A novel mechanism for the regulation of amyloid precursor protein metabolism

Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease

Sherrington, R., Rogaev, E. I., Liang, Y., Rogaeva, E. A., Levesque, G., Ikeda, M., Chi, H., Lin, C., Li, G., Holman, K., et al. (1995) · Nature · doi:10.1038/375754a0 · Cited by 4,051 · see citing works

Secreted amyloid β–protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease

Scheuner, D., Eckman, C., Jensen, M., Song, X., Citron, M., Suzuki, N., Bird, T. D., Hardy, J., Hutton, M., Kukull, W., et al. (1996) · Nature Medicine · doi:10.1038/nm0896-864 · Cited by 2,599 · see citing works

A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain

De Strooper, B., Annaert, W., Cupers, P., Saftig, P., Craessaerts, K., Mumm, J. S., Schroeter, E. H., Schrijvers, V., Wolfe, M. S., Ray, W. J., et al. (1999) · Nature · doi:10.1038/19083 · Cited by 2,100 · see citing works

Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene

Rogaev, E. I., Sherrington, R., Rogaeva, E. A., Levesque, G., Ikeda, M., Liang, Y., Chi, H., Lin, C., Holman, K., Tsuda, T., et al. (1995) · Nature · doi:10.1038/376775a0 · Cited by 2,052 · see citing works

Amyloid β-peptide is produced by cultured cells during normal metabolism

Haass, C., Schlossmacher, M. G., Hung, A. Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B. L., Lieberburg, I., Koo, E. H., Schenk, D., Teplow, D. B., et al. (1992) · Nature · doi:10.1038/359322a0 · Cited by 1,921 · see citing works

Rapid degradation of a large fraction of newly synthesized proteins by proteasomes

Schubert, U., Antón, L. C., Gibbs, J. S., Norbury, C. C., Yewdell, J. W., & Bennink, J. R. (2000) · Nature · doi:10.1038/35008096 · Cited by 1,536 · see citing works

Familial Alzheimer's Disease–Linked Presenilin 1 Variants Elevate Aβ1–42/1–40 Ratio In Vitro and In Vivo

Borchelt, D. R., Thinakaran, G., Eckman, C. B., Lee, M. K., Davenport, F., Ratovitsky, T., Prada, C.-M., Kim, G., Seekins, S., Yager, D., et al. (1996) · Neuron · doi:10.1016/s0896-6273(00)80230-5 · Cited by 1,478 · see citing works

Protein Oligomerization In The Endoplasmic Reticulum

Hurtley, S. M., & Helenius, A. (1989) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.05.110189.001425 · Cited by 1,002 · see citing works

Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity

Meng, L., Mohan, R., Kwok, B. H. B., Elofsson, M., Sin, N., & Crews, C. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10403 · Cited by 926 · see citing works

Presenilin is required for activity and nuclear access of Notch in Drosophila

Struhl, G., & Greenwald, I. (1999) · Nature · doi:10.1038/19091 · Cited by 804 · see citing works

Clonal cell lines from the rat central nervous system

Schubert, D. A., Heinemann, S. F., Carlisle, W., Tarikas, H., Kimes, B. W., Patrick, J. W., Steinbach, J. H., Culp, W., & Brandt, B. L. (1974) · Nature · doi:10.1038/249224a0 · Cited by 713 · see citing works

A presenilin‐1/γ‐secretase cleavage releases the E‐cadherin intracellular domain and regulates disassembly of adherens junctions

Marambaud, P., Shioi, J., Serban, G., Georgakopoulos, A., Sarner, S., Nagy, V., Baki, L., Wen, P., Efthimiopoulos, S., Shao, Z., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/21.8.1948 · Cited by 686 · see citing works

Protein degradation in the endoplasmic reticulum

Klausner, R. D., & Sitia, R. (1990) · Cell · doi:10.1016/0092-8674(90)90104-m · Cited by 653 · see citing works

Proteolytic processing and cell biological functions of the amyloid precursor protein

Strooper, B. D., & Annaert, W. G. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.11.1857 · Cited by 628 · see citing works

LIN-12/Notch signaling: lessons from worms and fliesPreprint

Greenwald, I. (1998) · Genes & Development · doi:10.1101/gad.12.12.1751 · Cited by 541 · see citing works

Presenilin-1 mutations downregulate the signalling pathway of the unfolded-protein response

Katayama, T., Imaizumi, K., Sato, N., Miyoshi, K., Kudo, T., Hitomi, J., Morihara, T., Yoneda, T., Gomi, F., Mori, Y., et al. (1999) · Nature Cell Biology · doi:10.1038/70265 · Cited by 521 · see citing works

Transition-state analogue inhibitors of γ-secretase bind directly to presenilin-1

Esler, W. P., Kimberly, W. T., Ostaszewski, B. L., Diehl, T. S., Moore, C. L., Tsai, J.-Y., Rahmati, T., Xia, W., Selkoe, D. J., & Wolfe, M. S. (2000) · Nature Cell Biology · doi:10.1038/35017062 · Cited by 514 · see citing works

Neurogenic phenotypes and altered Notch processing in Drosophila Presenilin mutants

Ye, Y., Lukinova, N. I., & Fortini, M. (1999) · Nature · doi:10.1038/19096 · Cited by 492 · see citing works

Alzheimer's Aβ(1–42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells

Cook, D. G., Forman, M. S., Sung, J. C., Leight, S., Kolson, D. L., Iwatsubo, T., Lee, V. M.-Y., & Doms, R. W. (1997) · Nature Medicine · doi:10.1038/nm0997-1021 · Cited by 439 · see citing works

Cellular mechanisms of β-amyloid production and secretion

Sinha, S., & Lieberburg, I. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11049 · Cited by 438 · see citing works

Lactacystin, Proteasome Function, and Cell Fate

Fenteany, G., & Schreiber, S. L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.15.8545 · Cited by 414 · see citing works

Lactacystin and clasto-Lactacystin β-Lactone Modify Multiple Proteasome β-Subunits and Inhibit Intracellular Protein Degradation and Major Histocompatibility Complex Class I Antigen Presentation

Craiu, A., Gaczynska, M. E., Akopian, T. N., Gramm, C. F., Fenteany, G., Goldberg, A. L., & Rock, K. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.20.13437 · Cited by 382 · see citing works

Protein Topology of Presenilin 1

Doan, A., Thinakaran, G., Borchelt, D., Slunt, H. H., Ratovitski, T., Podlisny, M. B., Selkoe, D. J., Seeger, M., Gandy, S., Price, D. L., et al. (1996) · Neuron · doi:10.1016/s0896-6273(00)80232-9 · Cited by 371 · see citing works

Effects of PS1 Deficiency on Membrane Protein Trafficking in Neurons

Naruse, S., Thinakaran, G., Luo, J.-J., Kusiak, J. W., Tomita, T., Iwatsubo, T., Qian, X., Ginty, D. D., Price, D. L., Borchelt, D. R., et al. (1998) · Neuron · doi:10.1016/s0896-6273(00)80637-6 · Cited by 355 · see citing works

The regulation of amyloid β protein precursor secretion and its modulatory role in cell adhesion

Schubert, D. A., Jin, L.-W., Saitoh, T., & Cole, G. M. (1989) · Neuron · doi:10.1016/0896-6273(89)90237-7 · Cited by 353 · see citing works

Peptidomimetic Probes and Molecular Modeling Suggest That Alzheimer's γ-Secretase Is an Intramembrane-Cleaving Aspartyl Protease

Wolfe, M. S., Xia, W., Moore, C. L., Leatherwood, D. D., Ostaszewski, B., Rahmati, T., Donkor, I. O., & Selkoe, D. J. (1999) · Biochemistry · doi:10.1021/bi982562p · Cited by 289 · see citing works

Generation of Alzheimer β-amyloid protein in the trans-Golgi network in the apparent absence of vesicle formation

Xu, H., Sweeney, D. A., Wang, R., Thinakaran, G., Lo, A., Sisodia, S. S., Greengard, P., & Gandy, S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.3748 · Cited by 281 · see citing works

A Role for Presenilin-1 in Nuclear Accumulation of Ire1 Fragments and Induction of the Mammalian Unfolded Protein Response

Niwa, M., Sidrauski, C., Kaufman, R. J., & Walter, P. (1999) · Cell · doi:10.1016/s0092-8674(00)81667-0 · Cited by 276 · see citing works

Alternative splicing generates a secreted form of N-CAM in muscle and brain

Gower, H. J., Barton, C. H., Elsom, V. L., Thompson, J., Moore, S. E., Dickson, G., & Walsh, F. S. (1988) · Cell · doi:10.1016/0092-8674(88)90241-3 · Cited by 241 · see citing works

Regulation of Amyloid Precursor Protein Cleavage

Mills, J., & Reiner, P. B. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0720443.x · Cited by 221 · see citing works

A Substrate-Based Difluoro Ketone Selectively Inhibits Alzheimer's γ-Secretase Activity

Wolfe, M. S., Citron, M., Diehl, T. S., Xia, W., Donkor, I. O., & Selkoe, D. J. (1998) · Journal of Medicinal Chemistry · doi:10.1021/jm970621b · Cited by 214 · see citing works

Characterization of a Presenilin-mediated Amyloid Precursor Protein Carboxyl-terminal Fragment γ

Yu, C., Kim, S.-H., Ikeuchi, T., Xu, H., Gasparini, L., Wang, R., & Sisodia, S. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100410200 · Cited by 210 · see citing works

Chloroquine inhibits intracellular degradation but not secretion of Alzheimer beta/A4 amyloid precursor protein.

Caporaso, G. L., Gandy, S., Buxbaum, J. D., & Greengard, P. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.6.2252 · Cited by 204 · see citing works

Peptides containing the RERMS sequence of amyloid beta/A4 protein precursor bind cell surface and promote neurite extension

Jin, L., Ninomiya, H., Roch, J., Schubert, D. A., Masliah, E., Otero, D. A., & Saitoh, T. (1994) · Journal of Neuroscience · doi:10.1523/jneurosci.14-09-05461.1994 · Cited by 198 · see citing works

N-CAM and N-Cadherin Expression during in Vitro Chondrogenesis

Tavella, S., Raffo, P., Tacchetti, C., Cancedda, R., & Castagnola, P. (1994) · Experimental Cell Research · doi:10.1006/excr.1994.1352 · Cited by 188 · see citing works

The Chaperone BiP/GRP78 Binds to Amyloid Precursor Protein and Decreases Aβ40 and Aβ42 Secretion

Yang, Y., Turner, R. S., & Gaut, J. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.40.25552 · Cited by 179 · see citing works

Regulation of Amyloid Protein Precursor (APP) Binding to Collagen and Mapping of the Binding Sites on APP and Collagen Type I

Beher, D., Hesse, L., Masters, C. L., & Multhaup, G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.3.1613 · Cited by 170 · see citing works

Presenilin-1 differentially facilitates endoproteolysis of the β-amyloid precursor protein and Notch

Capell, A., Steiner, H., Romig, H., Keck, S., Baader, M., Grim, M. G., Baumeister, R., & Haass, C. (2000) · Nature Cell Biology · doi:10.1038/35008626 · Cited by 147 · see citing works

Inhibition of β-amyloid formation identifies proteolytic precursors and subcellular site of catabolism

Higaki, J. N., Quon, D. H., Zhong, Z., & Cordell, B. (1995) · Neuron · doi:10.1016/0896-6273(95)90322-4 · Cited by 145 · see citing works

Presenilin complexes with the C-terminal fragments of amyloid precursor protein at the sites of amyloid β-protein generation

Xia, W., Ray, W. J., Ostaszewski, B. L., Rahmati, T., Kimberly, W. T., Wolfe, M. S., Zhang, J., Goate, A., & Selkoe, D. J. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.16.9299 · Cited by 133 · see citing works

The Role of Presenilins in γ-Secretase Activity

Wolfe, M. S., & Haass, C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.r000026200 · Cited by 132 · see citing works

The expression of amyloid beta protein precursor protects nerve cells from β-amyloid and glutamate toxicity and alters their interaction with the extracellular matrix

Schubert, D. A., & Behl, C. (1993) · Brain Research · doi:10.1016/0006-8993(93)91331-l · Cited by 131 · see citing works

Alzheimer's Amyloid Precursor Protein α-Secretase Is Inhibited by Hydroxamic Acid-Based Zinc Metalloprotease Inhibitors: Similarities to the Angiotensin Converting Enzyme Secretase

Parvathy, S., Hussain, I., Karran, E. H., Turner, A. J., & Hooper, N. M. (1998) · Biochemistry · doi:10.1021/bi972034y · Cited by 123 · see citing works

Aspartate Mutations in Presenilin and γ‐Secretase Inhibitors Both Impair Notch1 Proteolysis and Nuclear Translocation with Relative Preservation of Notch1 Signaling

Berezovska, O., Jack, C. E., McLean, P. J., Aster, J. C., Hicks, C. D., Xia, W., Wolfe, M. S., Kimberly, W. T., Weinmaster, G., Selkoe, D. J., et al. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0750583.x · Cited by 119 · see citing works

Role of the proteasome in Alzheimer’s disease

Checler, F., da Costa, C. A., Ancolio, K., Chevallier, N., Lopez‐Perez, E., & Marambaud, P. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00039-9 · Cited by 98 · see citing works

Cholesterol decreases secretion of the secreted form of amyloid precursor protein by interfering with glycosylation in the protein secretory pathway

Galbete, J. L., Martin, T. R., PERESSINI, E., Modena, P., Bianchi, R., & Forloni, G. (2000) · Biochemical Journal · doi:10.1042/bj3480307 · Cited by 97 · see citing works

An antibody to β amyloid and the amyloid precursor protein inhibits cell-substratum adhesion in many mammalian cell types

Chen, M., & Yankner, B. A. (1991) · Neuroscience Letters · doi:10.1016/0304-3940(91)90034-q · Cited by 96 · see citing works

In vivo inhibition of cyclin B degradation and induction of cell-cycle arrest in mammalian cells by the neutral cysteine protease inhibitor N-acetylleucylleucylnorleucinal.

Sherwood, S. W., Kung, A. L., Roitelman, J., Simoni, R., & SCHIMKE, R. T. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.8.3353 · Cited by 91 · see citing works

Expression of β-Amyloid Precursor Protein-CD3γ Chimeras to Demonstrate the Selective Generation of Amyloid β1–40and Amyloid β1–42 Peptides within Secretory and Endocytic Compartments

Soriano, S., Chyung, A. S. C., Chen, X., Stokin, G. B., Lee, V. M. ‐., & Koo, E. H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.45.32295 · Cited by 89 · see citing works

Wild-type but not Alzheimer-mutant amyloid precursor protein confers resistance against p53-mediated apoptosis

Xu, X., Yang, D., Wyss‐Coray, T., Yan, J. S., Gan, L., Sun, Y., & Mucke, L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.13.7547 · Cited by 86 · see citing works

Chloroquine inhibits intracellular segradation but not decretion of Alzheimerβ/A4 amyloid precursor protein.

Caporaso, G. (1992) · Medical Entomology and Zoology · Cited by 80 · see citing works

Complex, Two-way Traffic of Molecules Across the Membrane of the Endoplasmic Reticulum

Suzuki, T., Yan, Q., & Lennarz, W. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.17.10083 · Cited by 78 · see citing works

Calpain Inhibitor I Increases β-Amyloid Peptide Production by Inhibiting the Degradation of the Substrate of γ-Secretase

Zhang, L., Song, L., & Parker, E. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.13.8966 · Cited by 70 · see citing works

Isolation and Characterization of Novel Presenilin Binding Protein

Kashiwa, A., Yoshida, H., Lee, S., Paladino, T., Liu, Y., Chen, Q., Dargusch, R., Schubert, D. A., & Kimura, H. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0750109.x · Cited by 69 · see citing works

Binding Partners of Alzheimer's Disease Proteins: Are They Physiologically Relevant?

Gassen, G. V., Annaert, W. G., & Broeckhoven, C. V. (2000) · Neurobiology of Disease · doi:10.1006/nbdi.2000.0306 · Cited by 59 · see citing works

Down-regulation of the amyloid protein precursor of Alzheimer's disease by antisense oligonucleotides reduces neuronal adhesion to specific substrata

Coulson, E. J., Barrett, G. L., Storey, E., Bartlett, P. F., Beyreuther, K. T., & Masters, C. L. (1997) · Brain Research · doi:10.1016/s0006-8993(97)00757-9 · Cited by 52 · see citing works

Distinct Secretases, a Cysteine Protease and a Serine Protease, Generate the C Termini of Amyloid β‐Proteins Aβ1‐40 and Aβ1‐42, Respectively

Figueiredo‐Pereira, M. E., Efthimiopoulos, S., Tezapsidis, N., Buku, A., Ghiso, J. A., Mehta, P. D., & Robakis, N. K. R. K. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.721417.x · Cited by 46 · see citing works

Proteasome Inhibitors Induce the Association of Alzheimer's Amyloid Precursor Protein with Hsc73

Kouchi, Z., Sorimachi, H., Suzuki, K., & Ishiura, S. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9977 · Cited by 44 · see citing works

Appican Expression Induces Morphological Changes in C6 Glioma Cells and Promotes Adhesion of Neural Cells to the Extracellular Matrix

Wu, A., Pangalos, M. N., Efthimiopoulos, S., Shioi, J., & Robakis, N. K. R. K. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-13-04987.1997 · Cited by 43 · see citing works

γ-Secretase Cleavage Is Distinct from Endoplasmic Reticulum Degradation of the Transmembrane Domain of the Amyloid Precursor Protein

Bunnell, W. L., Pham, H. V., & Glabe, C. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.48.31947 · Cited by 37 · see citing works

Presenilin Binding Protein Is Associated with Neurofibrillary Alterations in Alzheimer’s Disease and Stimulates Tau Phosphorylation

Chen, Q., Yoshida, H., Schubert, D., Maher, P. A., Mallory, M. E., & Masliah, E. (2001) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63005-2 · Cited by 33 · see citing works

Heat shock alters Alzheimer's β amyloid precursor protein expression in human endothelial cells

Ciallella, J. R., Rangnekar, V., & McGillis, J. P. (1994) · Journal of Neuroscience Research · doi:10.1002/jnr.490370611 · Cited by 31 · see citing works

Expression of amyloid precursor protein in human astrocytes in vitro: isoform-specific increases following heat shock

Shepherd, C. E., Bowes, S., Parkinson, D., Cambray-Deakin, M. A., & Pearson, R. C. A. (2000) · Neuroscience · doi:10.1016/s0306-4522(00)00197-4 · Cited by 23 · see citing works

An Accomplice for γ-Secretase Brought into Focus

Sisodia, S. S. (2000) · Science · doi:10.1126/science.289.5488.2296 · Cited by 18 · see citing works

Protease Inhibitors Divert Amyloid Precursor Protein to the Secretory Pathway

Hare, J. F. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4507 · Cited by 9 · see citing works

Presenilin 1 expression in yeast lowers secretion of the amyloid precursor protein

Evin, G. M., Brocque, D. L., Culvenor, J. G., Galatis, D., Weidemann, A., Beyreuther, K. T., Masters, C. L., & Cappai, R. (2000) · Neuroreport · doi:10.1097/00001756-200002070-00036 · Cited by 6 · see citing works

Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity

Côté, J., & Vuori, K. (2002) · Journal of Cell Science · doi:10.1242/jcs.00219 · Cited by 412 · see citing works

DOCK4, a GTPase activator, is disrupted during tumorigenesis.

Yajnik, V., Paulding, C., Sordella, R., McClatchey, A. I., Saito, M., Wahrer, D. C. R., Reynolds, P., Bell, D. W., Lake, R., van den Heuvel, S., et al. (2003) · Cell · doi:10.1016/s0092-8674(03)00155-7 · Cited by 230 · see citing works

Dock180 and ELMO1 Proteins Cooperate to Promote Evolutionarily Conserved Rac-dependent Cell Migration

Grimsley, C. M., Kinchen, J. M., Tosello-Trampont, A.-C., Brugnera, E., Haney, L. B., Lu, M., Chen, Q., Klingele, D., Hengartner, M. O., & Ravichandran, K. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307087200 · Cited by 224 · see citing works

Loss of HRD1-Mediated Protein Degradation Causes Amyloid Precursor Protein Accumulation and Amyloid-β Generation

Kaneko, M., Koike, H., Saito, R., Kitamura, Y., Okuma, Y., & Nomura, Y. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.2422-09.2010 · Cited by 201 · see citing works

Localization and Processing of the Amyloid-β Protein Precursor in Mitochondria-Associated Membranes

Prete, D. D., Suski, J., Oulès, B., Debayle, D., Gay, A.-S., Lacas-Gervais, S., Bussiere, R., Bauer, C., Pinton, P., Paterlini-Bréchot, P., et al. (2016) · Journal of Alzheimer's Disease · doi:10.3233/jad-160953 · Cited by 158 · see citing works

Presenilin diversifies its portfolio

Parks, A. L., & Curtis, D. (2007) · Trends in Genetics · doi:10.1016/j.tig.2007.01.008 · Cited by 150 · see citing works

Determinants of conformational dimerization of Mad2 and its inhibition by p31comet

Mapelli, M., Filipp, F. V., Rancati, G. I., Massimiliano, L., Nezi, L., Stier, G., Hagan, R. S., Confalonieri, S., Piatti, S., Sattler, M., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601033 · Cited by 137 · see citing works

PH domain of ELMO functions in trans to regulate Rac activation via Dock180

Lu, M., Kinchen, J. M., Rossman, K. L., Grimsley‐Myers, C. M., deBakker, C. D., Brugnera, E., Tosello‐Trampont, A., Haney, L. B., Klingele, D., Sondek, J., et al. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb800 · Cited by 130 · see citing works

BubR1 acetylation at prometaphase is required for modulating APC/C activity and timing of mitosis

Choi, E., Choe, H., Min, J., Choi, J. Y., Kim, J., & Lee, H. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.123 · Cited by 126 · see citing works

Isolation and characterisation of DOCK8, a member of the DOCK180‐related regulators of cell morphology

Ruusala, A., & Aspenström, P. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.06.095 · Cited by 110 · see citing works

Mechanism of salvianolic acid B neuroprotection against ischemia/reperfusion induced cerebral injury

Fan, Y., Luo, Q., Wei, J., Lin, R., Li, Y., Li, Y., Chen, Q., Lin, W., & Chen, Q. (2017) · Brain Research · doi:10.1016/j.brainres.2017.11.027 · Cited by 103 · see citing works

Dock4 is regulated by RhoG and promotes Rac-dependent cell migration

Hiramoto, K., Negishi, M., & Katoh, H. (2006) · Experimental Cell Research · doi:10.1016/j.yexcr.2006.09.006 · Cited by 92 · see citing works

Fucoxanthin, a Marine Xanthophyll Isolated From Conticribra weissflogii ND-8: Preventive Anti-Inflammatory Effect in a Mouse Model of Sepsis

Su, J., Guo, K., Huang, M., Liu, Y., Zhang, J., Sun, L., Li, D., Pang, K., Wang, G., Chen, L., et al. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00906 · Cited by 89 · see citing works

Cellular signaling of Dock family proteins in neural function

Miyamoto, Y., & Yamauchi, J. (2009) · Cellular Signalling · doi:10.1016/j.cellsig.2009.09.036 · Cited by 85 · see citing works

MOCA Induces Membrane Spreading by Activating Rac1

Namekata, K., Enokido, Y., Iwasawa, K., & Kimura, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311275200 · Cited by 84 · see citing works

Cell adhesion molecules contribute to Alzheimer’s disease: multiple pathway analyses of two genome‐wide association studies

Liu, G., Jiang, Y., Wang, P., Feng, R., Jiang, N., Chen, X., Song, H., & Chen, Z. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07547.x · Cited by 83 · see citing works

Dock protein family in brain development and neurological disease

Shi, L. (2013) · Communicative & Integrative Biology · doi:10.4161/cib.26839 · Cited by 83 · see citing works

Inhibition of APP Trafficking by Tau Protein Does Not Increase the Generation of Amyloid‐β Peptides

Goldsbury, C., Mocanu, M., Thies, E., Kaether, C., Haass, C., Keller, P., Biernat, J., Mandelkow, E., & Mandelkow, E. (2006) · Traffic · doi:10.1111/j.1600-0854.2006.00434.x · Cited by 82 · see citing works

Phosphorylation and activation of Bub1 on unattached chromosomes facilitate the spindle checkpoint

Chen, R. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600308 · Cited by 76 · see citing works

HtrA2 Regulates β-Amyloid Precursor Protein (APP) Metabolism through Endoplasmic Reticulum-associated Degradation

Huttunen, H. J., Guénette, S. Y., Peach, C., Greco, C., Xia, W., Kim, D. Y., Barren, C., Tanzi, R. E., & Kovacs, D. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702951200 · Cited by 72 · see citing works

Loss of Modifier of Cell Adhesion Reveals a Pathway Leading to Axonal Degeneration

Chen, Q., Peto, C. A., Shelton, G. D., Mizisin, A. P., Sawchenko, P. E., & Schubert, D. A. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.3985-08.2009 · Cited by 65 · see citing works

Alzheimer's disease meets the ubiquitin–proteasome system

Song, S., & Jung, Y. (2004) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2004.09.005 · Cited by 65 · see citing works

Dock4 regulates dendritic development in hippocampal neurons.

Ueda, S., Fujimoto, S., Hiramoto, K., Negishi, M., & Katoh, H. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21763 · Cited by 61 · see citing works

The Role of Presenilin and its Interacting Proteins in the Biogenesis of Alzheimer’s Beta Amyloid

Verdile, G., Gandy, S., & Martins, R. N. (2006) · Neurochemical Research · doi:10.1007/s11064-006-9131-x · Cited by 60 · see citing works

Dock GEFs and their therapeutic potential: Neuroprotection and axon regeneration

Namekata, K., Kimura, A., Kawamura, K., Harada, C., & Harada, T. (2014) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2014.06.005 · Cited by 57 · see citing works

Inhibition of acyl‐coenzyme A: cholesterol acyl transferase modulates amyloid precursor protein trafficking in the early secretory pathway

Huttunen, H. J., Peach, C., Bhattacharyya, R., Barren, C., Pettingell, W. H., Hutter‐Paier, B., Windisch, M., Berezovska, O., & Kovacs, D. M. (2009) · The FASEB Journal · doi:10.1096/fj.09-134999 · Cited by 56 · see citing works

Drosophila Polo regulates the spindle assembly checkpoint through Mps1‐dependent BubR1 phosphorylation

Conde, C., Osswald, M., Barbosa, J., Moutinho‐Santos, T., Pinheiro, D., Guimarães, S., Matos, I., Maiato, H., & Sunkel, C. E. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.109 · Cited by 50 · see citing works

Dock3 interaction with a glutamate-receptor NR2D subunit protects neurons from excitotoxicity

Bai, N., Hayashi, H., Aida, T., Namekata, K., Harada, T., Mishina, M., & Tanaka, K. (2013) · Molecular Brain · doi:10.1186/1756-6606-6-22 · Cited by 48 · see citing works

Modifier of Cell Adhesion Regulates N-Cadherin-Mediated Cell-Cell Adhesion and Neurite Outgrowth

Chen, Q., Chen, T., Letourneau, P. C., Costa, L. D. F., & Schubert, D. A. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3692-04.2005 · Cited by 47 · see citing works

The FAM3 superfamily member ILEI ameliorates Alzheimer’s disease-like pathology by destabilizing the penultimate amyloid-β precursor

Hasegawa, H., Liu, L., Tooyama, I., Murayama, S., & Nishimura, M. (2014) · Nature Communications · doi:10.1038/ncomms4917 · Cited by 47 · see citing works

Rho GTPases in neurodegeneration diseases

DeGeer, J., & Lamarche-Vane, N. (2013) · Experimental Cell Research · doi:10.1016/j.yexcr.2013.06.016 · Cited by 46 · see citing works

Regulation of dendrite growth by the Cdc42 activator Zizimin1/Dock9 in hippocampal neurons

Kuramoto, K., Negishi, M., & Katoh, H. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.21997 · Cited by 46 · see citing works

The emerging role of guanine nucleotide exchange factors in ALS and other neurodegenerative diseases

Droppelmann, C. A., Campos‐Melo, D., Volkening, K., & Strong, M. J. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00282 · Cited by 41 · see citing works

Multi-trait association studies discover pleiotropic loci between Alzheimer’s disease and cardiometabolic traits

Program, T. V. M. V., Bone, W. P., Siewert, K. M., Jha, A., Klarin, D., Damrauer, S. M., Chang, K.-M., Tsao, P. S., Assimes, T. L., Ritchie, M. D., et al. (2021) · Alzheimer's Research & Therapy · doi:10.1186/s13195-021-00773-z · Cited by 41 · see citing works

Regulating Rac in the Nervous System: Molecular Function and Disease Implication of Rac GEFs and GAPs

Bai, Y., Xiang, X., Liang, C., & Shi, L. (2015) · BioMed Research International · doi:10.1155/2015/632450 · Cited by 40 · see citing works

Proteasome-mediated effects on amyloid precursor protein processing at the γ-secretase site

Flood, F., MURPHY, S., Cowburn, R. F., Lannfelt, L., Walker, B., & Johnston, J. A. (2005) · Biochemical Journal · doi:10.1042/bj20041145 · Cited by 40 · see citing works

Physiological Control of Nitric Oxide in Neuronal BACE1 Translation by Heme-Regulated eIF2α Kinase HRI Induces Synaptogenesis

ILL‐Raga, G., Tajes, M., Busquets-García, A., Ramos‐Fernández, E., Vargas, L. M., Bosch-Morató, M., Guivernau, B., Valls-Comamala, V., Eraso‐Pichot, A., Guix, F. X., et al. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6080 · Cited by 36 · see citing works

The DOCK Protein Sponge Binds to ELMO and Functions in Drosophila Embryonic CNS Development

Biersmith, B. H., Liu, Z., Bauman, K., & Geisbrecht, E. R. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016120 · Cited by 28 · see citing works

RHO to the DOCK for GDP disembarking: Structural insights into the DOCK GTPase nucleotide exchange factors

Thompson, A. P., Bitsina, C., Gray, J. L., von Delft, F., & Brennan, P. E. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100521 · Cited by 21 · see citing works

MOCA is an integrator of the neuronal death signals that are activated by familial Alzheimer's disease-related mutants of amyloid β precursor protein and presenilins

Tachi, N., Hashimoto, Y., & Matsuoka, M. (2012) · Biochemical Journal · doi:10.1042/bj20100993 · Cited by 20 · see citing works

Dock3 Participate in Epileptogenesis Through rac1 Pathway in Animal Models

Li, J., Mi, X., Chen, L., Jiang, G., Wang, N., Zhang, Y., Deng, W., Wang, Z., Chen, G., & Wang, X. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9406-9 · Cited by 19 · see citing works

Reversing Synapse Loss in Alzheimer's Disease: Rho-Guanosine Triphosphatases and Insights from Other Brain Disorders

Lefort, R. (2015) · Neurotherapeutics · doi:10.1007/s13311-014-0328-4 · Cited by 17 · see citing works

Cell adhesion protein decreases cell motion: Statistical characterization of locomotion activity

Diambra, L. A., Cintra, L. C., Chen, Q., Schubert, D., & Costa, L. D. F. (2005) · Physica A Statistical Mechanics and its Applications · doi:10.1016/j.physa.2005.10.006 · Cited by 16 · see citing works

The relationship between DNA methylation andReprimogene expression in gastric cancer cells

Lai, J., Wang, H., Luo, Q., Huang, S., Lin, S., Zheng, Y., & Chen, Q. (2017) · Oncotarget · doi:10.18632/oncotarget.21296 · Cited by 15 · see citing works

EDEM1 Regulates Amyloid Precursor Protein (APP) Metabolism and Amyloid-β Production

Nowakowska-Gołacka, J., Czapiewska, J., Sominka, H., Sowa-Rogozińska, N., & Słomińska-Wojewódzka, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010117 · Cited by 14 · see citing works

BACE1 Translation: At the Crossroads Between Alzheimer’s Disease Neurodegeneration and Memory Consolidation

Guix, F. X., Sartório, C. L., & ILL‐Raga, G. (2019) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-180089 · Cited by 13 · see citing works

Reduced amyloidogenic processing of the amyloid β-protein precursor by the small-molecule Differentiation Inducing Factor-1

Myre, M. A., Washicosky, K. J., Moir, R. D., Tesco, G., Tanzi, R. E., & Wasco, W. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2008.12.008 · Cited by 13 · see citing works

Effect of cell density on intracellular levels of the Alzheimer's amyloid precursor protein

Rebelo, S., Henriques, A. G., Silva, E. F. D. C. E., & Silva, O. A. B. D. C. E. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20091 · Cited by 13 · see citing works

An arrayed genome‐wide perturbation screen identifies the ribonucleoprotein Hnrnpk as rate‐limiting for prion propagation

Avar, M., Heinzer, D., Thackray, A. M., Liu, Y., Hruška-Plocháň, M., Sellitto, S., Schaper, E., Pease, D., Yin, J., Lakkaraju, A. K., et al. (2022) · The EMBO Journal · doi:10.15252/embj.2022112338 · Cited by 12 · see citing works

Redox Pioneer: Professor Hideo Kimura

Lefer, D. J. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7618 · Cited by 12 · see citing works

Neuroprotection and axon regeneration by novel low-molecular-weight compounds through the modification of DOCK3 conformation

Namekata, K., Tsuji, N., Guo, X., Nishijima, E., Honda, S., Kitamura, Y., Yamasaki, A., Kishida, M., Takeyama, J., Ishikawa, H., et al. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01460-8 · Cited by 8 · see citing works

Targeted ErbB4 receptor activation ameliorates neuronal deficits via DOCK3 signaling in a transgenic mouse AD model

Liu, C., Zhao, Y., Dao, J.-J., Zhang, W., Liu, J., Ma, Y.-K., Qiao, C.-M., Cui, C., Chen, S., Shen, Y., et al. (2025) · Neurotherapeutics · doi:10.1016/j.neurot.2025.e00739 · Cited by 5 · see citing works

Activation of GTPases by Dock180 Family of Proteins

Lu, M., & Ravichandran, K. S. (2005) · Springer eBooks · doi:10.1007/1-4020-3462-8_4 · Cited by 2 · see citing works

FAM3C in Alzheimer's disease

Nishimura, M., Watanabe, N., Hibino, E., Nakano, M., Mitsuishi, Y., Liu, L., & Sugi, T. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-815868-5.00019-0 · Cited by 1 · see citing works

Optic Nerve Regeneration

Namekata, K. (2014) · Springer eBooks · doi:10.1007/978-4-431-54965-9_23 · Cited by 1 · see citing works

Atypical Guanine Nucleotide Exchange Factors for Rho Family GTPases: DOCK9 Activation of Cdc42 and SmgGDS activation of RhoA

Hamel, B. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/kmq6-qg97 · Cited by 1 · see citing works

Whole Exome Analysis of Early Onset Alzheimer's Disease

Pericak‐Vance, M. A. (2013) · doi:10.21236/ada602412

Non-Maxwellian velocity distribution and anomalous diffusion of {\it in vitro} kidney cellsPreprint

Diambra, L. A., Cintra, L. C., Schubert, D., & Costa, L. D. F. (2005) · arXiv (Cornell University) · doi:10.48550/arxiv.q-bio/0503013

The Dock Family of Atypical Guanine Nucleotide Exchange Factors: Regulation by ELMO1 and RhoG

Holley, C. P. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/m95n-qm88

Die Funktionsanalyse und Pharmakomodulation des Amyloid-Vorläufer-Proteins (APP) in vitro und in vivo - Eine neue Zielstruktur zur Behandlung maligner Tumore

Venkataramani, V. (2012) · doi:10.53846/goediss-1184

Ubiquitin and Intracellular Aggregation

Song, S., & Jung, Y. (2003) · Springer eBooks · doi:10.1007/978-1-4757-5890-0_16

Additional file 1 of Multi-trait association studies discover pleiotropic loci between Alzheimer’s disease and cardiometabolic traits

Bone, W. P., Siewert, K. M., Jha, A., Klarin, D. M., Damrauer, S. M., Chang, K.-M., Tsao, P. S., Assimes, T. L., Ritchie, M. D., & Voight, B. F. (2021) · Figshare · doi:10.6084/m9.figshare.13719193

Dérégulation de l’homéostasie calcique du réticulum endoplasmique dans la maladie d’Alzheimer : rôle du récepteur de la ryanodine et de l’isoforme SERCA1 tronquée

Bussiere, R. (2018) · theses.fr (ABES) · doi:10.70675/2334ca11z42bfz4e8bza53bz02e8bbacc38e

MOCA is an integrator of the neuronal death signals that are activated by familial Alzheimer's disease-related mutants of amyloid β precursor protein and presenilins

Tachi, N., Hashimoto, Y., & Matsuoka, M. (2012) · Biochemical Journal · doi:10.1042/bj20100993 · Cited by 20 · see citing works

Exploring the Regulatory Role of Cellular Prion Protein (PrPC) in Amyloid Precursor Protein (APP) Processing and Trafficking: Implications for Alzheimer's Disease Therapeutics

Mehta, N. A. (2024) · Knowledge@UChicago (University of Chicago) · doi:10.6082/gdvbm-5z962

The regulation of amyloid β protein precursor secretion and its modulatory role in cell adhesion

Schubert, D. A., Jin, L.-W., Saitch, T., & Cole, G. J. (1990) · Alzheimer Disease & Associated Disorders · doi:10.1097/00002093-199004020-00006 · Cited by 1 · see citing works

Exploring the Regulatory Role of Cellular Prion Protein (PrPC) in Amyloid Precursor Protein Trafficking and Processing: Implications for Alzheimer’s Disease Therapeutics

Mehta, N. A. (2024) · University of Chicago · doi:10.6082/uchicago.11936

Novel modulators of amyloid‐β precursor protein processing

Tang, B. L., & Liou, Y. C. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04215.x · Cited by 57 · see citing works