| Year |
Citation |
Score |
| 2024 |
Mann MJ, Melendez-Suchi C, Vorndran HE, Sukhoplyasova M, Flory AR, Irvine MC, Iyer AR, Guerriero CJ, Brodsky JL, Hendershot LM, Buck TM. Loss of Grp170 results in catastrophic disruption of endoplasmic reticulum function. Molecular Biology of the Cell. mbcE24010012. PMID 38446639 DOI: 10.1091/mbc.E24-01-0012 |
0.398 |
|
| 2024 |
Porter A, Vorndran HE, Marciszyn A, Mutchler SM, Subramanya AR, Kleyman TR, Hendershot LM, Brodsky JL, Buck TM. Excess dietary sodium partially restores salt and water homeostasis caused by loss of the endoplasmic reticulum molecular chaperone, GRP170, in the mouse nephron. Biorxiv : the Preprint Server For Biology. PMID 38260467 DOI: 10.1101/2024.01.13.575426 |
0.314 |
|
| 2023 |
Hendershot LM, Buck TM, Brodsky JL. The Essential Functions of Molecular Chaperones and Folding Enzymes in Maintaining Endoplasmic Reticulum Homeostasis. Journal of Molecular Biology. 168418. PMID 38143019 DOI: 10.1016/j.jmb.2023.168418 |
0.447 |
|
| 2023 |
Mann MJ, Melendez-Suchi C, Sukhoplyasova M, Flory AR, Carson Irvine M, Iyer AR, Vorndran H, Guerriero CJ, Brodsky JL, Hendershot LM, Buck TM. Loss of Grp170 results in catastrophic disruption of endoplasmic reticulum functions. Biorxiv : the Preprint Server For Biology. PMID 37905119 DOI: 10.1101/2023.10.19.563191 |
0.395 |
|
| 2022 |
Brodsky JL, Engelman DM, Hendershot LM, Piana-Agostinetti S, Sommer T. Taking out the trash: How misfolded proteins are removed from the endoplasmic reticulum. Faculty Reviews. 11: 29. PMID 36267301 DOI: 10.12703/r-01-0000018 |
0.389 |
|
| 2022 |
Wiseman RL, Mesgarzadeh JS, Hendershot LM. Reshaping endoplasmic reticulum quality control through the unfolded protein response. Molecular Cell. 82: 1477-1491. PMID 35452616 DOI: 10.1016/j.molcel.2022.03.025 |
0.466 |
|
| 2022 |
Wood RK, Flory AR, Mann MJ, Talbot LJ, Hendershot LM. Secretory defects in pediatric osteosarcoma result from downregulation of selective COPII coatomer proteins. Iscience. 25: 104100. PMID 35402877 DOI: 10.1016/j.isci.2022.104100 |
0.349 |
|
| 2021 |
Ichhaporia VP, Hendershot LM. Role of the HSP70 Co-Chaperone SIL1 in Health and Disease. International Journal of Molecular Sciences. 22. PMID 33557244 DOI: 10.3390/ijms22041564 |
0.395 |
|
| 2019 |
Oikonomou C, Hendershot LM. Disposing of misfolded ER proteins: A troubled substrate's way out of the ER. Molecular and Cellular Endocrinology. 500: 110630. PMID 31669350 DOI: 10.1016/J.Mce.2019.110630 |
0.53 |
|
| 2018 |
Pobre KFR, Poet GJ, Hendershot LM. The endoplasmic reticulum (ER) chaperone BiP is a master regulator of ER functions: Getting by with a little help from ERdj friends. The Journal of Biological Chemistry. PMID 30563838 DOI: 10.1074/Jbc.Rev118.002804 |
0.547 |
|
| 2018 |
Ichhaporia VP, Kim J, Kavdia K, Vogel P, Horner L, Frase S, Hendershot LM. SIL1, the ER Hsp70 co-chaperone, plays a critical role in maintaining skeletal muscle proteostasis and physiology. Disease Models & Mechanisms. PMID 29666155 DOI: 10.1242/Dmm.033043 |
0.379 |
|
| 2016 |
Behnke J, Mann MJ, Scruggs FL, Feige MJ, Hendershot LM. Members of the Hsp70 Family Recognize Distinct Types of Sequences to Execute ER Quality Control. Molecular Cell. PMID 27546788 DOI: 10.1016/J.Molcel.2016.07.012 |
0.4 |
|
| 2016 |
Joo JH, Wang B, Frankel E, Ge L, Xu L, Iyengar R, Li-Harms X, Wright C, Shaw TI, Lindsten T, Green DR, Peng J, Hendershot LM, Kilic F, Sze JY, et al. The Noncanonical Role of ULK/ATG1 in ER-to-Golgi Trafficking Is Essential for Cellular Homeostasis. Molecular Cell. 62: 982. PMID 27315557 DOI: 10.1016/J.Molcel.2016.05.030 |
0.401 |
|
| 2016 |
Joo JH, Wang B, Frankel E, Ge L, Xu L, Iyengar R, Li-Harms X, Wright C, Shaw TI, Lindsten T, Green DR, Peng J, Hendershot LM, Kilic F, Sze JY, et al. The Noncanonical Role of ULK/ATG1 in ER-to-Golgi Trafficking Is Essential for Cellular Homeostasis. Molecular Cell. 62: 491-506. PMID 27203176 DOI: 10.1016/J.Molcel.2016.04.020 |
0.443 |
|
| 2015 |
Preissler S, Chambers JE, Crespillo-Casado A, Avezov E, Miranda E, Perez J, Hendershot LM, Harding HP, Ron D. Physiological modulation of BiP activity by trans-protomer engagement of the interdomain linker. Elife. 4. PMID 26473973 DOI: 10.7554/Elife.08961 |
0.502 |
|
| 2015 |
Feige MJ, Behnke J, Mittag T, Hendershot LM. Dimerization-dependent folding underlies assembly control of the clonotypic αβT cell receptor chains. The Journal of Biological Chemistry. 290: 26821-31. PMID 26400083 DOI: 10.1074/Jbc.M115.689471 |
0.437 |
|
| 2015 |
Behnke J, Feige MJ, Hendershot LM. BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions. Journal of Molecular Biology. 427: 1589-608. PMID 25698114 DOI: 10.1016/J.Jmb.2015.02.011 |
0.472 |
|
| 2015 |
Ichhaporia VP, Sanford T, Howes J, Marion TN, Hendershot LM. Sil1, a nucleotide exchange factor for BiP, is not required for antibody assembly or secretion. Molecular Biology of the Cell. 26: 420-9. PMID 25473114 DOI: 10.1091/Mbc.E14-09-1392 |
0.326 |
|
| 2014 |
Otero JH, Lizák B, Feige MJ, Hendershot LM. Dissection of structural and functional requirements that underlie the interaction of ERdj3 protein with substrates in the endoplasmic reticulum. The Journal of Biological Chemistry. 289: 27504-12. PMID 25143379 DOI: 10.1074/Jbc.M114.587147 |
0.424 |
|
| 2014 |
Leitman J, Shenkman M, Gofman Y, Shtern NO, Ben-Tal N, Hendershot LM, Lederkremer GZ. Herp coordinates compartmentalization and recruitment of HRD1 and misfolded proteins for ERAD. Molecular Biology of the Cell. 25: 1050-60. PMID 24478453 DOI: 10.1091/Mbc.E13-06-0350 |
0.546 |
|
| 2014 |
Pereira ER, Frudd K, Awad W, Hendershot LM. Endoplasmic reticulum (ER) stress and hypoxia response pathways interact to potentiate hypoxia-inducible factor 1 (HIF-1) transcriptional activity on targets like vascular endothelial growth factor (VEGF). The Journal of Biological Chemistry. 289: 3352-64. PMID 24347168 DOI: 10.1074/Jbc.M113.507194 |
0.732 |
|
| 2014 |
Behnke J, Hendershot LM. The large Hsp70 Grp170 binds to unfolded protein substrates in vivo with a regulation distinct from conventional Hsp70s. The Journal of Biological Chemistry. 289: 2899-907. PMID 24327659 DOI: 10.1074/Jbc.M113.507491 |
0.511 |
|
| 2013 |
Feige MJ, Hendershot LM. Quality control of integral membrane proteins by assembly-dependent membrane integration. Molecular Cell. 51: 297-309. PMID 23932713 DOI: 10.1016/J.Molcel.2013.07.013 |
0.429 |
|
| 2013 |
Preston AM, Hendershot LM. Examination of a second node of translational control in the unfolded protein response. Journal of Cell Science. 126: 4253-61. PMID 23843622 DOI: 10.1242/Jcs.130336 |
0.502 |
|
| 2013 |
Hendershot LM, Feige MJ, Buchner J. Acidification activates ERp44--a molecular litmus test for protein assembly. Molecular Cell. 50: 779-81. PMID 23806332 DOI: 10.1016/J.Molcel.2013.06.008 |
0.402 |
|
| 2013 |
Shenkman M, Groisman B, Ron E, Avezov E, Hendershot LM, Lederkremer GZ. A shared endoplasmic reticulum-associated degradation pathway involving the EDEM1 protein for glycosylated and nonglycosylated proteins. The Journal of Biological Chemistry. 288: 2167-78. PMID 23233672 DOI: 10.1074/Jbc.M112.438275 |
0.52 |
|
| 2012 |
Mann MJ, Pereira ER, Liao N, Hendershot LM. UPR-induced resistance to etoposide is downstream of PERK and independent of changes in topoisomerase IIα levels. Plos One. 7: e47931. PMID 23144714 DOI: 10.1371/Journal.Pone.0047931 |
0.733 |
|
| 2012 |
Lai CW, Otero JH, Hendershot LM, Snapp E. ERdj4 protein is a soluble endoplasmic reticulum (ER) DnaJ family protein that interacts with ER-associated degradation machinery. The Journal of Biological Chemistry. 287: 7969-78. PMID 22267725 DOI: 10.1074/Jbc.M111.311290 |
0.536 |
|
| 2012 |
Howes J, Shimizu Y, Feige MJ, Hendershot LM. C-terminal mutations destabilize SIL1/BAP and can cause Marinesco-Sjögren syndrome. The Journal of Biological Chemistry. 287: 8552-60. PMID 22219183 DOI: 10.1074/Jbc.M111.333286 |
0.466 |
|
| 2011 |
Santiago T, Kulemzin SV, Reshetnikova ES, Chikaev NA, Volkova OY, Mechetina LV, Zhao M, Davis RS, Taranin AV, Najakshin AM, Hendershot LM, Burrows PD. FCRLA is a resident endoplasmic reticulum protein that associates with intracellular Igs, IgM, IgG and IgA. International Immunology. 23: 43-53. PMID 21149418 DOI: 10.1093/Intimm/Dxq456 |
0.415 |
|
| 2011 |
Feige MJ, Hendershot LM. Disulfide bonds in ER protein folding and homeostasis. Current Opinion in Cell Biology. 23: 167-75. PMID 21144725 DOI: 10.1016/J.Ceb.2010.10.012 |
0.498 |
|
| 2010 |
Shimizu Y, Okuda-Shimizu Y, Hendershot LM. Ubiquitylation of an ERAD substrate occurs on multiple types of amino acids. Molecular Cell. 40: 917-26. PMID 21172657 DOI: 10.1016/J.Molcel.2010.11.033 |
0.436 |
|
| 2010 |
Pereira ER, Liao N, Neale GA, Hendershot LM. Transcriptional and post-transcriptional regulation of proangiogenic factors by the unfolded protein response. Plos One. 5. PMID 20824063 DOI: 10.1371/Journal.Pone.0012521 |
0.768 |
|
| 2010 |
Masciarelli S, Fra AM, Pengo N, Bertolotti M, Cenci S, Fagioli C, Ron D, Hendershot LM, Sitia R. CHOP-independent apoptosis and pathway-selective induction of the UPR in developing plasma cells. Molecular Immunology. 47: 1356-65. PMID 20044139 DOI: 10.1016/J.Molimm.2009.12.003 |
0.472 |
|
| 2010 |
Otero JH, Lizák B, Hendershot LM. Life and death of a BiP substrate. Seminars in Cell & Developmental Biology. 21: 472-8. PMID 20026282 DOI: 10.1016/J.Semcdb.2009.12.008 |
0.489 |
|
| 2010 |
Feige MJ, Hendershot LM, Buchner J. How antibodies fold. Trends in Biochemical Sciences. 35: 189-98. PMID 20022755 DOI: 10.1016/J.Tibs.2009.11.005 |
0.391 |
|
| 2010 |
Ma Y, Shimizu Y, Mann MJ, Jin Y, Hendershot LM. Plasma cell differentiation initiates a limited ER stress response by specifically suppressing the PERK-dependent branch of the unfolded protein response. Cell Stress & Chaperones. 15: 281-93. PMID 19898960 DOI: 10.1007/S12192-009-0142-9 |
0.486 |
|
| 2010 |
Feige MJ, Hendershot LM, Buchner J. Response to Corcos: exceptions to the rules Trends in Biochemical Sciences. 35: 594. DOI: 10.1016/J.Tibs.2010.07.011 |
0.328 |
|
| 2009 |
Shimizu Y, Meunier L, Hendershot LM. pERp1 is significantly up-regulated during plasma cell differentiation and contributes to the oxidative folding of immunoglobulin Proceedings of the National Academy of Sciences of the United States of America. 106: 17013-17018. PMID 19805157 DOI: 10.1073/Pnas.0811591106 |
0.439 |
|
| 2009 |
Vembar SS, Jin Y, Brodsky JL, Hendershot LM. The mammalian Hsp40 ERdj3 requires its Hsp70 interaction and substrate-binding properties to complement various yeast Hsp40-dependent functions. The Journal of Biological Chemistry. 284: 32462-71. PMID 19748898 DOI: 10.1074/Jbc.M109.000729 |
0.425 |
|
| 2009 |
Feige MJ, Groscurth S, Marcinowski M, Shimizu Y, Kessler H, Hendershot LM, Buchner J. An unfolded CH1 domain controls the assembly and secretion of IgG antibodies. Molecular Cell. 34: 569-79. PMID 19524537 DOI: 10.1016/J.Molcel.2009.04.028 |
0.333 |
|
| 2009 |
Shimizu Y, Hendershot LM. Oxidative folding: cellular strategies for dealing with the resultant equimolar production of reactive oxygen species. Antioxidants & Redox Signaling. 11: 2317-31. PMID 19243234 DOI: 10.1089/Ars.2009.2501 |
0.391 |
|
| 2008 |
Petrova K, Oyadomari S, Hendershot LM, Ron D. Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3. The Embo Journal. 27: 2862-72. PMID 18923430 DOI: 10.1038/Emboj.2008.199 |
0.392 |
|
| 2008 |
Jin Y, Awad W, Petrova K, Hendershot LM. Regulated release of ERdj3 from unfolded proteins by BiP. The Embo Journal. 27: 2873-82. PMID 18923428 DOI: 10.1038/Emboj.2008.207 |
0.373 |
|
| 2008 |
Awad W, Estrada I, Shen Y, Hendershot LM. BiP mutants that are unable to interact with endoplasmic reticulum DnaJ proteins provide insights into interdomain interactions in BiP. Proceedings of the National Academy of Sciences of the United States of America. 105: 1164-9. PMID 18203820 DOI: 10.1073/Pnas.0702132105 |
0.441 |
|
| 2008 |
Santiago T, Hendershot L, Burrows P. Su.93. Expression and Function of FcRLA, an Fc Receptor Related Intracellular Protein Clinical Immunology. 127: S154. DOI: 10.1016/J.Clim.2008.03.444 |
0.352 |
|
| 2007 |
Okuda-Shimizu Y, Hendershot LM. Characterization of an ERAD pathway for nonglycosylated BiP substrates, which require Herp. Molecular Cell. 28: 544-54. PMID 18042451 DOI: 10.1016/J.Molcel.2007.09.012 |
0.344 |
|
| 2007 |
Shen Y, Hendershot LM. Identification of ERdj3 and OBF-1/BOB-1/OCA-B as direct targets of XBP-1 during plasma cell differentiation. Journal of Immunology (Baltimore, Md. : 1950). 179: 2969-78. PMID 17709512 DOI: 10.4049/Jimmunol.179.5.2969 |
0.425 |
|
| 2007 |
Richter K, Hendershot LM, Freeman BC. The cellular world according to Hsp90. Nature Structural & Molecular Biology. 14: 90-4. PMID 17277798 DOI: 10.1038/Nsmb0207-90 |
0.323 |
|
| 2007 |
Shimizu Y, Hendershot LM. Organization of the functions and components of the endoplasmic reticulum. Advances in Experimental Medicine and Biology. 594: 37-46. PMID 17205673 DOI: 10.1007/978-0-387-39975-1_4 |
0.533 |
|
| 2006 |
Lee AS, Hendershot LM. ER stress and cancer. Cancer Biology & Therapy. 5: 721-2. PMID 16880733 DOI: 10.4161/Cbt.5.7.3120 |
0.323 |
|
| 2006 |
Mann MJ, Hendershot LM. UPR activation alters chemosensitivity of tumor cells. Cancer Biology & Therapy. 5: 736-40. PMID 16861918 DOI: 10.4161/Cbt.5.7.2969 |
0.358 |
|
| 2005 |
Dudek J, Greiner M, Müller A, Hendershot LM, Kopsch K, Nastainczyk W, Zimmermann R. ERj1p has a basic role in protein biogenesis at the endoplasmic reticulum. Nature Structural & Molecular Biology. 12: 1008-14. PMID 16244664 DOI: 10.1038/Nsmb1007 |
0.448 |
|
| 2005 |
Gray MD, Mann M, Nitiss JL, Hendershot LM. Activation of the unfolded protein response is necessary and sufficient for reducing topoisomerase IIalpha protein levels and decreasing sensitivity to topoisomerase-targeted drugs. Molecular Pharmacology. 68: 1699-707. PMID 16141312 DOI: 10.1124/Mol.105.014753 |
0.46 |
|
| 2005 |
Alder NN, Shen Y, Brodsky JL, Hendershot LM, Johnson AE. The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulum. The Journal of Cell Biology. 168: 389-99. PMID 15684029 DOI: 10.1083/Jcb.200409174 |
0.38 |
|
| 2005 |
Brewer JW, Hendershot LM. Building an antibody factory: a job for the unfolded protein response. Nature Immunology. 6: 23-9. PMID 15611778 DOI: 10.1038/Ni1149 |
0.394 |
|
| 2005 |
Shen Y, Hendershot LM. ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates. Molecular Biology of the Cell. 16: 40-50. PMID 15525676 DOI: 10.1091/Mbc.E04-05-0434 |
0.461 |
|
| 2005 |
Brewer JW, Hendershot LM. Erratum: Corrigendum: Building an antibody factory: a job for the unfolded protein response Nature Immunology. 6: 219-219. DOI: 10.1038/Ni0205-219D |
0.376 |
|
| 2004 |
Ma Y, Hendershot LM. The role of the unfolded protein response in tumour development: friend or foe? Nature Reviews. Cancer. 4: 966-77. PMID 15573118 DOI: 10.1038/Nrc1505 |
0.457 |
|
| 2004 |
Hendershot LM. The ER function BiP is a master regulator of ER function. The Mount Sinai Journal of Medicine, New York. 71: 289-97. PMID 15543429 |
0.467 |
|
| 2004 |
Ma Y, Hendershot LM. ER chaperone functions during normal and stress conditions. Journal of Chemical Neuroanatomy. 28: 51-65. PMID 15363491 DOI: 10.1016/J.Jchemneu.2003.08.007 |
0.562 |
|
| 2004 |
Tessitore A, del P Martin M, Sano R, Ma Y, Mann L, Ingrassia A, Laywell ED, Steindler DA, Hendershot LM, d'Azzo A. GM1-ganglioside-mediated activation of the unfolded protein response causes neuronal death in a neurodegenerative gangliosidosis. Molecular Cell. 15: 753-66. PMID 15350219 DOI: 10.1016/J.Molcel.2004.08.029 |
0.343 |
|
| 2004 |
Ma Y, Hendershot LM. Herp is dually regulated by both the endoplasmic reticulum stress-specific branch of the unfolded protein response and a branch that is shared with other cellular stress pathways. The Journal of Biological Chemistry. 279: 13792-9. PMID 14742429 DOI: 10.1074/Jbc.M313724200 |
0.476 |
|
| 2003 |
Ma Y, Hendershot LM. Delineation of a negative feedback regulatory loop that controls protein translation during endoplasmic reticulum stress. The Journal of Biological Chemistry. 278: 34864-73. PMID 12840028 DOI: 10.1074/Jbc.M301107200 |
0.511 |
|
| 2003 |
Ma Y, Hendershot LM. The stressful road to antibody secretion. Nature Immunology. 4: 310-1. PMID 12660729 DOI: 10.1038/Ni0403-310 |
0.378 |
|
| 2002 |
Meunier L, Usherwood YK, Chung KT, Hendershot LM. A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Molecular Biology of the Cell. 13: 4456-69. PMID 12475965 DOI: 10.1091/Mbc.E02-05-0311 |
0.493 |
|
| 2002 |
Marcu MG, Doyle M, Bertolotti A, Ron D, Hendershot L, Neckers L. Heat shock protein 90 modulates the unfolded protein response by stabilizing IRE1alpha. Molecular and Cellular Biology. 22: 8506-13. PMID 12446770 DOI: 10.1128/Mcb.22.24.8506-8513.2002 |
0.505 |
|
| 2002 |
Ma Y, Hendershot LM. The mammalian endoplasmic reticulum as a sensor for cellular stress. Cell Stress & Chaperones. 7: 222-9. PMID 12380691 DOI: 10.1379/1466-1268(2002)007<0222:Tmeraa>2.0.Co;2 |
0.44 |
|
| 2002 |
Chung KT, Shen Y, Hendershot LM. BAP, a mammalian BiP-associated protein, is a nucleotide exchange factor that regulates the ATPase activity of BiP. The Journal of Biological Chemistry. 277: 47557-63. PMID 12356756 DOI: 10.1074/jbc.M208377200 |
0.441 |
|
| 2002 |
Shen J, Chen X, Hendershot L, Prywes R. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Developmental Cell. 3: 99-111. PMID 12110171 DOI: 10.1016/S1534-5807(02)00203-4 |
0.467 |
|
| 2002 |
Ma Y, Brewer JW, Diehl JA, Hendershot LM. Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response. Journal of Molecular Biology. 318: 1351-65. PMID 12083523 DOI: 10.1016/S0022-2836(02)00234-6 |
0.5 |
|
| 2002 |
Shen Y, Meunier L, Hendershot LM. Identification and characterization of a novel endoplasmic reticulum (ER) DnaJ homologue, which stimulates ATPase activity of BiP in vitro and is induced by ER stress. The Journal of Biological Chemistry. 277: 15947-56. PMID 11836248 DOI: 10.1074/jbc.M112214200 |
0.485 |
|
| 2002 |
Ma Y, Hendershot LM. The unfolding tale of the unfolded protein response. Cell. 107: 827-30. PMID 11779459 DOI: 10.1016/S0092-8674(01)00623-7 |
0.524 |
|
| 2001 |
Vanhove M, Usherwood YK, Hendershot LM. Unassembled Ig heavy chains do not cycle from BiP in vivo but require light chains to trigger their release. Immunity. 15: 105-14. PMID 11485742 DOI: 10.1016/S1074-7613(01)00163-7 |
0.308 |
|
| 2001 |
Hendershot LM, Bulleid NJ. Protein-specific chaperones: the role of hsp47 begins to gel. Current Biology : Cb. 10: R912-5. PMID 11137028 DOI: 10.1016/S0960-9822(00)00850-2 |
0.406 |
|
| 2001 |
Creemers JW, van de Loo JW, Plets E, Hendershot LM, Van De Ven WJ. Binding of BiP to the processing enzyme lymphoma proprotein convertase prevents aggregation, but slows down maturation. The Journal of Biological Chemistry. 275: 38842-7. PMID 10964928 DOI: 10.1074/Jbc.M006758200 |
0.388 |
|
| 2000 |
Hendershot LM. Giving protein traffic the green light. Nature Cell Biology. 2: E105-6. PMID 10854339 DOI: 10.1038/35014100 |
0.516 |
|
| 2000 |
Bertolotti A, Zhang Y, Hendershot LM, Harding HP, Ron D. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nature Cell Biology. 2: 326-32. PMID 10854322 DOI: 10.1038/35014014 |
0.556 |
|
| 1999 |
Brewer JW, Hendershot LM, Sherr CJ, Diehl JA. Mammalian unfolded protein response inhibits cyclin D1 translation and cell-cycle progression. Proceedings of the National Academy of Sciences of the United States of America. 96: 8505-10. PMID 10411905 DOI: 10.1073/Pnas.96.15.8505 |
0.461 |
|
| 1999 |
Lee YK, Brewer JW, Hellman R, Hendershot LM. BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly. Molecular Biology of the Cell. 10: 2209-19. PMID 10397760 DOI: 10.1091/Mbc.10.7.2209 |
0.338 |
|
| 1999 |
Minegishi Y, Hendershot LM, Conley ME. Novel mechanisms control the folding and assembly of lambda5/14.1 and VpreB to produce an intact surrogate light chain. Proceedings of the National Academy of Sciences of the United States of America. 96: 3041-6. PMID 10077633 DOI: 10.1073/Pnas.96.6.3041 |
0.403 |
|
| 1999 |
Hellman R, Vanhove M, Lejeune A, Stevens FJ, Hendershot LM. The in vivo association of BiP with newly synthesized proteins is dependent on the rate and stability of folding and not simply on the presence of sequences that can bind to BiP. The Journal of Cell Biology. 144: 21-30. PMID 9885241 DOI: 10.1083/Jcb.144.1.21 |
0.497 |
|
| 1998 |
Hamman BD, Hendershot LM, Johnson AE. BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell. 92: 747-58. PMID 9529251 DOI: 10.1016/S0092-8674(00)81403-8 |
0.386 |
|
| 1998 |
Skowronek MH, Hendershot LM, Haas IG. The variable domain of nonassembled Ig light chains determines both their half-life and binding to the chaperone BiP. Proceedings of the National Academy of Sciences of the United States of America. 95: 1574-8. PMID 9465057 DOI: 10.1073/Pnas.95.4.1574 |
0.337 |
|
| 1998 |
Lawson B, Brewer JW, Hendershot LM. Geldanamycin, an hsp90/GRP94-binding drug, induces increased transcription of endoplasmic reticulum (ER) chaperones via the ER stress pathway. Journal of Cellular Physiology. 174: 170-8. PMID 9428803 DOI: 10.1002/(Sici)1097-4652(199802)174:2<170::Aid-Jcp4>3.0.Co;2-L |
0.58 |
|
| 1998 |
Brewer JW, Cleveland JL, Hendershot LM. A pathway distinct from the mammalian unfolded protein response regulates expression of endoplasmic reticulum chaperones in non-stressed cells. The Embo Journal. 16: 7207-16. PMID 9384597 DOI: 10.1093/Emboj/16.23.7207 |
0.511 |
|
| 1997 |
Lièvremont JP, Rizzuto R, Hendershot L, Meldolesi J. BiP, a major chaperone protein of the endoplasmic reticulum lumen, plays a direct and important role in the storage of the rapidly exchanging pool of Ca2+. The Journal of Biological Chemistry. 272: 30873-9. PMID 9388233 DOI: 10.1074/Jbc.272.49.30873 |
0.361 |
|
| 1997 |
Morris JA, Dorner AJ, Edwards CA, Hendershot LM, Kaufman RJ. Immunoglobulin binding protein (BiP) function is required to protect cells from endoplasmic reticulum stress but is not required for the secretion of selective proteins. The Journal of Biological Chemistry. 272: 4327-34. PMID 9020152 DOI: 10.1074/Jbc.272.7.4327 |
0.534 |
|
| 1996 |
Wei J, Hendershot LM. Protein folding and assembly in the endoplasmic reticulum. Exs. 77: 41-55. PMID 8856968 DOI: 10.1007/978-3-0348-9088-5_4 |
0.417 |
|
| 1996 |
Wang XZ, Lawson B, Brewer JW, Zinszner H, Sanjay A, Mi LJ, Boorstein R, Kreibich G, Hendershot LM, Ron D. Signals from the stressed endoplasmic reticulum induce C/EBP-homologous protein (CHOP/GADD153). Molecular and Cellular Biology. 16: 4273-80. PMID 8754828 DOI: 10.1128/Mcb.16.8.4273 |
0.314 |
|
| 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 |
0.447 |
|
| 1995 |
Fitts MG, Metzger DW, Hendershot LM, Mage RG. The rabbit B cell antigen receptor is non-covalently associated with unique heteromeric protein complexes: possible insights into the membrane IgM/IgD coexpression paradox. Molecular Immunology. 32: 753-9. PMID 7659100 DOI: 10.1016/0161-5890(95)00028-D |
0.374 |
|
| 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 |
0.464 |
|
| 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 |
0.314 |
|
| 1995 |
Wei J, Hendershot LM. Characterization of the nucleotide binding properties and ATPase activity of recombinant hamster BiP purified from bacteria. The Journal of Biological Chemistry. 270: 26670-6. PMID 7592893 DOI: 10.1074/Jbc.270.44.26670 |
0.326 |
|
| 1993 |
Gaut JR, Hendershot LM. The modification and assembly of proteins in the endoplasmic reticulum Current Opinion in Cell Biology. 5: 589-595. PMID 7903041 DOI: 10.1016/0955-0674(93)90127-C |
0.435 |
|
| 1992 |
Freiden P, Gaut J, Hendershot L. Interconversion of three differentially modified and assembled forms of BiP. The Embo Journal. 11: 63-70. DOI: 10.1002/J.1460-2075.1992.Tb05028.X |
0.465 |
|
| 1990 |
Ma J, Kearney JF, Hendershot LM. Association of transport-defective light chains with immunoglobulin heavy chain binding protein Molecular Immunology. 27: 623-630. PMID 2118593 DOI: 10.1016/0161-5890(90)90004-J |
0.306 |
|
| 1990 |
Hendershot LM. Immunoglobulin heavy chain and binding protein complexes are dissociated in vivo by light chain addition. The Journal of Cell Biology. 111: 829-37. PMID 2118144 DOI: 10.1083/Jcb.111.3.829 |
0.441 |
|
| 1988 |
Hendershot LM, Ting J, Lee AS. Identity of the immunoglobulin heavy-chain-binding protein with the 78,000-dalton glucose-regulated protein and the role of posttranslational modifications in its binding function Molecular and Cellular Biology. 8: 4250-4256. PMID 3141786 DOI: 10.1128/Mcb.8.10.4250 |
0.451 |
|
| 1987 |
Pollok BA, Anker R, Eldridge P, Hendershot L, Levitt D. Molecular basis of the cell-surface expression of immunoglobulin mu chain without light chain in human B lymphocytes. Proceedings of the National Academy of Sciences of the United States of America. 84: 9199-9203. PMID 3122216 DOI: 10.1073/Pnas.84.24.9199 |
0.363 |
|
| 1987 |
Hendershot L, Bole D, Kearney JF. The role of immunoglobulin heavy chain binding protein. in immunoglobulin transport Trends in Immunology. 8: 111-114. DOI: 10.1016/0167-5699(87)90861-9 |
0.327 |
|
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