proteolysis | Physiological aspects | Cell membranes | Research | Health aspects | invasion | site-2 protease | cell signalling | presenilin | tuberculosis | rhomboid | signal peptide peptidase | regulated intramembrane proteolysis | malaria | hepatitis | cholera
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8. Full Text Requirements for Signal Peptide Peptidase-Catalyzed Intramembrane Proteolysis
by Lemberg, Marius K and Martoglio, Bruno
Molecular Cell, ISSN 1097-2765, 2002, Volume 10, Issue 4, pp. 735 - 744
The presenilin-type aspartic protease signal peptide peptidase (SPP) can cleave signal peptides within their transmembrane region. SPP is essential for... 
ENDOPLASMIC-RETICULUM MEMBRANE | TRANSCRIPTION FACTORS | AMINO-ACIDS | BIOCHEMISTRY & MOLECULAR BIOLOGY | SEQUENCE-DERIVED PEPTIDES | SURFACE EXPRESSION | HLA-E BINDS | REGULATED RELEASE | CLEAVAGE | TRANSMEMBRANE SEGMENT | PROTEIN INSERTION | CELL BIOLOGY | Consensus Sequence | Amino Acid Sequence | Cell Line | Cricetinae | Protein Sorting Signals - physiology | Protein Precursors - chemistry | RNA, Messenger - genetics | Molecular Sequence Data | Substrate Specificity | Aspartic Acid Endopeptidases - genetics | RNA, Messenger - metabolism | Blotting, Western | Amino Acid Motifs | Protein Precursors - metabolism | Cell Membrane - enzymology | Animals | Aspartic Acid Endopeptidases - metabolism | Cell Membrane - metabolism
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9. Full Text Reconstitution of Intramembrane Proteolysis in vitro Reveals That Pure Rhomboid Is Sufficient for Catalysis and Specificity
by Sinisa Urban and Michael S. Wolfe and Thomas C. Südhof
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 2/2005, Volume 102, Issue 6, pp. 1883 - 1888
Intramembrane proteolysis is a new paradigm in biology that controls signaling events throughout evolution. Hydrolysis of peptide bonds is thought to occur... 
Proteins | Membrane lipids | Biological Sciences | Substrate specificity | Lipids | Bacteria | Phospholipids | Catalysis | Physiological regulation | Detergents | P branes | Presenilin | Signal peptide peptidase | Regulated intramembrane proteolysis | Site-2 protease | Cell signaling | COMPLEX | MEMBRANE | MULTIDISCIPLINARY SCIENCES | STRESS-RESPONSE | signal peptide peptidase | CLEAVAGE | IDENTIFICATION | PROTEASES | FAMILY | SUBSTRATE-SPECIFICITY | site-2 protease | presenilin | cell signaling | GAMMA-SECRETASE ACTIVITY | regulated intramembrame proteolysis | Detergents - chemistry | Membrane Proteins - genetics | Humans | Bacterial Proteins - genetics | Substrate Specificity | Protease Inhibitors - metabolism | Drosophila Proteins - metabolism | Recombinant Fusion Proteins - metabolism | Peptide Hydrolases - chemistry | Cell Membrane - chemistry | Animals | Micelles | Membrane Lipids - metabolism | Recombinant Fusion Proteins - genetics | Bacterial Proteins - metabolism | Signal Transduction - physiology | Cell Membrane - metabolism | Membrane Proteins - metabolism | Drosophila Proteins - genetics | Peptide Hydrolases - metabolism | Research | Proteolysis | Signal peptides | regulated intramembrane proteolysis
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10. Full Text TGF-β inhibits alveolar protein transport by promoting shedding, regulated intramembrane proteolysis, and transcriptional downregulation of megalin
by Mazzocchi, Luciana C and Vohwinkel, Christine U and Mayer, Konstantin and Herold, Susanne and Morty, Rory E and Seeger, Werner and Vadász, István
American Journal of Physiology - Lung Cellular and Molecular Physiology, ISSN 1040-0605, 11/2017, Volume 313, Issue 5, pp. L807 - L824
Disruption of the alveolar-capillary barrier is a hallmark of acute respiratory distress syndrome (ARDS) that leads to the accumulation of protein-rich edema... 
Receptor shedding | Alveolar protein transport | Matrix metalloproteinases | Regulated intramembrane proteolysis | Megalin | CLEARANCE | CELLS | PHYSIOLOGY | megalin | ACUTE LUNG INJURY | E-CADHERIN | alveolar protein transport | receptor shedding | FLUID | MMP-2 | RESPIRATORY SYSTEM | MEDIATED ENDOCYTOSIS | ALBUMIN | GELATINASES | regulated intramembrane proteolysis | matrix metalloproteinases | Matrix Metalloproteinase 2 - metabolism | Down-Regulation | Endocytosis - drug effects | Humans | Cells, Cultured | Low Density Lipoprotein Receptor-Related Protein-2 - metabolism | Protein Transport - drug effects | Proteolysis - drug effects | Transforming Growth Factor beta - pharmacology | Animals | Protein Kinase C - metabolism | Cell Membrane - metabolism | Lipoproteins, LDL - metabolism | Matrix Metalloproteinases - metabolism | Transforming Growth Factor beta - metabolism | Research
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11. Full Text Roles of regulated intramembrane proteolysis in virus infection and antiviral immunity
by Ye, Jin
BBA - Biomembranes, ISSN 0005-2736, 12/2013, Volume 1828, Issue 12, pp. 2926 - 2932
Regulated intramembrane proteolysis (RIP) is a signaling mechanism through which transmembrane precursor proteins are cleaved to liberate their cytoplasmic... 
Signal peptide-peptidase | Virus | CREB3 | Regulated intramembrane proteolysis | Site-2 protease | CREB3L1 | TRANSCRIPTION FACTOR LUMAN | RNA REPLICATION | SIGNAL PEPTIDE PEPTIDASE | ER STRESS | BIOCHEMISTRY & MOLECULAR BIOLOGY | SURFACE EXPRESSION | TRANSMEMBRANE DOMAIN | ENDOPLASMIC-RETICULUM STRESS | CORE PROTEIN | HLA-E | BIOPHYSICS | HEPATITIS-C VIRUS | Cell Nucleus - immunology | Metalloendopeptidases - genetics | Hepacivirus - immunology | Humans | Endoplasmic Reticulum - metabolism | Cell Nucleus - metabolism | Proteolysis | Cell Nucleus - virology | Cyclic AMP Response Element-Binding Protein - immunology | Nerve Tissue Proteins - immunology | Signal Transduction | Gene Expression Regulation | Histocompatibility Antigens Class I - immunology | Endoplasmic Reticulum - virology | Histocompatibility Antigens Class I - genetics | Immunity, Innate | Metalloendopeptidases - immunology | Nerve Tissue Proteins - genetics | Host-Pathogen Interactions | Cell Membrane - enzymology | Cyclic AMP Response Element-Binding Protein - genetics | Cytomegalovirus - immunology | Animals | Endoplasmic Reticulum - immunology | Cell Membrane - virology | Cell Membrane - immunology | Virus diseases | Proteins | Antiviral agents | Proteases | Health aspects
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12. Full Text Intramembrane proteolysis of Toxoplasma apical membrane antigen 1 facilitates host-cell invasion but is dispensable for replication
by Fabiola Parussini and Qing Tang and Syed M. Moin and Jeffrey Mital and Sinisa Urban and Gary E. Ward
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 5/2012, Volume 109, Issue 19, pp. 7463 - 7468
Apical membrane antigen 1 (AMA1) is a conserved transmembrane adhesin of apicomplexan parasites that plays an important role in host-cell invasion. Toxoplasma... 
Proteins | COS cells | Intracellular parasitism | Antigens | Secretion | Plasma cells | Parasitism | Cell membranes | Parasites | Parasite hosts | Microneme | Malaria | Regulated intramembrane proteolysis | Cell signaling | AMA1 | COMPLEX | PLASMODIUM-FALCIPARUM MEROZOITES | MULTIDISCIPLINARY SCIENCES | RON2 | MICRONEME PROTEINS | HOMOLOG | malaria | microneme | CLEAVAGE | cell signaling | MOVING JUNCTION | GONDII | regulated intramembrane proteolysis | EXPRESSION | Humans | Cercopithecus aethiops | Molecular Sequence Data | Male | Green Fluorescent Proteins - genetics | Toxoplasma - physiology | Protozoan Proteins - genetics | Antigens, Protozoan - metabolism | Protozoan Proteins - metabolism | Proteolysis | Cell Division | Antigens, Protozoan - genetics | Cell Membrane - metabolism | Host-Parasite Interactions | Toxoplasma - metabolism | Cell Membrane - parasitology | Amino Acid Sequence | Green Fluorescent Proteins - metabolism | Cells, Cultured | Blotting, Western | Sequence Homology, Amino Acid | Animals | Toxoplasma - genetics | Mutation | COS Cells | Microscopy, Fluorescence | Toxoplasma | Physiological aspects | Research | Cell adhesion molecules | Biological Sciences
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