scholarly article | Q13442814 |
P50 | author | Thomas Kukar | Q42165296 |
Jens Wiltfang | Q42165310 | ||
P2093 | author name string | Barbara A Cottrell | |
Edward H Koo | |||
Sascha Weggen | |||
Todd E Golde | |||
Hermann Esselmann | |||
Claus U Pietrzik | |||
Thomas B Ladd | |||
Karlheinz Baumann | |||
Robert Schubenel | |||
Sabine Paul | |||
Stefanie Leuchtenberger | |||
Justin W Torpey | |||
Eva Czirr | |||
P2860 | cites work | Purification and characterization of the human gamma-secretase complex | Q24300026 |
When loss is gain: reduced presenilin proteolytic function leads to increased Abeta42/Abeta40. Talking Point on the role of presenilin mutations in Alzheimer disease | Q24676480 | ||
Loss-of-function presenilin mutations in Alzheimer disease. Talking Point on the role of presenilin mutations in Alzheimer disease | Q24676498 | ||
Diverse compounds mimic Alzheimer disease-causing mutations by augmenting Abeta42 production | Q28245521 | ||
The gamma-secretase complex: membrane-embedded proteolytic ensemble | Q28248433 | ||
The same gamma-secretase accounts for the multiple intramembrane cleavages of APP | Q28284426 | ||
Presenilin clinical mutations can affect gamma-secretase activity by different mechanisms | Q28290934 | ||
Evidence that nonsteroidal anti-inflammatory drugs decrease amyloid beta 42 production by direct modulation of gamma-secretase activity | Q33187378 | ||
GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Abeta42. | Q33276402 | ||
Anti-Abeta42- and anti-Abeta40-specific mAbs attenuate amyloid deposition in an Alzheimer disease mouse model | Q34195981 | ||
Selected non-steroidal anti-inflammatory drugs and their derivatives target gamma-secretase at a novel site. Evidence for an allosteric mechanism. | Q34649758 | ||
Mechanism of the cleavage specificity of Alzheimer's disease gamma-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein | Q35065215 | ||
Disease modifying therapy for AD? | Q36640414 | ||
Selective modulation of Abeta42 production in Alzheimer's disease: non-steroidal anti-inflammatory drugs and beyond. | Q36653723 | ||
Generation of Abeta38 and Abeta42 is independently and differentially affected by familial Alzheimer disease-associated presenilin mutations and gamma-secretase modulation | Q40061988 | ||
1-(3',4'-Dichloro-2-fluoro[1,1'-biphenyl]-4-yl)-cyclopropanecarboxylic acid (CHF5074), a novel gamma-secretase modulator, reduces brain beta-amyloid pathology in a transgenic mouse model of Alzheimer's disease without causing peripheral toxicity. | Q40076266 | ||
gamma-Cleavage is dependent on zeta-cleavage during the proteolytic processing of amyloid precursor protein within its transmembrane domain | Q40374588 | ||
Presenilin 2 familial Alzheimer's disease mutations result in partial loss of function and dramatic changes in Abeta 42/40 ratios. | Q40467990 | ||
Longer forms of amyloid beta protein: implications for the mechanism of intramembrane cleavage by gamma-secretase. | Q40472233 | ||
A subset of NSAIDs lower amyloidogenic Abeta42 independently of cyclooxygenase activity | Q43793656 | ||
Sulindac sulfide is a noncompetitive gamma-secretase inhibitor that preferentially reduces Abeta 42 generation | Q44362261 | ||
Abeta42-lowering nonsteroidal anti-inflammatory drugs preserve intramembrane cleavage of the amyloid precursor protein (APP) and ErbB-4 receptor and signaling through the APP intracellular domain. | Q44460129 | ||
Nonsteroidal anti-inflammatory drugs lower Abeta42 and change presenilin 1 conformation | Q45078363 | ||
Insensitivity to Abeta42-lowering nonsteroidal anti-inflammatory drugs and gamma-secretase inhibitors is common among aggressive presenilin-1 mutations | Q48134209 | ||
Blocking the cleavage at midportion between gamma- and epsilon-sites remarkably suppresses the generation of amyloid beta-protein. | Q51468621 | ||
N-Substituted carbazolyloxyacetic acids modulate Alzheimer associated gamma-secretase. | Q53382308 | ||
P433 | issue | 25 | |
P407 | language of work or name | English | Q1860 |
P1104 | number of pages | 6 | |
P304 | page(s) | 17049-17054 | |
P577 | publication date | 2008-04-21 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | Independent generation of Abeta42 and Abeta38 peptide species by gamma-secretase | |
P478 | volume | 283 |
Q48300002 | APP mutations in the Aβ coding region are associated with abundant cerebral deposition of Aβ38. |
Q33572654 | Aberrant amyloid precursor protein (APP) processing in hereditary forms of Alzheimer disease caused by APP familial Alzheimer disease mutations can be rescued by mutations in the APP GxxxG motif |
Q28828789 | Aftins increase amyloid-β42, lower amyloid-β38, and do not alter amyloid-β40 extracellular production in vitro: toward a chemical model of Alzheimer's disease? |
Q34467478 | Alzheimer presenilin-1 mutations dramatically reduce trimming of long amyloid β-peptides (Aβ) by γ-secretase to increase 42-to-40-residue Aβ. |
Q39584972 | Attenuated Abeta42 responses to low potency gamma-secretase modulators can be overcome for many pathogenic presenilin mutants by second-generation compounds |
Q35029086 | Autosomal-dominant Alzheimer's disease: a review and proposal for the prevention of Alzheimer's disease |
Q33885289 | Beta-amyloid precursor protein mutants respond to gamma-secretase modulators |
Q36559869 | Cerebral white matter lesions - associations with Aβ isoforms and amyloid PET |
Q30363483 | Changed membrane integration and catalytic site conformation are two mechanisms behind the increased Aβ42/Aβ40 ratio by presenilin 1 familial Alzheimer-linked mutations. |
Q36081889 | Chemical Biology, Molecular Mechanism and Clinical Perspective of γ-Secretase Modulators in Alzheimer's Disease |
Q36668200 | Deposition of C-terminally truncated Aβ species Aβ37 and Aβ39 in Alzheimer's disease and transgenic mouse models |
Q38101383 | Development and mechanism of γ-secretase modulators for Alzheimer's disease |
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Q36674203 | Effect of Presenilin Mutations on APP Cleavage; Insights into the Pathogenesis of FAD |
Q41907099 | Effects of cerebrovascular disease on amyloid precursor protein metabolites in cerebrospinal fluid |
Q38693441 | Familial Presenilin Mutations and Sporadic Alzheimer's Disease Pathology: Is the Assumption of Biochemical Equivalence Justified? |
Q48299006 | Generation and Partial Characterization of Rabbit Monoclonal Antibody to Amyloid-β Peptide 1-37 (Aβ37). |
Q40506355 | Generation of Rabbit Monoclonal Antibody to Amyloid-β38 (Aβ38): Increased Plasma Aβ38 Levels in Down Syndrome |
Q90661748 | Helix-Switch Enables C99 Dimer Transition between the Multiple Conformations |
Q35913521 | Modulation of Aβ42 in vivo by γ-secretase modulator in primates and humans |
Q48031219 | Plasma Amyloid-β Levels, Cerebral Small Vessel Disease, and Cognition: The Rotterdam Study |
Q55516241 | Plasma amyloid-β levels, cerebral atrophy and risk of dementia: a population-based study. |
Q51770733 | Presenilin-1 but not amyloid precursor protein mutations present in mouse models of Alzheimer’s disease attenuate the response of cultured cells to γ-secretase modulators regardless of their potency and structure |
Q36294856 | Second generation γ-secretase modulators exhibit different modulation of Notch β and Aβ production |
Q33496258 | Selective modulation of amyloid-beta peptide degradation by flurbiprofen, fenofibrate, and related compounds regulates Abeta levels |
Q47222878 | Structural heterogeneity and intersubject variability of Aβ in familial and sporadic Alzheimer's disease |
Q35562828 | Substrate sequence influences γ-secretase modulator activity, role of the transmembrane domain of the amyloid precursor protein |
Q33726342 | The large hydrophilic loop of presenilin 1 is important for regulating gamma-secretase complex assembly and dictating the amyloid beta peptide (Abeta) Profile without affecting Notch processing |
Q36000134 | The mechanism of γ-Secretase dysfunction in familial Alzheimer disease |
Q37591341 | Transmembrane fragment structures of amyloid precursor protein depend on membrane surface curvature. |
Q39285976 | Unlocking truths of γ-secretase in Alzheimer's disease: what is the translational potential? |
Q39451354 | Γ-secretase modulators do not induce Aβ-rebound and accumulation of β-C-terminal fragment |
Q35871906 | γ-Secretase Modulators and APH1 Isoforms Modulate γ-Secretase Cleavage but Not Position of ε-Cleavage of the Amyloid Precursor Protein (APP). |
Q41831750 | γ-Secretase associated with lipid rafts: multiple interactive pathways in the stepwise processing of β-carboxyl-terminal fragment |
Q26830462 | γ-Secretase inhibitors and modulators |