| Year |
Citation |
Score |
| 2003 |
King GD, Perez RG, Steinhilb ML, Gaut JR, Turner RS. X11alpha modulates secretory and endocytic trafficking and metabolism of amyloid precursor protein: mutational analysis of the YENPTY sequence. Neuroscience. 120: 143-54. PMID 12849748 DOI: 10.1016/S0306-4522(03)00284-7 |
0.457 |
|
| 2002 |
Ho CS, Marinescu V, Steinhilb ML, Gaut JR, Turner RS, Stuenkel EL. Synergistic effects of Munc18a and X11 proteins on amyloid precursor protein metabolism. The Journal of Biological Chemistry. 277: 27021-8. PMID 12016213 DOI: 10.1074/Jbc.M201823200 |
0.486 |
|
| 2002 |
Steinhilb ML, Turner RS, Gaut JR. ELISA analysis of beta-secretase cleavage of the Swedish amyloid precursor protein in the secretory and endocytic pathways. Journal of Neurochemistry. 80: 1019-28. PMID 11953452 DOI: 10.1046/J.0022-3042.2002.00764.X |
0.458 |
|
| 2002 |
Gau JT, Steinhilb ML, Kao TC, D'Amato CJ, Gaut JR, Frey KA, Turner RS. Stable beta-secretase activity and presynaptic cholinergic markers during progressive central nervous system amyloidogenesis in Tg2576 mice. The American Journal of Pathology. 160: 731-8. PMID 11839594 DOI: 10.1016/S0002-9440(10)64893-6 |
0.421 |
|
| 2001 |
Steinhilb ML, Turner RS, Gaut JR. The protease inhibitor, MG132, blocks maturation of the amyloid precursor protein Swedish mutant preventing cleavage by beta-Secretase. The Journal of Biological Chemistry. 276: 4476-84. PMID 11084038 DOI: 10.1074/Jbc.M008793200 |
0.453 |
|
| 2000 |
Steinhilb ML, Scott Turner R, Gaut JR. Quantitative evaluation of β-secretase cleavage of amyloid precursor protein in the secretory and endocytic pathways Neurobiology of Aging. 21: 115. DOI: 10.1016/S0197-4580(00)82317-9 |
0.358 |
|
| 1998 |
Yang Y, Turner RS, Gaut JR. The chaperone BiP/GRP78 binds to amyloid precursor protein and decreases Abeta40 and Abeta42 secretion. The Journal of Biological Chemistry. 273: 25552-5. PMID 9748217 DOI: 10.1074/Jbc.273.40.25552 |
0.516 |
|
| 1997 |
Gaut JR. In vivo threonine phosphorylation of immunoglobulin binding protein (BiP) maps to its protein binding domain Cell Stress and Chaperones. 2: 252-262. PMID 9495282 DOI: 10.1379/1466-1268(1997)002<0252:Ivtpoi>2.3.Co;2 |
0.341 |
|
| 1996 |
Hendershot L, Wei J, Gaut J, Melnick J, Aviel S, Argon Y. Inhibition of immunoglobulin folding and secretion by dominant negative BiP ATPase mutants. Proceedings of the National Academy of Sciences of the United States of America. 93: 5269-74. PMID 8643565 DOI: 10.1073/Pnas.93.11.5269 |
0.382 |
|
| 1995 |
Hendershot LM, Wei JY, Gaut JR, Lawson B, Freiden PJ, Murti KG. In vivo expression of mammalian BiP ATPase mutants causes disruption of the endoplasmic reticulum Molecular Biology of the Cell. 6: 283-296. PMID 7612964 DOI: 10.1091/Mbc.6.3.283 |
0.338 |
|
| 1995 |
Wei J, Gaut JR, Hendershot LM. In vitro dissociation of BiP-peptide complexes requires a conformational change in BiP after ATP binding but does not require ATP hydrolysis Journal of Biological Chemistry. 270: 26677-26682. PMID 7592894 DOI: 10.1074/Jbc.270.44.26677 |
0.358 |
|
| 1993 |
Gaut JR, Hendershot LM. Mutations within the nucleotide binding site of immunoglobulin-binding protein inhibit ATPase activity and interfere with release of immunoglobulin heavy chain Journal of Biological Chemistry. 268: 7248-7255. PMID 8463260 |
0.318 |
|
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