Protein Quality Control as a Strategy for Cellular Regulation: Lessons from Ubiquitin-Mediated Regulation of the Sterol Pathway

Targeting of HIF-α to the von Hippel-Lindau Ubiquitylation Complex by O ₂ -Regulated Prolyl Hydroxylation

Jaakkola, P., Mole, D. R., Tian, Y.-M., Wilson, M. I., Gielbert, J., Gaskell, S. J., Kriegsheim, A. V., Hebestreit, H. F., Mukherji, M., Schofield, C. J., et al. (2001) · Science · doi:10.1126/science.1059796 · Cited by 5,535 · see citing works

Regulation of the mevalonate pathway

Goldstein, J. L., & Brown, M. S. (1990) · Nature · doi:10.1038/343425a0 · Cited by 5,394 · see citing works

Lipopolysaccharide endotoxins

Raetz, C. R. H., & Whitfield, C. (2002) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.71.110601.135414 · Cited by 4,404 · see citing works

Functional and Genomic Analyses Reveal an Essential Coordination between the Unfolded Protein Response and ER-Associated Degradation

Travers, K. J., Patil, C. K., Wodicka, L. M., Lockhart, D. J., Weissman, J. S., & Walter, P. (2000) · Cell · doi:10.1016/s0092-8674(00)80835-1 · Cited by 1,994 · see citing works

Mechanism of auxin perception by the TIR1 ubiquitin ligase

Tan, X., Calderon-Villalobos, L. I. A., Sharon, M., Zheng, C., Robinson, C. V., Estelle, M., & Zheng, N. (2007) · Nature · doi:10.1038/nature05731 · Cited by 1,688 · see citing works

Protein Sensors for Membrane Sterols

Goldstein, J. L., DeBose‐Boyd, R. A., & Brown, M. S. (2006) · Cell · doi:10.1016/j.cell.2005.12.022 · Cited by 1,685 · see citing works

Degradation of CFTR by the ubiquitin-proteasome pathway

Ward, C. L., ŌMURA, S., & Kopito, R. R. (1995) · Cell · doi:10.1016/0092-8674(95)90240-6 · Cited by 1,308 · see citing works

The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol

Ye, Y., Meyer, H. H., & Rapoport, T. A. (2001) · Nature · doi:10.1038/414652a · Cited by 1,099 · see citing works

Mdm2 Is a RING Finger-dependent Ubiquitin Protein Ligase for Itself and p53

Fang, S., Jensen, J. P., Ludwig, R. L., Vousden, K. H., & Weissman, A. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.8945 · Cited by 1,044 · see citing works

A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol

Ye, Y., Shibata, Y., Yun, C., Ron, D., & Rapoport, T. A. (2004) · Nature · doi:10.1038/nature02656 · Cited by 963 · see citing works

Opposing activities protect against age-onset proteotoxicity

Cohen, E., Bieschke, J., Perciavalle, R. M., Kelly, J. W., & Dillin, A. (2006) · Science · doi:10.1126/science.1124646 · Cited by 843 · see citing works

The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation

Meacham, G. C., Patterson, C., Zhang, W., Younger, J. M., & Cyr, D. (2000) · Nature Cell Biology · doi:10.1038/35050509 · Cited by 839 · see citing works

Protein Prenyltransferases

Casey, P. J., & Seabra, M. C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.10.5289 · Cited by 716 · see citing works

ER Degradation of a Misfolded Luminal Protein by the Cytosolic Ubiquitin-Proteasome Pathway

Hiller, M. M., Finger, A., Schweiger, M. W., & Wolf, D. H. (1996) · Science · doi:10.1126/science.273.5282.1725 · Cited by 708 · see citing works

Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein.

Hampton, R. Y., Gardner, R. G., & Rine, J. (1996) · Molecular Biology of the Cell · doi:10.1091/mbc.7.12.2029 · Cited by 586 · see citing works

A Series of Ubiquitin Binding Factors Connects CDC48/p97 to Substrate Multiubiquitylation and Proteasomal Targeting

Richly, H., Rapé, M., Braun, S. J., Rumpf, S., Hoege, C., & Jentsch, S. (2005) · Cell · doi:10.1016/j.cell.2004.11.013 · Cited by 523 · see citing works

Structural Basis for Phosphodependent Substrate Selection and Orientation by the SCFCdc4 Ubiquitin Ligase

Orlicky, S. M., Tang, X., Willems, A. R., Tyers, M., & Sicheri, F. (2003) · Cell · doi:10.1016/s0092-8674(03)00034-5 · Cited by 510 · see citing works

Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins.

Ward, C. L., & Kopito, R. R. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47306-1 · Cited by 495 · see citing works

Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation

Bays, N. W., Gardner, R. G., Seelig, L. P., Joazeiro, C. A. P., & Hampton, R. Y. (2000) · Nature Cell Biology · doi:10.1038/35050524 · Cited by 465 · see citing works

A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matα2 repressor degradationPreprint

Swanson, R. J., Locher, M., & Hochstrasser, M. (2001) · Genes & Development · doi:10.1101/gad.933301 · Cited by 456 · see citing works

Sequential Quality-Control Checkpoints Triage Misfolded Cystic Fibrosis Transmembrane Conductance Regulator

Younger, J. M., Chen, L., Ren, H.-Y., Rosser, M. F. N., Turnbull, E. L., Fan, C., Patterson, C., & Cyr, D. (2006) · Cell · doi:10.1016/j.cell.2006.06.041 · Cited by 440 · see citing works

CELLULAR FUNCTIONS, MECHANISM OF ACTION, AND REGULATION OF FTSH PROTEASE

Ito, K., & Akiyama, Y. (2005) · Annual Review of Microbiology · doi:10.1146/annurev.micro.59.030804.121316 · Cited by 438 · see citing works

Development of Protacs to Target Cancer-promoting Proteins for Ubiquitination and Degradation

Sakamoto, K. M., Kim, K. B., Verma, R., Ransick, A., Stein, B., Crews, C. M., & Deshaies, R. J. (2003) · Molecular & Cellular Proteomics · doi:10.1074/mcp.t300009-mcp200 · Cited by 425 · see citing works

The 3-hydroxy-3-methylglutaryl coenzyme-A (HMG-CoA) reductases.

Friesen, J. A., & Rodwell, V. W. (2004) · Genome biology · doi:10.1186/gb-2004-5-11-248 · Cited by 409 · see citing works

Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast.

Knop, M., Finger, A. C., Braun, T., Hellmuth, K., & Wolf, D. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00411.x · Cited by 388 · see citing works

Rad23 and Rpn10 Serve as Alternative Ubiquitin Receptors for the Proteasome

Elsasser, S., Chandler-Militello, D., Mueller, B., Hanna, J. W., & Finley, D. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404020200 · Cited by 349 · see citing works

Polar residues drive association of polyleucine transmembrane helices

Zhou, F. X., Merianos, H. J., Brünger, A. T., & Engelman, D. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.041593698 · Cited by 344 · see citing works

Direct Binding of Cholesterol to the Purified Membrane Region of SCAP

Radhakrishnan, A., Sun, L.-P., Kwon, H. J., Brown, M. S., & Goldstein, J. L. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.06.019 · Cited by 333 · see citing works

The Unfolded Protein Response Regulates Multiple Aspects of Secretory and Membrane Protein Biogenesis and Endoplasmic Reticulum Quality Control

Ng, D., Spear, E. D., & Walter, P. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.1.77 · Cited by 333 · see citing works

Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane

Lilley, B. N., & Ploegh, H. L. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505014102 · Cited by 315 · see citing works

Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation

Schuberth, C. E., & Buchberger, A. (2005) · Nature Cell Biology · doi:10.1038/ncb1299 · Cited by 314 · see citing works

Insig-dependent Ubiquitination and Degradation of Mammalian 3-Hydroxy-3-methylglutaryl-CoA Reductase Stimulated by Sterols and Geranylgeraniol

Sever, N., Song, B., Yabe, D., Goldstein, J. L., Brown, M. S., & DeBose‐Boyd, R. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m310053200 · Cited by 305 · see citing works

Ubx2 links the Cdc48 complex to ER-associated protein degradation

Neuber, O., Jarosch, E., Volkwein, C., Walter, J., & Sommer, T. (2005) · Nature Cell Biology · doi:10.1038/ncb1298 · Cited by 300 · see citing works

A lipid-based model for the creation of an escape hatch from the endoplasmic reticulum

Ploegh, H. L. (2007) · Nature · doi:10.1038/nature06004 · Cited by 286 · see citing works

Pharmacological chaperones: potential treatment for conformational diseases

Bernier, V., Lagacé, M., Bichet, D. G., & Bouvier, M. (2004) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2004.05.003 · Cited by 285 · see citing works

Insig-mediated degradation of HMG CoA reductase stimulated by lanosterol, an intermediate in the synthesis of cholesterol

Song, B., Javitt, N. B., & DeBose‐Boyd, R. A. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.01.001 · Cited by 283 · see citing works

Degradation-Mediated Protein Quality Control in the Nucleus

Gardner, R. G., Nelson, Z. W., & Gottschling, D. E. (2005) · Cell · doi:10.1016/j.cell.2005.01.016 · Cited by 280 · see citing works

Induction of Rat Hepatic N-Nitrosodimethylamine Demethylase by Acetone Is Due to Protein Stabilization

Song, B. J., Veech, R. L., Park, S. S., Gelboin, H. V., & Gonzalez, F. J. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94103-7 · Cited by 277 · see citing works

Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli

Ogura, T., Inoue, K., Tatsuta, T., Suzaki, T., Karata, K., Young, K., Su, L. J., Fierke, C. A., Jackman, J. E., Raetz, C. R. H., et al. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01221.x · Cited by 265 · see citing works

Mitosis: a matter of getting rid of the right protein at the right time

Pines, J. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2005.11.006 · Cited by 262 · see citing works

Ligands act as pharmacological chaperones and increase the efficiency of δ opioid receptor maturation

Petäjä‐Repo, U. E., Hogue, M., Bhalla, S. S., Laperrière, A., Morello, J.-P., & Bouvier, M. (2002) · The EMBO Journal · doi:10.1093/emboj/21.7.1628 · Cited by 262 · see citing works

Folding and Quality Control of the VHL Tumor Suppressor Proceed through Distinct Chaperone Pathways

McClellan, A. J., Scott, M. D., & Frydman, J. (2005) · Cell · doi:10.1016/j.cell.2005.03.024 · Cited by 260 · see citing works

Motifs of serine and threonine can drive association of transmembrane helices

Dawson, J. P., Weinger, J. S., & Engelman, D. M. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5353 · Cited by 249 · see citing works

Pharmacologic Chaperones as a Potential Treatment for X-Linked Nephrogenic Diabetes Insipidus

Bernier, V., Morello, J.-P., ZARRUK, A. R., Debrand, N., Salahpour, A., Lonergan, M., Arthus, M., Laperrière, A., Brouard, R., Bouvier, M., et al. (2005) · Journal of the American Society of Nephrology · doi:10.1681/asn.2005080854 · Cited by 244 · see citing works

Exploration of the Topological Requirements of ERAD Identifies Yos9p as a Lectin Sensor of Misfolded Glycoproteins in the ER Lumen

Bhamidipati, A., Denic, V., Toyama, E. Q., & Weissman, J. S. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.07.027 · Cited by 234 · see citing works

A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery

Gauss, R., Jarosch, E., Sommer, T., & Hirsch, C. (2006) · Nature Cell Biology · doi:10.1038/ncb1445 · Cited by 231 · see citing works

Characterization of an ERAD Pathway for Nonglycosylated BiP Substrates, which Require Herp

Okuda-Shimizu, Y., & Hendershot, L. M. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.09.012 · Cited by 215 · see citing works

The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site

Chen, B., Mariano, J. M., Tsai, Y. C., Chan, A. H., Cohen, M. M., & Weissman, A. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506618103 · Cited by 213 · see citing works

Degradation Signal Masking by Heterodimerization of MATα2 and MATa1 Blocks Their Mutual Destruction by the Ubiquitin-Proteasome Pathway

Johnson, P. R., Swanson, R. J., Rakhilina, L., & Hochstrasser, M. (1998) · Cell · doi:10.1016/s0092-8674(00)81421-x · Cited by 196 · see citing works

The SREBP Pathway in Drosophila

Seegmiller, A. C., Dobrosotskaya, I., Goldstein, J. L., Ho, Y. K., Brown, M. S., & Rawson, R. B. (2002) · Developmental Cell · doi:10.1016/s1534-5807(01)00119-8 · Cited by 194 · see citing works

Degradation of proteins within the endoplasmic reticulum

Bonifacio, J. S., & Lippincott‐Schwartz, J. (1991) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(91)90028-w · Cited by 193 · see citing works

Yos9p Detects and Targets Misfolded Glycoproteins for ER-Associated Degradation

Kim, W., Spear, E. D., & Ng, D. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.08.010 · Cited by 191 · see citing works

Cod1p/Spf1p is a P-type ATPase involved in ER function and Ca2+ homeostasis

Cronin, S. R., Rao, R., & Hampton, R. Y. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200203052 · Cited by 170 · see citing works

Catabolite Degradation of Fructose-1,6-bisphosphatase in the YeastSaccharomyces cerevisiae: A Genome-wide Screen Identifies Eight NovelGIDGenes and Indicates the Existence of Two Degradation Pathways

Regelmann, J., Schüle, T., Josupeit, F. S., Horak, J., Rose, M., Entian, K., Thumm, M., & Wolf, D. H. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-08-0456 · Cited by 159 · see citing works

A Highly Conserved Signal Controls Degradation of 3-Hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) Reductase in Eukaryotes

Gardner, R. G., & Hampton, R. Y. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.44.31671 · Cited by 156 · see citing works

Structural and Functional Conservation Between Yeast and Human 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductases, the Rate-Limiting Enzyme of Sterol Biosynthesis

Basson, M. E., Thorsness, M. K., Finer-Moore, J. S., Stroud, R. M., & Rine, J. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.9.3797 · Cited by 156 · see citing works

Functional Rescue of the Constitutively Internalized V2 Vasopressin Receptor Mutant R137H by the Pharmacological Chaperone Action of SR49059

Bernier, V., Lagacé, M., Lonergan, M., Arthus, M., Bichet, D. G., & Bouvier, M. (2004) · Molecular Endocrinology · doi:10.1210/me.2004-0080 · Cited by 154 · see citing works

Real-Time Fluorescence Detection of ERAD Substrate Retrotranslocation in a Mammalian In Vitro System

Wahlman, J., Demartino, G., Skach, W. R., Bulleid, N. J., Brodsky, J. L., & Johnson, A. E. (2007) · Cell · doi:10.1016/j.cell.2007.03.046 · Cited by 136 · see citing works

Pharmacological chaperone action on G-protein-coupled receptors

Bernier, V., Bichet, D. G., & Bouvier, M. (2004) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2004.08.001 · Cited by 130 · see citing works

The Role of a Novel p97/Valosin-containing Protein-interacting Motif of gp78 in Endoplasmic Reticulum-associated Degradation

Ballar, P., Shen, Y., Yang, H., & Fang, S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603355200 · Cited by 129 · see citing works

HPV E6, E6AP and cervical cancer

Beaudenon, S. L., & Huibregtse, J. M. (2008) · BMC Biochemistry · doi:10.1186/1471-2091-9-s1-s4 · Cited by 126 · see citing works

In Vivo Action of the HRD Ubiquitin Ligase Complex: Mechanisms of Endoplasmic Reticulum Quality Control and Sterol Regulation

Gardner, R. G., Shearer, A. G., & Hampton, R. Y. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.13.4276-4291.2001 · Cited by 116 · see citing works

The Ubiquitin System: From Basic Mechanisms to the Patient Bed

Ciechanover, A. J., & Iwaï, K. (2004) · IUBMB Life · doi:10.1080/1521654042000223616 · Cited by 115 · see citing works

The C‐terminal end of LpxC is required for degradation by the FtsH protease

Führer, F., Schäkermann, S., & Narberhaus, F. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04994.x · Cited by 110 · see citing works

Single, context-specific glycans can target misfolded glycoproteins for ER-associated degradation

Spear, E. D., & Ng, D. T. W. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200411136 · Cited by 110 · see citing works

Regulation of Hmg-Coa Reductase Degradation Requires the P-Type Atpase Cod1p/Spf1p

Cronin, S. R., Khoury, A., Ferry, D. K., & Hampton, R. Y. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.5.915 · Cited by 110 · see citing works

SPFH2 Mediates the Endoplasmic Reticulum-associated Degradation of Inositol 1,4,5-Trisphosphate Receptors and Other Substrates in Mammalian Cells

Pearce, M. M. P., Wang, Y., Kelley, G. G., & Wojcikiewicz, R. J. H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701862200 · Cited by 107 · see citing works

Proteolysis and Sterol Regulation

Hampton, R. Y. (2002) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.18.032002.131219 · Cited by 104 · see citing works

Regulation of UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine Deacetylase in Escherichia coli

Sorensen, P. G., Lutkenhaus, J., Young, K., Eveland, S. S., Anderson, M. S., & Raetz, C. R. H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.42.25898 · Cited by 94 · see citing works

Common and specific mechanisms of AAA+ proteins involved in protein quality control

Mogk, A., Haslberger, T., Tessarz, P., & Bukau, B. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360120 · Cited by 86 · see citing works

Yeast Derlin Dfm1 interacts with Cdc48 and functions in ER homeostasis

Sato, B. K., & Hampton, R. Y. (2006) · Yeast · doi:10.1002/yea.1407 · Cited by 82 · see citing works

A ‘distributed degron’ allows regulated entry into the ER degradation pathway

Gardner, R. G., & Hampton, R. Y. (1999) · The EMBO Journal · doi:10.1093/emboj/18.21.5994 · Cited by 79 · see citing works

Lipid‐mediated, reversible misfolding of a sterol‐sensing domain protein

Shearer, A. G., & Hampton, R. Y. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600498 · Cited by 71 · see citing works

INSIG: a broadly conserved transmembrane chaperone for sterol‐sensing domain proteins

Flury, I., Garza, R. M., Shearer, A. G., Rosen, J., Cronin, S. R., & Hampton, R. Y. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600855 · Cited by 70 · see citing works

Cue1p Is an Activator of Ubc7p E2 Activity in Vitro and in Vivo

Bazirgan, O. A., & Hampton, R. Y. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801122200 · Cited by 66 · see citing works

Yeast Genes Controlling Responses to Topogenic Signals in a Model Transmembrane Protein

Tipper, D. J., & Harley, C. A. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-10-0488 · Cited by 63 · see citing works

Proteolysis in prokaryotes: protein quality control and regulatory principles

Hengge, R., & Bukau, B. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03693.x · Cited by 62 · see citing works

A RING‐H2 finger motif is essential for the function of Der3/Hrd1 in endoplasmic reticulum associated protein degradation in the yeast Saccharomyces cerevisiae

Bordallo, J., & Wolf, D. H. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00362-2 · Cited by 57 · see citing works

Vpu-Mediated Degradation of CD4 Reconstituted in Yeast Reveals Mechanistic Differences to Cellular ER-Associated Protein Degradation

Meusser, B., & Sommer, T. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00212-6 · Cited by 56 · see citing works

Structural Control of Endoplasmic Reticulum-associated Degradation

Shearer, A. G., & Hampton, R. Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307734200 · Cited by 51 · see citing works

Regulation of Cytochrome P450 2E1 by Heat Shock Protein 90-Dependent Stabilization and CHIP-Dependent Proteasomal Degradation

Morishima, Y., Peng, H., Lin, H.-L., Hollenberg, P. F., Sunahara, R. K., Osawa, Y., & Pratt, W. B. (2005) · Biochemistry · doi:10.1021/bi0515570 · Cited by 51 · see citing works

Involvement of the p97-Ufd1-Npl4 Complex in the Regulated Endoplasmic Reticulum-associated Degradation of Inositol 1,4,5-Trisphosphate Receptors

Alzayady, K. J., Panning, M. M., Kelley, G. G., & Richard Wojcikiewicz, J. H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508890200 · Cited by 47 · see citing works

Characterization of the Physiological Turnover of Native and Inactivated Cytochromes P450 3A in Cultured Rat Hepatocytes: A Role for the Cytosolic AAA ATPase p97?

Faouzi, S., Medzihradszky, K. F., Hefner, C. A., Maher, J. J., & Correia, M. A. (2007) · Biochemistry · doi:10.1021/bi700340n · Cited by 34 · see citing works

Ligand binding directly stimulates ubiquitination of the inositol 1,4,5-trisphosphate receptor

Zhu, C.-C., & Wojcikiewicz, R. J. H. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3480551 · Cited by 33 · see citing works

Mass spectrometry advances in lipidomica: collision-induced decomposition of Kdo2–lipid A

Murphy, R. C., Raetz, C. R. H., Reynolds, C. M., & Barkley, R. M. (2004) · Prostaglandins & Other Lipid Mediators · doi:10.1016/j.prostaglandins.2004.09.004 · Cited by 33 · see citing works

Endoplasmic Reticulum-Associated Degradation of Cytochrome P450 CYP3A4 in Saccharomyces cerevisiae: Further Characterization of Cellular Participants and Structural Determinants

Liao, M., Faouzi, S., Karyakin, A., & Correia, M. A. (2006) · Molecular Pharmacology · doi:10.1124/mol.105.021816 · Cited by 30 · see citing works

Mass Spectrometric Analysis of Type 1 Inositol 1,4,5-Trisphosphate Receptor Ubiquitination

Sliter, D. A., Kubota, K., Kirkpatrick, D. S., Alzayady, K. J., Gygi, S. P., & Wojcikiewicz, R. J. H. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807288200 · Cited by 27 · see citing works

Protein Secretion and Membrane Insertion Systems in Bacteria and Eukaryotic Organelles

Saier, M. H., Hong, C., Rodgers, L., Tamang, D. G., & Yen, M. R. (2008) · Advances in applied microbiology · doi:10.1016/s0065-2164(08)00606-0 · Cited by 24 · see citing works

The N‐end rule pathway and regulation by proteolysis

Varshavsky, A. J. (2011) · Protein Science · doi:10.1002/pro.666 · Cited by 696 · see citing works

Orm family proteins mediate sphingolipid homeostasis

Breslow, D. K., Collins, S. R., Bodenmiller, B., Aebersold, R. H., Simons, K., Shevchenko, A., Ejsing, C. S., & Weissman, J. S. (2010) · Nature · doi:10.1038/nature08787 · Cited by 599 · see citing works

Regulation of HMG-CoA reductase in mammals and yeast

Burg, J. S., & Espenshade, P. J. (2011) · Progress in Lipid Research · doi:10.1016/j.plipres.2011.07.002 · Cited by 303 · see citing works

The Ubiquitin System, an Immense Realm

Varshavsky, A. J. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-051910-094049 · Cited by 278 · see citing works

Protein folding and quality control in the endoplasmic reticulum: Recent lessons from yeast and mammalian cell systems

Brodsky, J. L., & Skach, W. R. (2011) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2011.05.004 · Cited by 242 · see citing works

Misfolded Membrane Proteins Are Specifically Recognized by the Transmembrane Domain of the Hrd1p Ubiquitin Ligase

Sato, B. K., Schulz, D., Do, P. H., & Hampton, R. Y. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.03.010 · Cited by 212 · see citing works

An endoplasmic reticulum-engineered yeast platform for overproduction of triterpenoids

Arendt, P., Miettinen, K., Pollier, J., Rycke, R. M. D., Callewaert, N., & Goossens, A. (2017) · Metabolic Engineering · doi:10.1016/j.ymben.2017.02.007 · Cited by 186 · see citing works

Control of cholesterol synthesis through regulated ER-associated degradation of HMG CoA reductase

Jo, Y., & DeBose‐Boyd, R. A. (2010) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2010.485605 · Cited by 165 · see citing works

Quality and quantity control at the endoplasmic reticulum

Hegde, R. S., & Ploegh, H. L. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.05.005 · Cited by 157 · see citing works

Finding the will and the way of ERAD substrate retrotranslocation

Hampton, R. Y., & Sommer, T. (2012) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2012.05.010 · Cited by 133 · see citing works

Protein Quality Control of the Endoplasmic Reticulum and Ubiquitin–Proteasome-Triggered Degradation of Aberrant Proteins: Yeast Pioneers the Path

Berner, N., Reutter, K., & Wolf, D. H. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062917-012749 · Cited by 125 · see citing works

The protein quality control system manages plant defence compound synthesis

Pollier, J., Moses, T., González‐Guzmán, M., Geyter, N. D., Lippens, S., Bossche, R. V., Marhavý, P., Kremer, A., Morreel, K., Guérin, C. J., et al. (2013) · Nature · doi:10.1038/nature12685 · Cited by 116 · see citing works

Signal peptide peptidase functions in ERAD to cleave the unfolded protein response regulator XBP1u

Chen, C., Malchus, N. S., Hehn, B., Stelzer, W., Avci, D., Langosch, D., & Lemberg, M. K. (2014) · The EMBO Journal · doi:10.15252/embj.201488208 · Cited by 115 · see citing works

The GARP complex is required for cellular sphingolipid homeostasis

Fröhlich, F., Petit, C. S. V., Kory, N., Christiano, R., Hannibal‐Bach, H. K., Graham, M. M., Liu, X., Ejsing, C. S., Farese, R. V., & Walther, T. C. (2015) · eLife · doi:10.7554/elife.08712 · Cited by 105 · see citing works

RNF170 Protein, an Endoplasmic Reticulum Membrane Ubiquitin Ligase, Mediates Inositol 1,4,5-Trisphosphate Receptor Ubiquitination and Degradation

Lu, J. P., Wang, Y., Sliter, D. A., Pearce, M. M. P., & Wojcikiewicz, R. J. H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.251983 · Cited by 102 · see citing works

The Dfm1 Derlin Is Required for ERAD Retrotranslocation of Integral Membrane Proteins

Neal, S. E., Jaeger, P. A., Duttke, S. H. C., Benner, C. W., Glass, C. K., Ideker, T. E., & Hampton, R. Y. (2018) · Molecular Cell · doi:10.1016/j.molcel.2017.12.012 · Cited by 100 · see citing works

Membrane-associated Ubiquitin Ligase Complex Containing gp78 Mediates Sterol-accelerated Degradation of 3-Hydroxy-3-methylglutaryl-coenzyme A Reductase

Jo, Y., Sguigna, P. V., & DeBose‐Boyd, R. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.211326 · Cited by 93 · see citing works

Biocommunication of Fungi

Palková, Z., & Váchová, L. (. (2012) · Springer eBooks · doi:10.1007/978-94-007-4264-2 · Cited by 92 · see citing works

Yeast SREBP Cleavage Activation Requires the Golgi Dsc E3 Ligase Complex

Stewart, E. V., Nwosu, C. C., Tong, Z., Roguev, A., Cummins, T. D., Kim, D.-U., Hayles, J., Park, H.-O., Hoe, K., Powell, D. W., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.02.035 · Cited by 91 · see citing works

Clipping or Extracting: Two Ways to Membrane Protein Degradation

Avci, D., & Lemberg, M. K. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.07.003 · Cited by 86 · see citing works

Substrate-specific mediators of ER associated degradation (ERAD)

Brodsky, J. L., & Wojcikiewicz, R. J. H. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.04.006 · Cited by 82 · see citing works

E3 Ubiquitin Ligases Neurobiological Mechanisms: Development to Degeneration

Upadhyay, A., Joshi, V., Amanullah, A., Mishra, R., Arora, N., Prasad, A., & Mishra, A. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00151 · Cited by 79 · see citing works

Ancient ubiquitous protein-1 mediates sterol-induced ubiquitination of 3-hydroxy-3-methylglutaryl CoA reductase in lipid droplet–associated endoplasmic reticulum membranes

Jo, Y., Hartman, I. Z., & DeBose‐Boyd, R. A. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-07-0564 · Cited by 77 · see citing works

DEVELOPING A YEAST CELL FACTORY FOR THE PRODUCTION OF TERPENOIDS

Kampranis, S. C., & Makris, A. M. (2012) · Computational and Structural Biotechnology Journal · doi:10.5936/csbj.201210006 · Cited by 72 · see citing works

Direct and essential function for Hrd3 in ER-associated degradation

Vashistha, N., Neal, S. E., Singh, A., Carroll, S. M., & Hampton, R. Y. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1603079113 · Cited by 70 · see citing works

Geranylgeranyl Pyrophosphate Is a Potent Regulator of HRD-dependent 3-Hydroxy-3-methylglutaryl-CoA Reductase Degradation in Yeast

Garza, R. M., Tran, P. N., & Hampton, R. Y. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.023994 · Cited by 69 · see citing works

Usa1p Is Required for Optimal Function and Regulation of the Hrd1p Endoplasmic Reticulum-associated Degradation Ubiquitin Ligase

Carroll, S. M., & Hampton, R. Y. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.067876 · Cited by 69 · see citing works

Positive genetic interactors of HMG2 identify a new set of genetic perturbations for improving sesquiterpene production in Saccharomyces cerevisiae

Ignea, C., Trikka, F. A., Kourtzelis, I., Argiriou, A., Kanellis, A. K., Kampranis, S. C., & Makris, A. M. (2012) · Microbial Cell Factories · doi:10.1186/1475-2859-11-162 · Cited by 60 · see citing works

Specificity and Regulation of the Endoplasmic Reticulum‐Associated Degradation Machinery

Merulla, J., Fasana, E., Soldà, T., & Molinari, M. (2013) · Traffic · doi:10.1111/tra.12068 · Cited by 59 · see citing works

Maternal low-protein diet causes epigenetic deregulation of HMGCR and CYP7α1 in the liver of weaning piglets

Cong, R., Jia, Y., Li, R., Ni, Y., Yang, X., Sun, Q., Parvizi, N., & Zhao, R. (2012) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2011.11.007 · Cited by 60 · see citing works

When worlds collide: IP3 receptors and the ERAD pathway

Wojcikiewicz, R. J. H., Pearce, M. M. P., Sliter, D. A., & Wang, Y. (2009) · Cell Calcium · doi:10.1016/j.ceca.2009.05.002 · Cited by 54 · see citing works

N-terminal acetylation of the yeast Derlin Der1 is essential for Hrd1 ubiquitin-ligase activity toward luminal ER substrates

Zattas, D., Adle, D. J., Rubenstein, E. M., & Hochstrasser, M. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-11-0838 · Cited by 50 · see citing works

The Sterol-sensing Domain (SSD) Directly Mediates Signal-regulated Endoplasmic Reticulum-associated Degradation (ERAD) of 3-Hydroxy-3-methylglutaryl (HMG)-CoA Reductase Isozyme Hmg2

Theesfeld, C. L., Pourmand, D., Davis, T. C., Garza, R. M., & Hampton, R. Y. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.244798 · Cited by 49 · see citing works

Sampling the membrane: function of rhomboid-family proteins

Lemberg, M. K. (2013) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.01.002 · Cited by 46 · see citing works

Derlin rhomboid pseudoproteases employ substrate engagement and lipid distortion to enable the retrotranslocation of ERAD membrane substrates

Nejatfard, A., Wauer, N. A., Bhaduri, S., Conn, A. B., Gourkanti, S., Singh, N., Kuo, T., Kandel, R., Amaro, R. E., & Neal, S. E. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109840 · Cited by 43 · see citing works

“Mallostery”—ligand-dependent protein misfolding enables physiological regulation by ERAD

Wangeline, M. A., & Hampton, R. Y. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.001808 · Cited by 41 · see citing works

A Cdc48 “Retrochaperone” Function Is Required for the Solubility of Retrotranslocated, Integral Membrane Endoplasmic Reticulum-associated Degradation (ERAD-M) Substrates

Neal, S. E., Mak, R., Bennett, E. J., & Hampton, R. Y. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.770610 · Cited by 38 · see citing works

Five Questions (with their Answers) on ER ‐Associated Degradation

Pisoni, G. B., & Molinari, M. (2016) · Traffic · doi:10.1111/tra.12373 · Cited by 39 · see citing works

Posttranscriptional Regulation of Glycoprotein Quality Control in the Endoplasmic Reticulum Is Controlled by the E2 Ub-Conjugating Enzyme UBC6e

Hagiwara, M., Ling, J. J., Koenig, P.-A., & Ploegh, H. L. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.07.014 · Cited by 39 · see citing works

Proteostatic Tactics in the Strategy of Sterol Regulation

Wangeline, M. A., Vashistha, N., & Hampton, R. Y. (2017) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-111315-125036 · Cited by 38 · see citing works

Liver Cytochrome P450 3A Ubiquitination in Vivo by gp78/Autocrine Motility Factor Receptor and C Terminus of Hsp70-interacting Protein (CHIP) E3 Ubiquitin Ligases

Kim, S., Acharya, P., Engel, J. C., & Correia, M. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.167189 · Cited by 36 · see citing works

Regulated Endoplasmic Reticulum-associated Degradation of a Polytopic Protein

Ikeda, Y., Demartino, G., Brown, M. S., Lee, J. N., Goldstein, J. L., & Ye, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.044875 · Cited by 35 · see citing works

Ubiquitin-specific protease 19 regulates the stability of the E3 ubiquitin ligase MARCH6

Nakamura, N., Harada, K., Kato, M., & Hirose, S. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.07.025 · Cited by 34 · see citing works

Roles of Cdc48 in Regulated Protein Degradation in Yeast

Buchberger, A. (2013) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-5940-4_8 · Cited by 33 · see citing works

Proteolytic regulation of metabolic enzymes by E3 ubiquitin ligase complexes: lessons from yeast

Nakatsukasa, K., Okumura, F., & Kamura, T. (2015) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2015.1081869 · Cited by 33 · see citing works

Insulin-induced Gene Protein (INSIG)-dependent Sterol Regulation of Hmg2 Endoplasmic Reticulum-associated Degradation (ERAD) in Yeast

Theesfeld, C. L., & Hampton, R. Y. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.404517 · Cited by 33 · see citing works

Live Cell Imaging of Protein Dislocation from the Endoplasmic Reticulum

Zhong, Y., & Fang, S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.381798 · Cited by 33 · see citing works

Interactions between intersubunit transmembrane domains regulate the chaperone-dependent degradation of an oligomeric membrane protein

Buck, T. M., Jordahl, A. S., Yates, M. E., Preston, G. M., Cook, E., Kleyman, T. R., & Brodsky, J. L. (2016) · Biochemical Journal · doi:10.1042/bcj20160760 · Cited by 32 · see citing works

The degradation pathway of a model misfolded protein is determined by aggregation propensity

Sun, Z., & Brodsky, J. L. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e18-02-0117 · Cited by 30 · see citing works

Human Liver Cytochrome P450 3A4 Ubiquitination

Wang, Y., Kim, S., Trnka, M. J., Liu, Y., Burlingame, A. L., & Correia, M. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.611525 · Cited by 30 · see citing works

Hepatic cytochromes P450: structural degrons and barcodes, posttranslational modifications and cellular adapters in the ERAD-endgame

Kim, S., Wang, Y., Nabavi, N., Liu, Y., & Correia, M. A. (2016) · Drug Metabolism Reviews · doi:10.1080/03602532.2016.1195403 · Cited by 30 · see citing works

Phosphorylation and Methylation of Proteasomal Proteins of the Haloarcheon Haloferax volcanii

Humbard, M. A., Reuter, C., Zuobi-Hasona, K., Zhou, G.-Y., & Maupin-Furlow, J. (2010) · Archaea · doi:10.1155/2010/481725 · Cited by 27 · see citing works

HRD Complex Self-Remodeling Enables a Novel Route of Membrane Protein Retrotranslocation

Neal, S. E., Syau, D., Nejatfard, A., Nadeau, S., & Hampton, R. Y. (2020) · iScience · doi:10.1016/j.isci.2020.101493 · Cited by 24 · see citing works

Metabolically Regulated Endoplasmic Reticulum-associated Degradation of 3-Hydroxy-3-methylglutaryl-CoA Reductase

Leichner, G. S., Avner, R., Harats, D., & Roitelman, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.278036 · Cited by 24 · see citing works

Distinct Elements in the Proteasomal β5 Subunit Propeptide Required for Autocatalytic Processing and Proteasome Assembly

Li, X., Li, Y., Arendt, C. S., & Hochstrasser, M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.677047 · Cited by 23 · see citing works

Engineered Saccharomyces cerevisiae for the de novo synthesis of the aroma compound longifolene

Hassan, J. U., Kaleem, I., Rasool, A., Xu, K., Tahir, R. A., Lv, B., & Li, C. (2020) · Chemical Engineering Science · doi:10.1016/j.ces.2020.115799 · Cited by 23 · see citing works

Microbial Production of Isoprenoids

Wong, J., Rios‐Solis, L., & Keasling, J. D. (2017) · Springer eBooks · doi:10.1007/978-3-319-50436-0_219 · Cited by 21 · see citing works

Liver Cytochrome P450 3A Endoplasmic Reticulum-associated Degradation

Acharya, P., Liao, M., Engel, J. C., & Correia, M. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.186981 · Cited by 22 · see citing works

Subcellular Fractionation Analysis of the Extraction of Ubiquitinated Polytopic Membrane Substrate during ER-Associated Degradation

Nakatsukasa, K., & Kamura, T. (2016) · PLoS ONE · doi:10.1371/journal.pone.0148327 · Cited by 20 · see citing works

Hepatic cytochrome P450 ubiquitination: Conformational phosphodegrons for E2/E3 recognition?

Correia, M. A., Wang, Y., Kim, S.-M., & Guan, S. (2014) · IUBMB Life · doi:10.1002/iub.1247 · Cited by 17 · see citing works

Lipid-regulated degradation of HMG-CoA reductase and Insig-1 through distinct mechanisms in insect cells

Faulkner, R. A., Nguyen, A. D., Jo, Y., & DeBose‐Boyd, R. A. (2013) · Journal of Lipid Research · doi:10.1194/jlr.m033639 · Cited by 14 · see citing works

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Varshavsky, A. J. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-474-2_1 · Cited by 14 · see citing works

A bacterial toxin and a nonenveloped virus hijack ER-to-cytosol membrane translocation pathways to cause disease

He, K., Ravindran, M. S., & Tsai, B. (2015) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2015.1085826 · Cited by 13 · see citing works

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Fenech, E. J., Ben‐Dor, S., & Schuldiner, M. (2020) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-011520-104831 · Cited by 13 · see citing works

Emerging roles of rhomboid‐like pseudoproteases in inflammatory and innate immune responses

Luo, W., & Shu, H. (2017) · FEBS Letters · doi:10.1002/1873-3468.12796 · Cited by 12 · see citing works

Systemic inhibition of neddylation by 3-day MLN4924 treatment regime does not impair autophagic flux in mouse hearts and brains.

Reihe, C. A., Pekas, N., Wu, P., & Wang, X. (2017) · PubMed Central · Cited by 12 · see citing works

Cadmium and Secondary Structure-dependent Function of a Degron in the Pca1p Cadmium Exporter

Smith, N., Wei, W., Zhao, M., Qin, X., Seravalli, J., Kim, H., & Lee, J. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.724930 · Cited by 11 · see citing works

Thoughts on Quorum Sensing and Fungal Dimorphism

Nickerson, K. W., Atkin, A. L., Hargarten, J. C., Pathirana, R. U., & Hasim, S. (2012) · Springer eBooks · doi:10.1007/978-94-007-4264-2_12 · Cited by 10 · see citing works

Assays for protein retrotranslocation in ERAD

Neal, S. E., Duttke, S. H. C., & Hampton, R. Y. (2019) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2019.01.002 · Cited by 9 · see citing works

Applying natural product repurposing strategy to identify baicalein as novel caseinolytic protease P inhibitor and its application in the treatment of rice bacterial diseases

Sun, Z., Yang, T., Long, Z., Fu, X., Meng, J., Zhou, X., Yang, C., & Yang, S. (2025) · Pesticide Biochemistry and Physiology · doi:10.1016/j.pestbp.2025.106577 · Cited by 8 · see citing works

Absence of farnesol salvage in Candida albicans and probably in other fungi

Voshall, A., Gutzmann, D. J., Verdaguer, I. B., Crispim, M., Boone, C. H. T., Atkin, A. L., & Nickerson, K. W. (2024) · Applied and Environmental Microbiology · doi:10.1128/aem.00874-24 · Cited by 8 · see citing works

Microbial Production of Isoprenoids

Wong, J., Rios‐Solis, L., & Keasling, J. D. (2017) · Springer eBooks · doi:10.1007/978-3-319-31421-1_219-2 · Cited by 7 · see citing works

Membralin is required for maize development and defines a branch of the endoplasmic reticulum–associated degradation pathway in plants

Liu, B., Xu, C., He, Q., Zhang, K., Qi, S., Jin, Z., Cheng, W., Ding, Z., Chen, D., Zhao, X., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2406090121 · Cited by 6 · see citing works

Fish oil improves lipid profile in juvenile rats with intrauterine growth retardation by altering the transcriptional expression of lipid-related hepatic genes

Chen, L., Liang, L., Fang, Y., Wang, Y., & Zhu, W.-F. (2015) · The Journal of Maternal-Fetal & Neonatal Medicine · doi:10.3109/14767058.2015.1123244 · Cited by 6 · see citing works

Inner-nuclear-membrane–associated degradation employs Dfm1-independent retrotranslocation and alleviates misfolded transmembrane-protein toxicity

Flagg, M. P., Wangeline, M. A., Holland, S. R., Duttke, S. H. C., Benner, C. W., Neal, S. E., & Hampton, R. Y. (2021) · Molecular Biology of the Cell · doi:10.1091/mbc.e20-11-0720 · Cited by 6 · see citing works

San1-Mediated Quality Control: Substrate Recognition “Sans” Chaperones

Hampton, R. Y. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.12.022 · Cited by 6 · see citing works

Chapter 26 Mechanism-Based Inhibition of CYP3A4 and Other Cytochromes P450

Murray, B. P. (2009) · Annual reports in medicinal chemistry · doi:10.1016/s0065-7743(09)04426-1 · Cited by 6 · see citing works

Microbial Production of Isoprenoids

Wong, J., Rios‐Solis, L., & Keasling, J. D. (2016) · Springer eBooks · doi:10.1007/978-3-319-31421-1_219-1 · Cited by 5 · see citing works

Inositol 1,4,5‐trisphosphate receptor degradation pathways

Wojcikiewicz, R. J. H. (2012) · Wiley Interdisciplinary Reviews Membrane Transport and Signalling · doi:10.1002/wmts.4 · Cited by 5 · see citing works

Mechanism and Engineering Strategies of Sterol Homeostasis in Yeast

Li, M., Yu, H., & Ye, L. (2025) · ACS Synthetic Biology · doi:10.1021/acssynbio.5c00508 · Cited by 4 · see citing works

Multiplexed Photo-Cross-Linking Reveals Comprehensive Midnolin Interactome: Insights into Ubiquitin-Independent Degradation and Functional Diversity

Xu, Y., Zhao, W., Fu, J., Liu, Z., Nie, H., Zhang, J., Guo, J., Tan, M., & Chen, X. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c22099 · Cited by 4 · see citing works

New trends in microbial production of natural complex bioactive isoprenoids

Baadhe, R. R., Potumarthi, R., Mekala, N. K., & Gupta, V. K. (2015) · doi:10.1002/9781118733103.ch11 · Cited by 3 · see citing works

Isolation and Identification of Antimicrobial Protein from Saccharomyces cerevisiae and its Efficacy Against the Human Pathogens

Senthilraj, P., Sahu, S. K., & Kathiresan, K. (2015) · Research Journal of Microbiology · doi:10.3923/jm.2015.24.32 · Cited by 2 · see citing works

Derlin Rhomboid Pseudoproteases Employ Substrate Engagement and Lipid Distortion Function for Retrotranslocation of ER Multi-Spanning Membrane SubstratesPreprint

Nejatfard, A., Wauer, N. A., Bhaduri, S., Conn, A. B., Gourkanti, S., Singh, N., Kuo, T., Kandel, R., Amaro, R. E., & Neal, S. E. (2021) · SSRN Electronic Journal · doi:10.2139/ssrn.3811835 · Cited by 1 · see citing works

Regulation of the PAH1-encoded phosphatidate phosphatase and its role in lipid metabolism in yeast

Pascual, F. L. (2013) · doi:10.7282/t3862dgn

ERAD Substrate Recognition by the HRD1 Transmembrane Domain: A Molecular Genetic Analysis

Ma, M. (2013) · eScholarship (California Digital Library)

ChemInform Abstract: Protein Quality Control as a Strategy for Cellular Regulation: Lessons from Ubiquitin‐Mediated Regulation of the Serol Pathway

Hampton, R. Y., & Garza, R. M. (2009) · ChemInform · doi:10.1002/chin.200926269

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Devarajan, S. (2020) · doi:10.33612/diss.132023701

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Zinkevičiūtė, R., Ražanskas, R., Kaupinis, A., Macijauskaitė, N., Čiplys, E., Houen, G., & Slibinskas, R. (2022) · Current Issues in Molecular Biology · doi:10.3390/cimb44050122

Proteasomal and Lysosomal Degradation of Misfolded Proteins From the Endoplasmic Reticulum

Molinari, M. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-821618-7.00078-x

Navigating Misfolded Terrain: ER-Associated Degradation of Membrane Proteins

Agarwal, D., Solorio-Kirpichyan, K., Jordahl, E. M., Ramakrishnan, G., Scott, N. A., & Neal, S. E. (2026) · Chemical Reviews · doi:10.1021/acs.chemrev.5c00780

E3 Ubiquitin ligases molecular strategies against proteostasis defects of imperfect ageing

Upadhyay, A., Joshi, V., Amanullah, A., Mishra, R., Verma, R. K., Adlakha, Y. K., Suresh, A. K., Dhiman, R., Bhattacharyya, S., & Mishra, A. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103319

ChemInform Abstract: Protein Quality Control as a Strategy for Cellular Regulation: Lessons from Ubiquitin‐Mediated Regulation of the Serol Pathway

Hampton, R. Y., & Garza, R. M. (2009) · ChemInform · doi:10.1002/chin.200926269

ER-associated degradation in protein quality control and cellular regulation

Hampton, R. Y. (2002) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(02)00358-7 · Cited by 475 · see citing works

Proteostatic Tactics in the Strategy of Sterol Regulation

Wangeline, M. A., Vashistha, N., & Hampton, R. Y. (2017) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-111315-125036 · Cited by 38 · see citing works

Regulated quality control in physiological regulation of cellular processes: lessons from regulated ERAD of HMG‐CoA reductase (353.3)

Neal, S. E., Ornelas, L., Ruckstuhl, M., Singh, A., Tang, X., Vashista, N., Wangeline, M., & Hampton, R. Y. (2014) · The FASEB Journal · doi:10.1096/fasebj.28.1_supplement.353.3

Proteolysis and Sterol Regulation

Hampton, R. Y. (2002) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.18.032002.131219 · Cited by 104 · see citing works