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1 SLRPs belong to the group of extracellular leucine-rich
2 SLRPs have been localized to most skeletal regions, with
4 osome 9q22-9q21.3 where asporin is part of a SLRP gene cluster that includes extracellular matrix pro
6 ic reticulum stress that results in abnormal SLRP synthesis and secretion, which ultimately affects s
11 ch as collagens, fibronectins, laminins, and SLRP family proteins, whereas genes involved in ECM degr
12 of MMPs to digest cross-linked collagen and SLRPs, a model reaction system using purified collagen t
14 esults suggest that the interactions between SLRPs and collagen caused by RFUVA protect both SLRPs an
20 Such activity implies a broader role for SLRP family members in regulating collagen cross-linking
22 subset of small leucine-rich glycoproteins (SLRPs) that may function downstream of Hh signaling in t
26 ily which is distinct from the other class I SLRPs since it possesses a unique stretch of aspartate r
33 Together, our data indicate that the novel SLRP CHADL is expressed in cartilaginous tissues, influe
35 his expanded list we describe a new class of SLRP sequences that could be representative of an ancest
38 These studies highlight the importance of SLRPs in maintaining periodontal homeostasis through reg
39 LRPs themselves and cross-linked polymers of SLRPs and collagen appear able to resist degradation.
41 emistry (IHC) revealed increased staining of SLRPs (asporin, lumican, and decorin) and dentin matrix
42 red: the small leucine-rich proteoglycans or SLRPs, pronounced "slurps, " and the modular proteoglyca
45 rast to the tissue distribution of the other SLRPs, DSPG3 is predominantly expressed in cartilage.
46 chromosomal locations of the newly predicted SLRP genes would support the large-scale genome or gene
47 ll leucine-rich repeat proteoglycan/protein (SLRP) family members, a novel gene, nephrocan (NPN), has
48 eins, including small leucine-rich proteins (SLRPs), but the regulatory mechanisms are not well under
51 ss I small leucine-rich repeat proteoglycan (SLRP) family which is distinct from the other class I SL
52 the small leucine-rich repeat proteoglycan (SLRP) family, including decorin, biglycan, fibromodulin,
53 n, the main small leucine-rich proteoglycan (SLRP) expressed and produced by osteoblasts, in the anti
55 ongs to the small leucine-rich proteoglycan (SLRP) gene family and is one of the major components of
56 Lumican, a small leucine rich proteoglycan (SLRP), is a component of extracellular matrix which also
57 Decorin, a small leucine-rich proteoglycan (SLRP), is involved in the pathophysiology of human conge
59 cine-rich repeat proteins and proteoglycans (SLRPs) form an important family of regulatory molecules
61 lagens and small leucine-rich proteoglycans (SLRPs) interact to produce the transparent corneal struc
62 re class I small leucine-rich proteoglycans (SLRPs) involved in regulation of collagen fibril and mat
63 e class of small leucine-rich proteoglycans (SLRPs) is a family of homologous proteoglycans harboring
66 While the small leucine rich proteoglycans (SLRPs), including decorin and lumican, have been studied
67 osylated, commercially available recombinant SLRPs, keratocan, lumican, mimecan, decorin, and biglyca
68 the extracellular small leucine-rich repeat (SLRP) proteoglycan and protein family attached to the ce
70 oteins in intestine development and suggests SLRPs as novel regulators of smooth muscle cell differen
71 ears that the majority of the introns in the SLRP genes were inserted after the differentiation of th
73 Taken together, NPN is a novel member of the SLRP family that may play important roles in kidney deve
75 re inserted after the differentiation of the SLRP genes from an ancestral gene that was most likely c
82 chanism underlying CSCD in which a truncated SLRP protein core is retained intracellularly, its accum
83 teractions of biglycan and fibromodulin, two SLRPs highly expressed in tendons and bones, were invest