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J Biol Chem, Vol. 273, Issue 15, 8545-8548, April 10, 1998
From the Howard Hughes Medical Institute, Departments of Chemistry
and Chemical Biology and of Molecular and Cellular Biology, Harvard
University, Cambridge, Massachusetts 02138
Lactacystin, a microbial natural product that
inhibits cell proliferation and induces neurite outgrowth in a murine
neuroblastoma cell line, has become a widely used reagent in functional
studies of the proteasome, a high molecular weight, multicatalytic
protease complex responsible for most non-lysosomal intracellular
protein degradation. The proteasome is composed of a 20 S catalytic
core and additional subunits that are thought to be involved in the recognition and unfolding of ubiquitinated proteins; the composite structure has a sedimentation coefficient of 26 S. Lactacystin binds
certain catalytic subunits of the 20 S proteasome and inhibits the
three best characterized peptidase activities of the proteasome, two
irreversibly and all at different rates (1). At least one of these
catalytic subunits is modified by lactacystin on the side chain
hydroxyl of the amino-terminal threonine (1), which appears to function
as the catalytic nucleophile in the proteolytic mechanism. Lactacystin
also inhibits peptide hydrolysis by the larger 26 S complex and
inhibits ubiquitin/proteasome-mediated degradation of short and long
lived proteins in the cell (2). This small molecule is currently the
only compound known that inhibits the proteasome specifically without
inhibiting any other protease yet tested in vitro (1, 3);
also it does not inhibit lysosomal protein degradation in the cell (2).
This is in contrast to other commonly used proteasome inhibitors, such
as peptide aldehydes and 3,4-dichloroisocoumarin, which inhibit a wide
range of proteases. Lactacystin has been used to implicate proteolysis by the proteasome in a number of fundamental processes from cellular differentiation and apoptosis to the degradation of proteins normally residing in the endoplasmic reticulum. In this review, the putative mechanism of action and some applications of lactacystin are discussed, as well as recent findings on proteasome function.
The Streptomyces product lactacystin (Fig.
1) was discovered on the basis of its
ability to inhibit cell growth and to induce neurite outgrowth in a
murine neuroblastoma cell line, Neuro-2a (3). The cytostatic effects of
lactacystin are not unique to Neuro-2a cells (4), and lactacystin has
been found to inhibit cell cycle progression in both the
G0/G1 and G2/M phases of the cell
cycle (4, 5). Lactacystin treatment of Neuro-2a cells results in a
predominantly bipolar morphology with two long processes emanating from
opposite sides of the cell body, maximal between 16 and 32 h after
the start of treatment (4). The cells become progressively more
multipolar (multiple neurite bearing) with continued exposure, and the
neurites become increasingly branched and display the hallmarks of
mature neurites (3). The phosphatase inhibitors okadaic acid and
calyculin A block lactacystin-induced bipolar morphology but not the
formation of branched neurite networks after 3 days (6). This implies
that induction of bipolar morphology and subsequent formation of
branched neurite networks are separable processes, with only the former
being dependent on the activity of phosphatases. Both of these
responses to lactacystin require de novo protein synthesis,
microtubule assembly, and actin polymerization (4).
The predominantly bipolar morphology that follows treatment with
lactacystin is distinct from the response to a number of other common
treatments leading to morphological differentiation. Neuro-2a cells
deprived of serum or treated with a variety of agents that raise
intracellular cAMP levels (and thus activate protein kinase A) tend to
become predominantly multipolar (4, 7, 8). Treatment of Neuro-2a cells
with retinoic acid, natural gangliosides, and synthetic sialyl
compounds tends to induce a more unipolar (single neurite bearing)
morphology (7, 8).
Lactacystin was initially tested in a variety of cellular and
biochemical assays in the hope of shedding light on its mode of action.
Lactacystin treatment was found to result in a transient intracellular
increase in cAMP levels, peaking at 24 h after the start of
treatment, which coincides with the window of maximal bipolar
morphology (3). The kinetics of this accumulation of intracellular cAMP
are very different from that observed with commonly used agents that
increase intracellular cAMP, such as prostaglandin E1 or
adenosine and isobutylmethylxanthine, which result in peak levels
within about 15-30 min of treatment in Neuro-2a cells (3). Since there
is evidence that secreted proteases and protease inhibitors play roles
in regulating neurite outgrowth and nerve regeneration (for review, see
Ref. 9), lactacystin was tested for its ability to inhibit two
extracellular serine proteases, thrombin and plasminogen activator, and
found to have no effect on these proteases (3). Lactacystin was also
shown to have no effect on protein kinase C activity, the inhibition of
which had also been previously implicated in neuronal differentiation (3).
Based on studies of neurite outgrowth in Neuro-2a cells and
inhibition of cell cycle progression in MG-63 human osteosarcoma cells
using a series of analogs of lactacystin, it was determined that an
electrophilic carbonyl at the C-4 position was required for activity
(4). Of particular interest was the finding that a The product of acylation was expected to be
clasto-lactacystin covalently attached to its target. In
order to identify the lactacystin-binding molecule, radioactive
versions of lactacystin and the related The Lactacystin and clasto-lactacystin Lactacystin inhibits the three well characterized, distinct peptidase
activities of the proteasome, chymotrypsin-like, trypsin-like, and
caspase-like, the first two irreversibly and all at different rates
(1). The The recent crystal structure of the Saccharomyces cerevisiae
20 S proteasome with clasto-lactacystin bound (soaked into
the already crystallized 20 S proteasome for 6 h) reveals that
only the side chain oxygen of the amino-terminal threonine of Pre2, the
yeast homolog of the mammalian subunit X, is covalently bound to
clasto-lactacystin (13). Although it is formally possible that the amino-terminal Four additional Lactacystin is highly specific for the proteasome, unlike peptide
aldehyde inhibitors often used in proteasome studies. Rock et
al. (14) reported the use of protease inhibitors to study the role
of the proteasome in the degradation of various proteins; however, the
peptide aldehyde inhibitors used in these studies were also shown to
inhibit potently the cysteine proteases calpain and cathepsin B. As
demonstrated in initial studies, lactacystin does not inhibit the
serine proteases thrombin or plasminogen activator (3). Lactacystin was
later shown to have no effect on any other protease tested, including
the serine proteases trypsin and chymotrypsin and the cysteine
proteases papain, calpain I, calpain II, and cathepsin B (1).
Furthermore, lactacystin does not inhibit lysosomal protein degradation
(2). Lactacystin therefore appears to interact with structural elements
unique to certain Lactacystin has been used to study the degradation of proteins that
normally reside in the endoplasmic reticulum. The cystic fibrosis
transmembrane conductance regulator undergoes maturation in the
endoplasmic reticulum, during which time much of the wild type and all
of a mutant form of the cystic fibrosis transmembrane conductance
regulator precursor protein are degraded; this degradation occurs at
least in part by proteasome-mediated proteolysis of the cytoplasmic
domain, as demonstrated using lactacystin and peptide aldehydes (14,
15). Other transmembrane proteins have also been found to be degraded
in this fashion (16-19). The degradation of abnormal and unassembled
proteins localized to the endoplasmic reticulum lumen is also dependent
upon the function of the proteasome (20-23).
The proteasome appears to be the sole or at least main
physiologically relevant target of lactacystin. There is a perfect correlation between the ability of a series of structural and stereochemical analogs of lactacystin to inhibit the proteasome's function and to compete with radiolabeled lactacystin for proteasome binding and their ability to induce neurite outgrowth in Neuro-2a cells
and to inhibit cell cycle progression in MG-63 cells (1, 4). There is
evidence that regulation of ubiquitination may be involved in
determining cell fate (for review, see Ref. 24), and it is also
possible that regulation of the proteasome itself may be involved in
determining cell fate and morphology over the course of
development.
The idea that the proteasome may be involved in neuronal
differentiation is not entirely unprecedented, although the prior evidence to support this notion is not compelling. The peptide aldehyde
protease inhibitor, N-benzyloxycarbonyl-Leu-Leu-leucinal, and certain other peptide aldehydes induce neurite outgrowth in PC12
rat pheochromocytoma cells, and purification of the
Z-Leu-Leu-Leu-7-amido-4-methylcoumarin-degrading activity
reveals the proteasome as the main target (25). Lactacystin exhibits
dose-dependent toxic effects on PC12 cells; however, it
does not appear to cause PC12 cells to differentiate (4). The
differentiation of PC12 cells induced by such peptide aldehydes may be
the result of inhibition of a protease or proteases other than the
proteasome, such as the calpains, since these inhibitors are not
specific for the proteasome. Alternatively, lactacystin may inhibit a
different subset of the proteasome's peptidase activities than
N-benzyloxycarbonyl-Leu-Leu-leucinal, and this may somehow abrogate neurite outgrowth in PC12 cells.
In addition to its effects on cell morphology in Neuro-2a cells,
lactacystin has been found to affect cell fate in other cell types.
Treatment with lactacystin blocks morphological changes of
Trypanosoma cruzi at two separate stages in the life cycle of this intracellular protozoan parasite (26). Lactacystin has also
been found to prolong survival of sympathetic neurons deprived of nerve
growth factor, implying that apoptosis of these cells upon nerve growth
factor deprivation involves the proteasome and that the proteasome acts
upstream of the interleukin-1 The induction of bipolar morphology by lactacystin in Neuro-2a cells
appears to involve inhibition of the chymotrypsin-like activity of the
proteasome, since of all the peptidase activities of the proteasome
only this activity seems to "antagonize" neurite outgrowth (31).
The chymotrypsin-like activity may be responsible for either the
proteolytic activation of a protein that antagonizes neurite outgrowth
or the degradation of a protein that promotes neurite outgrowth. This
activity could either specifically cleave the protein substrate after a
critical hydrophobic residue or else be a rate-limiting initial step in
the degradation of the relevant protein substrate(s). The potential
importance of the chymotrypsin-like activity as a modulator of cell
fate is further demonstrated by the finding that inhibition of this
activity in rat fibroblast and PC12 cells results in apoptosis
(30).
Since phosphatase inhibitors appear to block lactacystin-induced
bipolar neurite outgrowth (6), the immediate target of the proteasome
may help regulate the phosphorylation state of critical proteins
involved in the process of neurite outgrowth. For instance, the
proteasome may directly or indirectly inactivate a phosphatase that
promotes neurite outgrowth, or it may directly or indirectly activate a
kinase that antagonizes neurite outgrowth. The inhibition of such
activities by lactacystin's action on the proteasome could lead to
decreased phosphorylation of certain proteins, resulting in neurite
outgrowth in Neuro-2a cells.
Neurite outgrowth resulting from inhibition of the
chymotrypsin-like activity of the proteasome could reflect a
normal mechanism for the induction of a differentiated state in
Neuro-2a cells, although this is not clear at present. It is possible
that neurite outgrowth through lactacystin-mediated proteasome
inhibition mimics a normal mechanism involved in cellular
differentiation. A number of endogenous inhibitors of the proteasome
have been discovered, some of which affect multiple activities, whereas
others are more specific (32-34). Endogenous regulators of proteasome
activities might influence cell physiology and fate.
Lactacystin is the only known truly specific inhibitor of the
proteasome, and its utility has been demonstrated in a wide range of
systems. Lactacystin provides a means to rapidly and specifically
inactivate the proteasome and thereby provides a powerful new tool for
exploring proteasome function. Lactacystin's action is analogous to
the product of a temperature-sensitive allele, except that lactacystin
can remove function more rapidly and without resulting in a stress
response. Its use is highly portable, even to systems that are less
tractable to molecular biology, such as tissues and multicellular
organisms.
*
This minireview will be reprinted
in the 1997 Minireview Compendium, which
will be available in December, 1997. Some of the research summarized here was supported by
the National Institute of General Medical Sciences (to S. L. S.).
§
Investigator of the Howard Hughes Medical Institute. To whom
correspondence should be addressed. Tel.: 617-495-5318; Fax: 617-495-0751; E-mail: sls{at}slsiris.harvard.edu;
fenteany{at}slsiris.harvard.edu.
MINIREVIEW
Lactacystin, Proteasome Function, and Cell Fate*
and
INTRODUCTION
Top
Introduction
References
Lactacystin Inhibits Cell Cycle Progression in Different Cell
Types and Induces Neurite Outgrowth in a Murine Neuroblastoma Cell
Line
View larger version (22K):
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Fig. 1.
Putative mechanism of action of lactacystin
(see Refs. 1, 4, and 10). In addition to
N-acetylcysteine, glutathione can also react with
clasto-lactacystin 
-lactone to form a thioester analogous
to lactacystin, and there is some evidence that only the -lactone,
and not lactacystin itself, is capable of crossing the cell membrane
(11). Of eukaryotic proteasome subunits, there is at present direct
evidence only for amino-terminal threonine modification of mammalian
subunit X (1) and its homolog in yeast, Pre2 (13), although other
putative catalytic -type subunits of the eukaryotic proteasome also
appear capable of binding lactacystin (1, 2).
Identification of the Target of Lactacystin and Mechanism of
Action
-lactone related
to lactacystin, clasto-lactacystin -lactone (Fig. 1),
retained activity, whereas the corresponding dihydroxy acid, formally
the product of hydrolysis of the lactacystin thioester or the
-lactone, did not (4). The C-4 carbonyls of both the thioester and
the -lactone are reactive electrophiles, whereas the carboxylate of
the dihydroxy acid is essentially inert to nucleophilic attack. These
results suggested that the target may contain a reactive nucleophile
that attacks the C-4 position and that this reaction may affect the
target's activity. The acylation of the target by lactacystin was
envisioned to occur possibly through formation of
clasto-lactacystin -lactone as an active intermediate,
resulting from cyclization of the lactacystin with concomitant loss of
the leaving group N-acetylcysteine.
-lactone were synthesized
(1), with the expectation that these compounds would serve as covalent
affinity labels. This strategy led to the identification of the 20 S
proteasome as the sole observed target of lactacystin (1). Lactacystin binds specifically and covalently to certain putatively catalytic subunits of the proteasome and inhibits multiple proteasome peptidase activities (1), apparently through the intermediacy of the -lactone
(10). In particular, the amino-terminal threonine of the mammalian
proteasome subunit X (also known as MB1 or 
) is modified on its side
chain hydroxyl by clasto-lactacystin -lactone, forming an
ester-linked clasto-lactacystin/proteasome subunit X adduct
(Fig. 1).
-lactone can be formed spontaneously from lactacystin by
an intramolecular nucleophilic attack of the C-6 hydroxyl on the C-4
carbonyl carbon with displacement of the N-acetylcysteine moiety as leaving group. The -lactone can undergo spontaneous hydrolysis with ring opening to form clasto-lactacystin
dihydroxy acid, an inactive species (Fig. 1). There appear to be two
other major possible fates for the -lactone, which occur only within the cell (unlike hydrolysis, which can occur inside or outside the
cell). The first, as described, is the acylation of the proteasome, which involves a nucleophilic attack on the C-4 carbonyl carbon of the
-lactone with subsequent ring opening. The second is attack by the
sulfhydryl of glutathione with ring opening to form a thioester adduct
analogous to lactacystin; the resulting species does not directly react
with the proteasome but can subsequently undergo recyclization to
regenerate the active -lactone (11). Not only is there evidence to
suggest that the -lactone is the active intermediate in these
reactions, but there is also some evidence to suggest that only the
-lactone (and not lactacystin) can enter cultured mammalian
cells (11).
Lactacystin as a Probe of Proteasome Function
-lactone
covalently modify two -type subunits of proteasome purified from
bovine brain (1). Lactacystin acylates the amino-terminal threonine on
proteasome subunit X, the primary lactacystin-binding protein in bovine
brain, as well as an internal residue on this protein, and it inhibits multiple proteasome peptidase activities (1). The amino-terminal threonine residue of this mammalian -type subunit may therefore function as the catalytic nucleophile in the attack on the amide carbonyl carbon of the substrate, as in the archaeal and yeast proteasomes. Although lactacystin also binds at a much slower rate to
proteasome subunit Z in bovine brain proteasome preparations, there is
no evidence that the amino-terminal threonine of this protein is
modified (1).
-lactone inhibits each of these activities 15-20 times
faster than does lactacystin with the same rank order of effectiveness.
The complete, irreversible inhibition of the chymotrypsin-like and
trypsin-like activities in the bovine brain proteasome occurs in a time
frame in which only subunit X is modified with a 2:1
lactacystin:protein stoichiometry at saturation. This suggests that in
bovine brain proteasome covalent modification of subunit X alone
accounts for the irreversible inhibition of two distinct peptidase
activities. In addition to inhibiting the activities of the 20 S
proteasome (1), lactacystin and the -lactone also inhibit
peptidolysis by the 26 S proteasome and the
ubiquitin-dependent, proteasome-mediated degradation of
short-lived and long-lived proteins in the cell (2). Lactacystin also
blocks major histocompatibility complex class I antigen presentation (2, 12).
-amino group of threonine might also attack
the -lactone, the fact that the modified amino-terminal threonine on
subunit X is not blocked to Edman degradation (1) and the
aforementioned structural data (13) suggest that the side chain
hydroxyl is the final, if not only, nucleophile involved in this
reaction. clasto-Lactacystin displays four hydrogen bonds with the main chain of Pre2, and the dimethyl group on C-10 of clasto-lactacystin projects into the hydrophobic S-1 pocket
of Pre2 (13). These results are consistent with structure/activity relationships observed using lactacystin analogs (1, 4). The yeast
proteasome subunit Pup1, a homolog of the mammalian subunit Z (the
secondary lactacystin-binding protein in bovine brain) is not bound to
clasto-lactacystin in the crystal structure (13).
-type proteasome subunits, subunit Y and the
-interferon-inducible subunits LMP2, LMP7, and MECL1, appear capable
of binding lactacystin in other tissues, as determined by labeling with
radioactive compound followed by two-dimensional gel electrophoresis
(2). Therefore, six putatively catalytic proteasome subunits, falling
into three groups of related and reciprocally regulated subunits,
appear to be able to bind lactacystin, and none of the other subunits
of the proteasome bind lactacystin (1, 2). However, there is as yet no
evidence to suggest that the amino-terminal threonine residues of these
other subunits are modified.
-type catalytic subunits of the proteasome. These results demonstrate that, unlike peptide aldehyde inhibitors often used
in proteasome studies, lactacystin is highly specific for the
proteasome and thus seems a more useful reagent for the study of the
proteasome's involvement in biological processes.
The Proteasome and Cell Fate
-converting enzyme/Ced-3-like cysteine
protease, a protease previously known to be involved in apoptosis (27).
Lactacystin also prevents apoptosis in non-proliferating thymocytes,
although prolonged exposure to proteasome inhibitors actually results
in increased cell death in thymocytes even in the absence of other
inducers of apoptosis (28). On the other hand, lactacystin treatment induces rather than inhibits apoptosis in human monoblast cells (29). Inhibition of the proteasome also results in apoptosis in
proliferating rat fibroblast cells (but not in quiescent fibroblasts) and in both proliferating and non-proliferating, differentiated PC12
cells (30). Therefore, inhibition of the proteasome may result in cell
survival or death, depending on the cells examined, and the response
may be partly, though clearly not exclusively, determined by the
proliferation state of the cell. On a more mundane level, the response
may also simply depend on concentration of inhibitor used and the
duration of its effects (and consequently on the level of inhibition of
the proteasome over time). This is in basic agreement with findings
that the cytostatic and neuritogenic effects of lactacystin and peptide
aldehydes give way to cell death with increased dosage (4, 31).
FOOTNOTES
Supported by a National Graduate Science and Engineering Graduate
Fellowship.
REFERENCES
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Introduction
References
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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F. J. Iborra, A. E. Escargueil, K. Y. Kwek, A. Akoulitchev, and P. R. Cook Molecular cross-talk between the transcription, translation, and nonsense-mediated decay machineries J. Cell Sci., February 22, 2004; 117(6): 899 - 906. [Abstract] [Full Text] [PDF]
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G. R. Beck Jr. and N. Knecht Osteopontin Regulation by Inorganic Phosphate Is ERK1/2-, Protein Kinase C-, and Proteasome-dependent J. Biol. Chem., October 24, 2003; 278(43): 41921 - 41929. [Abstract] [Full Text] [PDF]
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 J.-T. Guo, Q. Zhu, and C. Seeger Cytopathic and Noncytopathic Interferon Responses in Cells Expressing Hepatitis C Virus Subgenomic Replicons J. Virol., October 15, 2003; 77(20): 10769 - 10779. [Abstract] [Full Text] [PDF]
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J. Zhao, Y. Ren, Q. Jiang, and J. Feng Parkin is recruited to the centrosome in response to inhibition of proteasomes J. Cell Sci., October 1, 2003; 116(19): 4011 - 4019. [Abstract] [Full Text] [PDF]
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L. A. Pasquini, P. M. Paez, M. A. N. B. Moreno, J. M. Pasquini, and E. F. Soto Inhibition of the Proteasome by Lactacystin Enhances Oligodendroglial Cell Differentiation J. Neurosci., June 1, 2003; 23(11): 4635 - 4644. [Abstract] [Full Text] [PDF]
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 S. C. Dryden, F. A. Nahhas, J. E. Nowak, A.-S. Goustin, and M. A. Tainsky Role for Human SIRT2 NAD-Dependent Deacetylase Activity in Control of Mitotic Exit in the Cell Cycle Mol. Cell. Biol., May 1, 2003; 23(9): 3173 - 3185. [Abstract] [Full Text] [PDF]
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P. Morales, M. Kong, E. Pizarro, and C. Pasten Participation of the sperm proteasome in human fertilization Hum. Reprod., May 1, 2003; 18(5): 1010 - 1017. [Abstract] [Full Text] [PDF]
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Y. Ren, J. Zhao, and J. Feng Parkin Binds to alpha /beta Tubulin and Increases their Ubiquitination and Degradation J. Neurosci., April 15, 2003; 23(8): 3316 - 3324. [Abstract] [Full Text] [PDF]
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B. Kessler, X. Hong, J. Petrovic, A. Borodovsky, N. P. Dantuma, M. Bogyo, H. S. Overkleeft, H. Ploegh, and R. Glas Pathways Accessory to Proteasomal Proteolysis Are Less Efficient in Major Histocompatibility Complex Class I Antigen Production J. Biol. Chem., March 14, 2003; 278(12): 10013 - 10021. [Abstract] [Full Text] [PDF]
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H. J. Rideout, Q. Wang, D. S. Park, and L. Stefanis Cyclin-Dependent Kinase Activity Is Required for Apoptotic Death But Not Inclusion Formation in Cortical Neurons after Proteasomal Inhibition J. Neurosci., February 15, 2003; 23(4): 1237 - 1245. [Abstract] [Full Text] [PDF]
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 L.-Y. Chen, C.-J. Pan, J.-J. Shieh, and J. Y. Chou Structure-function analysis of the glucose-6-phosphate transporter deficient in glycogen storage disease type Ib Hum. Mol. Genet., December 1, 2002; 11(25): 3199 - 3207. [Abstract] [Full Text] [PDF]
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L. Garrigue-Antar, N. Hartigan, and K. E. Kadler Post-translational Modification of Bone Morphogenetic Protein-1 Is Required for Secretion and Stability of the Protein J. Biol. Chem., November 1, 2002; 277(45): 43327 - 43334. [Abstract] [Full Text] [PDF]
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R. D. Erwert, R. K. Winn, J. M. Harlan, and D. D. Bannerman Shiga-like Toxin Inhibition of FLICE-like Inhibitory Protein Expression Sensitizes Endothelial Cells to Bacterial Lipopolysaccharide-induced Apoptosis J. Biol. Chem., October 18, 2002; 277(43): 40567 - 40574. [Abstract] [Full Text] [PDF]
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M. Lerm, M. Pop, G. Fritz, K. Aktories, and G. Schmidt Proteasomal Degradation of Cytotoxic Necrotizing Factor 1-Activated Rac Infect. Immun., August 1, 2002; 70(8): 4053 - 4058. [Abstract] [Full Text] [PDF]
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R. Z. Orlowski, G. W. Small, and Y. Y. Shi Evidence That Inhibition of p44/42 Mitogen-activated Protein Kinase Signaling Is a Factor in Proteasome Inhibitor-mediated Apoptosis J. Biol. Chem., July 26, 2002; 277(31): 27864 - 27871. [Abstract] [Full Text] [PDF]
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 Q. Chen, H. Kimura, and D. Schubert A novel mechanism for the regulation of amyloid precursor protein metabolism J. Cell Biol., July 8, 2002; 158(1): 79 - 89. [Abstract] [Full Text] [PDF]
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 I. Monleon, M. Iturralde, M. J. Martinez-Lorenzo, L. Monteagudo, P. Lasierra, L. Larrad, A. Pineiro, J. Naval, M. A. Alava, and A. Anel Lack of Fas/CD95 Surface Expression in Highly Proliferative Leukemic Cell Lines Correlates with Loss of CtBP/BARS and Redirection of the Protein toward Giant Lysosomal Structures Cell Growth Differ., July 1, 2002; 13(7): 315 - 324. [Abstract] [Full Text]
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A. Kallies, F. Rosenbauer, M. Scheller, K.-P. Knobeloch, and I. Horak Accumulation of c-Cbl and rapid termination of colony-stimulating factor 1 receptor signaling in interferon consensus sequence binding protein-deficient bone marrow-derived macrophages Blood, May 1, 2002; 99(9): 3213 - 3219. [Abstract] [Full Text] [PDF]
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U. Bohme and G. A. M. Cross Mutational analysis of the variant surface glycoprotein GPI-anchor signal sequence in Trypanosoma brucei J. Cell Sci., February 15, 2002; 115(4): 805 - 816. [Abstract] [Full Text] [PDF]
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J.-J. Shieh, M. Terzioglu, H. Hiraiwa, J. Marsh, C.-J. Pan, L.-Y. Chen, and J. Y. Chou The Molecular Basis of Glycogen Storage Disease Type 1a. STRUCTURE AND FUNCTION ANALYSIS OF MUTATIONS IN GLUCOSE-6-PHOSPHATASE J. Biol. Chem., February 8, 2002; 277(7): 5047 - 5053. [Abstract] [Full Text] [PDF]
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C.-J. Li and M. L. DePamphilis Mammalian Orc1 Protein Is Selectively Released from Chromatin and Ubiquitinated during the S-to-M Transition in the Cell Division Cycle Mol. Cell. Biol., January 1, 2002; 22(1): 105 - 116. [Abstract] [Full Text] [PDF]
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G. D. Strachan, R. Rallapalli, B. Pucci, T. P. Lafond, and D. J. Hall A Transcriptionally Inactive E2F-1 Targets the MDM Family of Proteins for Proteolytic Degradation J. Biol. Chem., November 30, 2001; 276(49): 45677 - 45685. [Abstract] [Full Text] [PDF]
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H. N. Kovacic, K. Irani, and P. J. Goldschmidt-Clermont Redox Regulation of Human Rac1 Stability by the Proteasome in Human Aortic Endothelial Cells J. Biol. Chem., November 30, 2001; 276(49): 45856 - 45861. [Abstract] [Full Text] [PDF]
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I. Bodo, A. Katsumi, E. A. Tuley, J. C. J. Eikenboom, Z. Dong, and J. E. Sadler Type 1 von Willebrand disease mutation Cys1149Arg causes intracellular retention and degradation of heterodimers: a possible general mechanism for dominant mutations of oligomeric proteins Blood, November 15, 2001; 98(10): 2973 - 2979. [Abstract] [Full Text] [PDF]
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 A. O. Aliprantis, D. S. Weiss, and A. Zychlinsky Toll-like receptor-2 transduces signals for NF-{kappa}B activation, apoptosis and reactive oxygen species production Innate Immunity, August 1, 2001; 7(4): 287 - 291. [Abstract] [PDF]
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A. Takano, I. Usui, T. Haruta, J. Kawahara, T. Uno, M. Iwata, and M. Kobayashi Mammalian Target of Rapamycin Pathway Regulates Insulin Signaling via Subcellular Redistribution of Insulin Receptor Substrate 1 and Integrates Nutritional Signals and Metabolic Signals of Insulin Mol. Cell. Biol., August 1, 2001; 21(15): 5050 - 5062. [Abstract] [Full Text] [PDF]
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J. M. Johnson, C. Nicot, J. Fullen, V. Ciminale, L. Casareto, J. C. Mulloy, S. Jacobson, and G. Franchini Free Major Histocompatibility Complex Class I Heavy Chain Is Preferentially Targeted for Degradation by Human T-Cell Leukemia/Lymphotropic Virus Type 1 p12I Protein J. Virol., July 1, 2001; 75(13): 6086 - 6094. [Abstract] [Full Text] [PDF]
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F. Noya, W.-M. Chien, T. R. Broker, and L. T. Chow p21cip1 Degradation in Differentiated Keratinocytes Is Abrogated by Costabilization with Cyclin E Induced by Human Papillomavirus E7 J. Virol., July 1, 2001; 75(13): 6121 - 6134. [Abstract] [Full Text] [PDF]
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 E. H. Hinchcliffe and G. Sluder "It Takes Two to Tango": understanding how centrosome duplication is regulated throughout the cell cycle Genes & Dev., May 15, 2001; 15(10): 1167 - 1181. [Full Text]
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Y. Tanaka, S. Engelender, S. Igarashi, R. K. Rao, T. Wanner, R. E. Tanzi, A. Sawa, V. L. Dawson, T. M. Dawson, and C. A. Ross Inducible expression of mutant {{alpha}}-synuclein decreases proteasome activity and increases sensitivity to mitochondria-dependent apoptosis Hum. Mol. Genet., April 1, 2001; 10(9): 919 - 926. [Abstract] [Full Text] [PDF]
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 B. Strack, A. Calistri, M. A. Accola, G. Palu, and H. G. Gottlinger A role for ubiquitin ligase recruitment in retrovirus release PNAS, November 21, 2000; 97(24): 13063 - 13068. [Abstract] [Full Text] [PDF]
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 E. Bülow, U. Gullberg, and I. Olsson Structural requirements for intracellular processing and sorting of bactericidal/permeability-increasing protein (BPI): comparison with lipopolysaccharide-binding protein J. Leukoc. Biol., November 1, 2000; 68(5): 669 - 678. [Abstract] [Full Text]
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H. Hilbi, R. J. Puro, and A. Zychlinsky Tripeptidyl Peptidase II Promotes Maturation of Caspase-1 in Shigella flexneri-Induced Macrophage Apoptosis Infect. Immun., October 1, 2000; 68(10): 5502 - 5508. [Abstract] [Full Text] [PDF]
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 G. Quievryn and A. Zhitkovich Loss of DNA-protein crosslinks from formaldehyde-exposed cells occurs through spontaneous hydrolysis and an active repair process linked to proteosome function Carcinogenesis, August 1, 2000; 21(8): 1573 - 1580. [Abstract] [Full Text] [PDF]
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A. Dace, L. Zhao, K. S. Park, T. Furuno, N. Takamura, M. Nakanishi, B. L. West, J. A. Hanover, and S.-y. Cheng Hormone binding induces rapid proteasome-mediated degradation of thyroid hormone receptors PNAS, July 19, 2000; (2000) 160257997. [Abstract] [Full Text]
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P. Masdehors, H. Merle-Beral, K. Maloum, S. Omura, H. Magdelenat, and J. Delic Deregulation of the ubiquitin system and p53 proteolysis modify the apoptotic response in B-CLL lymphocytes Blood, July 1, 2000; 96(1): 269 - 274. [Abstract] [Full Text] [PDF]
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 K. Schwarz, R. de Giuli, G. Schmidtke, S. Kostka, M. van den Broek, K. B. Kim, C. M. Crews, R. Kraft, and M. Groettrup The Selective Proteasome Inhibitors Lactacystin and Epoxomicin Can Be Used to Either Up- or Down-Regulate Antigen Presentation at Nontoxic Doses J. Immunol., June 15, 2000; 164(12): 6147 - 6157. [Abstract] [Full Text] [PDF]
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 T. Haruta, T. Uno, J. Kawahara, A. Takano, K. Egawa, P. M. Sharma, J. M. Olefsky, and M. Kobayashi A Rapamycin-Sensitive Pathway Down-Regulates Insulin Signaling via Phosphorylation and Proteasomal Degradation of Insulin Receptor Substrate-1 Mol. Endocrinol., June 1, 2000; 14(6): 783 - 794. [Abstract] [Full Text]
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 E. S. Lightcap, T. A. McCormack, C. S. Pien, V. Chau, J. Adams, and P. J. Elliott Proteasome Inhibition Measurements: Clinical Application Clin. Chem., May 1, 2000; 46(5): 673 - 683. [Abstract] [Full Text] [PDF]
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P. D. Yorgin, S. D. Hartson, A. M. Fellah, B. T. Scroggins, W. Huang, E. Katsanis, J. M. Couchman, R. L. Matts, and L. Whitesell Effects of Geldanamycin, a Heat-Shock Protein 90-Binding Agent, on T Cell Function and T Cell Nonreceptor Protein Tyrosine Kinases J. Immunol., March 15, 2000; 164(6): 2915 - 2923. [Abstract] [Full Text] [PDF]
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 O. VIEIRA, I. ESCARGUEIL-BLANC, G. JÜRGENS, C. BORNER, L. ALMEIDA, R. SALVAYRE, and A. NÈGRE-SALVAYRE Oxidized LDLs alter the activity of the ubiquitin-proteasome pathway: potential role in oxidized LDL-induced apoptosis FASEB J, March 1, 2000; 14(3): 532 - 542. [Abstract] [Full Text]
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C. A. Lange, T. Shen, and K. B. Horwitz Phosphorylation of human progesterone receptors at serine-294 by mitogen-activated protein kinase signals their degradation by the 26S proteasome PNAS, February 1, 2000; 97(3): 1032 - 1037. [Abstract] [Full Text] [PDF]
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S. Noguchi, S. Jianmongkol, A. T. Bender, Y. Kamada, D. R. Demady, and Y. Osawa Guanabenz-mediated Inactivation and Enhanced Proteolytic Degradation of Neuronal Nitric-oxide Synthase J. Biol. Chem., January 28, 2000; 275(4): 2376 - 2380. [Abstract] [Full Text] [PDF]
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J. Chillarón and I. G. Haas Dissociation from BiP and Retrotranslocation of Unassembled Immunoglobulin Light Chains Are Tightly Coupled to Proteasome Activity Mol. Biol. Cell, January 1, 2000; 11(1): 217 - 226. [Abstract] [Full Text]
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M. A. Accola, A. A. Bukovsky, M. S. Jones, and H. G. Göttlinger A Conserved Dileucine-Containing Motif in p6gag Governs the Particle Association of Vpx and Vpr of Simian Immunodeficiency Viruses SIVmac and SIVagm J. Virol., December 1, 1999; 73(12): 9992 - 9999. [Abstract] [Full Text]
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S. Soriano, A. S. C. Chyung, X. Chen, G. B. Stokin, V. M.-Y. Lee, and E. H. Koo Expression of beta -Amyloid Precursor Protein-CD3gamma Chimeras to Demonstrate the Selective Generation of Amyloid beta 1-40 and Amyloid beta 1-42 Peptides within Secretory and Endocytic Compartments J. Biol. Chem., November 5, 1999; 274(45): 32295 - 32300. [Abstract] [Full Text] [PDF]
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X.-Y. Li, M. Boudjelal, J.-H. Xiao, Z.-H. Peng, A. Asuru, S. Kang, G. J. Fisher, and J. J. Voorhees 1,25-Dihydroxyvitamin D3 Increases Nuclear Vitamin D3 Receptors by Blocking Ubiquitin/Proteasome-Mediated Degradation in Human Skin Mol. Endocrinol., October 1, 1999; 13(10): 1686 - 1694. [Abstract] [Full Text]
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H. Barth, C. Olenik, P. Sehr, G. Schmidt, K. Aktories, and D. K. Meyer Neosynthesis and Activation of Rho by Escherichia coli Cytotoxic Necrotizing Factor (CNF1) Reverse Cytopathic Effects of ADP-ribosylated Rho J. Biol. Chem., September 24, 1999; 274(39): 27407 - 27414. [Abstract] [Full Text] [PDF]
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M. Chiravuri, T. Schmitz, K. Yardley, R. Underwood, Y. Dayal, and B. T. Huber A Novel Apoptotic Pathway in Quiescent Lymphocytes Identified by Inhibition of a Post-Proline Cleaving Aminodipeptidase: A Candidate Target Protease, Quiescent Cell Proline Dipeptidase J. Immunol., September 15, 1999; 163(6): 3092 - 3099. [Abstract] [Full Text] [PDF]
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E. Freed, K. R. Lacey, P. Huie, S. A. Lyapina, R. J. Deshaies, T. Stearns, and P. K. Jackson Components of an SCF ubiquitin ligase localize to the centrosome and regulate the centrosome duplication cycle Genes & Dev., September 1, 1999; 13(17): 2242 - 2257. [Abstract] [Full Text]
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T. Tsukamoto and S. K. Nigam Cell-Cell Dissociation upon Epithelial Cell Scattering Requires a Step Mediated by the Proteasome J. Biol. Chem., August 27, 1999; 274(35): 24579 - 24584. [Abstract] [Full Text] [PDF]
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S. Glockzin, A. von Knethen, M. Scheffner, and B. Brune Activation of the Cell Death Program by Nitric Oxide Involves Inhibition of the Proteasome J. Biol. Chem., July 9, 1999; 274(28): 19581 - 19586. [Abstract] [Full Text] [PDF]
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N. Sakata, J. D. Stoops, and J. L. Dixon Cytosolic Components Are Required for Proteasomal Degradation of Newly Synthesized Apolipoprotein B in Permeabilized HepG2 Cells J. Biol. Chem., June 11, 1999; 274(24): 17068 - 17074. [Abstract] [Full Text] [PDF]
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G. Tang and S. H. Leppla Proteasome Activity Is Required for Anthrax Lethal Toxin To Kill Macrophages Infect. Immun., June 1, 1999; 67(6): 3055 - 3060. [Abstract] [Full Text] [PDF]
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L. Meng, B. H. B. Kwok, N. Sin, and C. M. Crews Eponemycin Exerts Its Antitumor Effect through the Inhibition of Proteasome Function Cancer Res., June 1, 1999; 59(12): 2798 - 2801. [Abstract] [Full Text] [PDF]
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Y. Zhang, M. Pasparakis, G. Kollias, and M. Simons Myocyte-dependent Regulation of Endothelial Cell Syndecan-4 Expression. ROLE OF TNF-alpha J. Biol. Chem., May 21, 1999; 274(21): 14786 - 14790. [Abstract] [Full Text] [PDF]
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K. Su, M. D. Roos, X. Yang, I. Han, A. J. Paterson, and J. E. Kudlow An N-terminal Region of Sp1 Targets Its Proteasome-dependent Degradation in Vitro J. Biol. Chem., May 21, 1999; 274(21): 15194 - 15202. [Abstract] [Full Text] [PDF]
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M. Obin, E. Mesco, X. Gong, A. L. Haas, J. Joseph, and A. Taylor Neurite Outgrowth in PC12 Cells. DISTINGUISHING THE ROLES OF UBIQUITYLATION AND UBIQUITIN-DEPENDENT PROTEOLYSIS J. Biol. Chem., April 23, 1999; 274(17): 11789 - 11795. [Abstract] [Full Text] [PDF]
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 Q. Fu, S.-W. Kim, H.-X. Chen, S. Grill, and Y.-C. Cheng Degradation of Topoisomerase I Induced by Topoisomerase I Inhibitors Is Dependent on Inhibitor Structure but Independent of Cell Death Mol. Pharmacol., April 1, 1999; 55(4): 677 - 683. [Abstract] [Full Text]
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J. A. Johnston, C. L. Ward, and R. R. Kopito Aggresomes: A Cellular Response to Misfolded Proteins J. Cell Biol., December 28, 1998; 143(7): 1883 - 1898. [Abstract] [Full Text] [PDF]
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G. J. F. Ding, P. A. Fischer, R. C. Boltz, J. A. Schmidt, J. J. Colaianne, A. Gough, R. A. Rubin, and D. K. Miller Characterization and Quantitation of NF-kappa B Nuclear Translocation Induced by Interleukin-1 and Tumor Necrosis Factor-alpha . DEVELOPMENT AND USE OF A HIGH CAPACITY FLUORESCENCE CYTOMETRIC SYSTEM J. Biol. Chem., October 30, 1998; 273(44): 28897 - 28905. [Abstract] [Full Text] [PDF]
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J. Tanikawa, E. Ichikawa-Iwata, C. Kanei-Ishii, A. Nakai, S.-i. Matsuzawa, J. C. Reed, and S. Ishii p53 Suppresses the c-Myb-induced Activation of Heat Shock Transcription Factor 3 J. Biol. Chem., May 12, 2000; 275(20): 15578 - 15585. [Abstract] [Full Text] [PDF]
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S. Nam, D. M. Smith, and Q. P. Dou Ester Bond-containing Tea Polyphenols Potently Inhibit Proteasome Activity in Vitro and in Vivo J. Biol. Chem., April 13, 2001; 276(16): 13322 - 13330. [Abstract] [Full Text] [PDF]
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D. D. Bannerman, J. C. Tupper, W. A. Ricketts, C. F. Bennett, R. K. Winn, and J. M. Harlan A Constitutive Cytoprotective Pathway Protects Endothelial Cells from Lipopolysaccharide-induced Apoptosis J. Biol. Chem., April 27, 2001; 276(18): 14924 - 14932. [Abstract] [Full Text] [PDF]
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R. Khanna, M. P. Myers, M. Laine, and D. M. Papazian Glycosylation Increases Potassium Channel Stability and Surface Expression in Mammalian Cells J. Biol. Chem., August 31, 2001; 276(36): 34028 - 34034. [Abstract] [Full Text] [PDF]
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F. Verdier, P. Walrafen, N. Hubert, S. Chretien, S. Gisselbrecht, C. Lacombe, and P. Mayeux Proteasomes Regulate the Duration of Erythropoietin Receptor Activation by Controlling Down-regulation of Cell Surface Receptors J. Biol. Chem., June 9, 2000; 275(24): 18375 - 18381. [Abstract] [Full Text] [PDF]
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M. Stasiolek, V. Gavrilyuk, A. Sharp, P. Horvath, K. Selmaj, and D. L. Feinstein Inhibitory and Stimulatory Effects of Lactacystin on Expression of Nitric Oxide Synthase Type 2 in Brain Glial Cells. THE ROLE OF Ikappa B-beta J. Biol. Chem., August 4, 2000; 275(32): 24847 - 24856. [Abstract] [Full Text] [PDF]
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Y. M. Patel and M. D. Lane Mitotic Clonal Expansion during Preadipocyte Differentiation: Calpain-mediated Turnover of p27 J. Biol. Chem., June 2, 2000; 275(23): 17653 - 17660. [Abstract] [Full Text] [PDF]
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A. Dace, L. Zhao, K. S. Park, T. Furuno, N. Takamura, M. Nakanishi, B. L. West, J. A. Hanover, and S.-y. Cheng Hormone binding induces rapid proteasome-mediated degradation of thyroid hormone receptors PNAS, August 1, 2000; 97(16): 8985 - 8990. [Abstract] [Full Text] [PDF]
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