1                                              FPLD-associated mutations cluster within a small surface

2                     One family with atypical FPLD harbored an R582H alteration in exon 11 of lamin A.

3  lamin A to SREBP1 was noticeably reduced by FPLD mutations.

4 cid substitutions at position 482 that cause FPLD.

5                            Mutations causing FPLD, in contrast to those causing muscle disorders, are

6                 We have localized a gene for FPLD to chromosome 1q21-q23, and it has recently been pr

7 roposed that nuclear lamin A/C is altered in FPLD, on the basis of a novel missense mutation (R482Q)

8                             All mutations in FPLD affect the globular C-terminal domain of the lamin

9              Familial partial lipodystrophy (FPLD), Dunnigan variety, is an autosomal dominant disord

10 d the other, familial partial lipodystrophy (FPLD), involves loss of subcutaneous adipose tissue.

11 ly linked to familial partial lipodystrophy (FPLD).

12 unnigan-type familial partial lipodystrophy (FPLD).

13 ystrophy and familial partial lipodystrophy (FPLD).

14                         The genetic basis of FPLD is unknown.

15 e expression and subcellular localization of FPLD lamin A mutants and found no abnormalities.

16 ns could not be detected in lamin A/C in one FPLD family in which there was linkage to chromosome 1q2

17                                          The FPLD mutations R482Q and R482W occurred on different hap

18  well-characterized pedigrees and mapped the FPLD locus to chromosome 1q21-22.

19 cation of the lamin A tail is reduced by two FPLD-causing mutations, G465D and K486N, and by single m

20 al partial lipodystrophy, Dunnigan variety, (FPLD, OMIM 308980) is an autosomal-dominant condition ch

21                 We examined 15 families with FPLD for mutations in lamin A/C.