FOLDING INTERMEDIATES ARE INVOLVED IN GENETIC-DISEASES

被引：66

作者：

BYCHKOVA, VE ^{[1
]}

PTITSYN, OB ^{[1
]}

机构：

[1] NCI,MATH BIOL LAB,BETHESDA,MD 20892

来源：

FEBS LETTERS | 1995年 / 359卷 / 01期

关键词：

PROTEIN FOLDING; GENETIC DISEASE; MOLTEN GLOBULE STATE; MISLOCATION OF PROTEINS;

D O I：

10.1016/0014-5793(95)00004-S

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Recent experimental data show that some human genetic diseases are due to mutations in proteins which influence their trafficking and lead to retaining of proteins in the endoplasmic reticulum or their unproper processing. In this paper a hypothesis is proposed that these mutations are connected with an incomplete protein folding, blocking it at the stage of the kinetic molten globule or even earlier. If so, the specific drugs against these diseases may be ligands and other factors which facilitate the correct protein folding.

引用

页码：6 / 8

页数：3

共 35 条

[1] ACCILI D, 1992, J BIOL CHEM, V267, P586
[2] Amara J F, 1992, Trends Cell Biol, V2, P145, DOI 10.1016/0962-8924(92)90101-R
[3] Bychkova V.E., 1993, CHEMTRACTS BIOCH MOL, V4, P133
[4] THE MOLTEN GLOBULE STATE IS INVOLVED IN THE TRANSLOCATION OF PROTEINS ACROSS MEMBRANES
BYCHKOVA, VE
PAIN, RH
PTITSYN, OB
[J]. FEBS LETTERS, 1988, 238 (02) : 231 - 234
[5] CRYSTAL-STRUCTURE OF A P53 TUMOR-SUPPRESSOR DNA COMPLEX - UNDERSTANDING TUMORIGENIC MUTATIONS
CHO, YJ
GORINA, S
JEFFREY, PD
PAVLETICH, NP
[J]. SCIENCE, 1994, 265 (5170) : 346 - 355
[6] HIGH-RESOLUTION STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTIDIMENSIONAL NMR
CLORE, GM
OMICHINSKI, JG
SAKAGUCHI, K
ZAMBRANO, N
SAKAMOTO, H
APPELLA, E
GRONENBORN, AM
[J]. SCIENCE, 1994, 265 (5170) : 386 - 391
[7] CREIG S, 1985, J MOL BIOL, V185, P681
[8] PROCESSING OF MUTANT CYSTIC-FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR IS TEMPERATURE-SENSITIVE
DENNING, GM
ANDERSON, MP
AMARA, JF
MARSHALL, J
SMITH, AE
WELSH, MJ
[J]. NATURE, 1992, 358 (6389) : 761 - 764
[9] P53 - A GLIMPSE AT THE PUPPET BEHIND THE SHADOW PLAY
FRIEND, S
[J]. SCIENCE, 1994, 265 (5170) : 334 - 335
[10] TEMPERATURE-SENSITIVE MUTANTS BLOCKED IN THE FOLDING OR SUBUNIT ASSEMBLY OF THE BACTERIOPHAGE-P22 TAIL SPIKE PROTEIN .2. ACTIVE MUTANT PROTEINS MATURED AT 30-DEGREES-C
GOLDENBERG, DP
KING, J
[J]. JOURNAL OF MOLECULAR BIOLOGY, 1981, 145 (04) : 633 - 651

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