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1 g proteins Insig1 or the cytosolic domain of SREBP cleavage-activating protein.
2  cleaving SREBP-2 in a fashion that requires SREBP cleavage-activating protein.
3 tivating point mutation in the gene encoding SREBP cleavage-activating protein.
4  [sterol-regulatory element-binding protein (SREBP) cleavage-activating protein] acts as a cholestero
5 the enzyme; and 2) sterol-induced binding to SREBP cleavage-activating protein, an action that blocks
6 rmal SREBP-processing pathway, including the SREBP cleavage-activating protein and the Site 1 proteas
7 l regulation of the mammalian proteins SCAP (SREBP cleavage activating protein) and HMG-CoA reductase
8 hrough their sterol-induced binding to Scap (SREBP cleavage-activating protein) and 3-hydroxy-3-methy
9  pathway, including a single SREBP (dSREBP), SREBP cleavage-activating protein (dSCAP), and the two p
10                                        SCAP (SREBP cleavage-activating protein) forms a complex with
11 Ps in the lung, we conditionally deleted the SREBP cleavage-activating protein gene, Scap, in respira
12 inding proteins (SREBPs) by binding to SCAP (SREBP cleavage-activating protein) in a sterol-regulated
13                                        SCAP (SREBP cleavage-activating protein) is a sterol-regulated
14 transgenic SREBP-1a, transgenic SREBP-2, and SREBP cleavage-activating protein knockout mice recently
15   Overexpression of either dominant-negative SREBP cleavage-activating protein or 25-hydroxycholester
16  endoplasmic reticulum-to-Golgi transport of SREBP cleavage-activating protein requires the actin-bas
17 erol levels are high, Insig proteins bind to SREBP cleavage-activating protein, retaining it in the E
18                                              SREBP cleavage activating protein (SCAP), a membrane-bou
19 yos injected with a morpholino to knock down Srebp cleavage activating protein (scap).
20 D and the putative sterol-sensing regions of SREBP cleavage-activating protein (SCAP) and 3-hydroxy-3
21 tein that binds the sterol-sensing domain of SREBP cleavage-activating protein (SCAP) and facilitates
22                           Mammalian proteins SREBP cleavage-activating protein (SCAP) and HMG-CoA red
23 sig's exert this action in the ER by binding SREBP cleavage-activating protein (SCAP) and preventing
24  through a mechanism that required an intact SREBP cleavage-activating protein (SCAP) pathway.
25                                              SREBP cleavage-activating protein (SCAP) stimulates the
26     Release of membrane-bound SREBP requires SREBP cleavage-activating protein (SCAP) to escort SREBP
27                         Sequence analysis of SREBP cleavage-activating protein (SCAP) transcripts fro
28  a proteolytic process that is stimulated by SREBP cleavage-activating protein (SCAP), a membrane pro
29 es by proteases whose activities depend upon SREBP cleavage-activating protein (SCAP), a polytopic en
30 clear SREBPs as a result of gene knockout of SREBP cleavage-activating protein (SCAP), a protein requ
31                 This response is mediated by SREBP cleavage-activating protein (SCAP), a regulatory p
32 lglutaryl coenzyme A (HMG-CoA) reductase and SREBP cleavage-activating protein (SCAP), and to the NPC
33 cells and elicits a conformational change in SREBP cleavage-activating protein (SCAP), as revealed by
34    VEGF-induced SREBP activation depended on SREBP cleavage-activating protein (SCAP), because knocki
35 c(-/-) mice was greater than in mice lacking SREBP cleavage-activating protein (SCAP), in which all n
36 evels are high, Insig proteins bind and trap SREBP cleavage-activating protein (SCAP), retaining it i
37 s to the membranous sterol-sensing domain of SREBP cleavage-activating protein (SCAP), retaining the
38                                       In the SREBP cleavage-activating protein (SCAP), sterols inhibi
39 erexpression of the sterol-sensing domain of SREBP cleavage-activating protein (SCAP), suggesting tha
40 , and -2) or a dominant positive form of the SREBP cleavage-activating protein (SCAP), which facilita
41 nt-binding proteins (SREBPs) is regulated by SREBP cleavage-activating protein (SCAP), which forms co
42 cently discovered as a specific inhibitor of SREBP cleavage-activating protein (SCAP), which is requi
43 ion cloning we have isolated a cDNA-encoding SREBP cleavage-activating protein (SCAP), which regulate
44  but is restored by increasing the levels of SREBP cleavage-activating protein (SCAP).
45 ite 1, due to mutations in the gene encoding SREBP cleavage-activating protein (SCAP).
46 with a polytopic membrane protein designated SREBP cleavage-activating protein (SCAP).
47 rane protein of 1276 amino acids, designated SREBP cleavage-activating protein (SCAP).
48 nt SREBP-1c by enhancing the affinity of the SREBP cleavage-activating protein (SCAP).SREBP-1c comple
49 SREBP) pathway by preventing movement of the SREBP cleavage-activating protein (SCAP)/SREBP complex f
50 , sterol regulatory element-binding protein (SREBP) cleavage activating protein (SCAP), and SREBP-2.
51 : sterol regulatory element-binding protein (SREBP) cleavage-activating protein (SCAP) and 3-hydroxy-
52 f sterol regulatory element-binding protein (SREBP) cleavage-activating protein (SCAP) and consequent
53 f sterol regulatory element-binding protein (SREBP) cleavage-activating protein (SCAP), a sterol-sens
54 f sterol regulatory element-binding protein (SREBP) cleavage-activating protein (SCAP), an essential
55 s subsequently leads to the transport of the SREBP cleavage-activating protein.SREBP complex from the
56 lular sterol levels in mammalian cells in an SREBP cleavage-activating protein-stimulated fashion.

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