PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10679025-2 2000 NTF2 has been shown to bind nuclear pore complex proteins and the GDP form of Ran in vitro. Guanosine Diphosphate 66-69 RAN, member RAS oncogene family Homo sapiens 78-81 10369786-7 1999 Ran-GDP was coupled to the sensor chip and reacted with RCC1 mutants to categorise them into different groups, demonstrating the usefulness of plasmon surface resonance in the study of complex multi-step kinetic processes. Guanosine Diphosphate 4-7 RAN, member RAS oncogene family Homo sapiens 0-3 9878368-0 1998 The structure of the Q69L mutant of GDP-Ran shows a major conformational change in the switch II loop that accounts for its failure to bind nuclear transport factor 2 (NTF2). Guanosine Diphosphate 36-39 RAN, member RAS oncogene family Homo sapiens 40-43 9889103-9 1998 We conclude that NTF2 functions as a transport receptor for Ran, permitting rapid entry into the nucleus where GTP-GDP exchange mediated by RCC1 [7] converts Ran into its GTP-bound state. Guanosine Diphosphate 115-118 RAN, member RAS oncogene family Homo sapiens 60-63 9889103-9 1998 We conclude that NTF2 functions as a transport receptor for Ran, permitting rapid entry into the nucleus where GTP-GDP exchange mediated by RCC1 [7] converts Ran into its GTP-bound state. Guanosine Diphosphate 115-118 RAN, member RAS oncogene family Homo sapiens 158-161 9843686-4 1998 In this study, we show that mammalian p10/NTF2 dramatically inhibits the dissociation of [3H]GDP from Ran and the binding of [35S]GTPgammaS to Ran following the dissociation of non-radioactive GDP by RCC1, the only known mammalian guanine nucleotide exchange factor for Ran (Ran-GEF) [7]. Guanosine Diphosphate 193-196 RAN, member RAS oncogene family Homo sapiens 143-146 9843686-7 1998 These results suggest that p10/NTF2 acts as a GDP dissociation inhibitor for Ran (Ran-GDI), thereby coordinating the Ran-dependent reactions that underlie nuclear protein import. Guanosine Diphosphate 46-49 RAN, member RAS oncogene family Homo sapiens 77-80 9843686-7 1998 These results suggest that p10/NTF2 acts as a GDP dissociation inhibitor for Ran (Ran-GDI), thereby coordinating the Ran-dependent reactions that underlie nuclear protein import. Guanosine Diphosphate 46-49 RAN, member RAS oncogene family Homo sapiens 82-85 9843686-7 1998 These results suggest that p10/NTF2 acts as a GDP dissociation inhibitor for Ran (Ran-GDI), thereby coordinating the Ran-dependent reactions that underlie nuclear protein import. Guanosine Diphosphate 46-49 RAN, member RAS oncogene family Homo sapiens 82-85 9857054-5 1998 We did, however, find that a pool of free GTP (or its structural equivalent) must be added, probably because the GDP Ran that is added must be converted to GTP Ran during the import process. Guanosine Diphosphate 113-116 RAN, member RAS oncogene family Homo sapiens 117-120 9843686-0 1998 Nuclear transport factor p10/NTF2 functions as a Ran-GDP dissociation inhibitor (Ran-GDI). Guanosine Diphosphate 53-56 RAN, member RAS oncogene family Homo sapiens 49-52 9843686-0 1998 Nuclear transport factor p10/NTF2 functions as a Ran-GDP dissociation inhibitor (Ran-GDI). Guanosine Diphosphate 53-56 RAN, member RAS oncogene family Homo sapiens 81-84 9843686-4 1998 In this study, we show that mammalian p10/NTF2 dramatically inhibits the dissociation of [3H]GDP from Ran and the binding of [35S]GTPgammaS to Ran following the dissociation of non-radioactive GDP by RCC1, the only known mammalian guanine nucleotide exchange factor for Ran (Ran-GEF) [7]. Guanosine Diphosphate 93-96 RAN, member RAS oncogene family Homo sapiens 102-105 9843686-4 1998 In this study, we show that mammalian p10/NTF2 dramatically inhibits the dissociation of [3H]GDP from Ran and the binding of [35S]GTPgammaS to Ran following the dissociation of non-radioactive GDP by RCC1, the only known mammalian guanine nucleotide exchange factor for Ran (Ran-GEF) [7]. Guanosine Diphosphate 193-196 RAN, member RAS oncogene family Homo sapiens 143-146 9843686-4 1998 In this study, we show that mammalian p10/NTF2 dramatically inhibits the dissociation of [3H]GDP from Ran and the binding of [35S]GTPgammaS to Ran following the dissociation of non-radioactive GDP by RCC1, the only known mammalian guanine nucleotide exchange factor for Ran (Ran-GEF) [7]. Guanosine Diphosphate 193-196 RAN, member RAS oncogene family Homo sapiens 143-146 9878368-2 1998 When the structure of GDP-RanQ69L from monoclinic crystals with P21 symmetry was compared with the structure of wild-type Ran obtained from monoclinic crystals, the Q69L mutant showed a large conformational change in residues 68-74, which are in the switch II region of the molecule which changes conformation in response to nucleotide state and which forms the major interaction interface with nuclear transport factor 2 (NTF2, sometimes called p10). Guanosine Diphosphate 22-25 RAN, member RAS oncogene family Homo sapiens 26-29 9878368-3 1998 This conformational change alters the positions of key residues such as Lys71, Phe72 and Arg76 that are crucial for the interaction of GDP-Ran with NTF2 and indeed, solution binding studies were unable to detect any interaction between NTF2 and GDP-RanQ69L under conditions where GDP-Ran bound effectively. Guanosine Diphosphate 135-138 RAN, member RAS oncogene family Homo sapiens 139-142 9878368-3 1998 This conformational change alters the positions of key residues such as Lys71, Phe72 and Arg76 that are crucial for the interaction of GDP-Ran with NTF2 and indeed, solution binding studies were unable to detect any interaction between NTF2 and GDP-RanQ69L under conditions where GDP-Ran bound effectively. Guanosine Diphosphate 245-248 RAN, member RAS oncogene family Homo sapiens 139-142 9878368-3 1998 This conformational change alters the positions of key residues such as Lys71, Phe72 and Arg76 that are crucial for the interaction of GDP-Ran with NTF2 and indeed, solution binding studies were unable to detect any interaction between NTF2 and GDP-RanQ69L under conditions where GDP-Ran bound effectively. Guanosine Diphosphate 245-248 RAN, member RAS oncogene family Homo sapiens 139-142 9878368-4 1998 This interaction between NTF2 and GDP-Ran is required for efficient nuclear protein import and may function between the docking and translocation steps of the pathway. Guanosine Diphosphate 34-37 RAN, member RAS oncogene family Homo sapiens 38-41 9533885-0 1998 Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran. Guanosine Diphosphate 93-96 RAN, member RAS oncogene family Homo sapiens 133-136 9640542-2 1998 Ran is thought to be primarily bound to GTP in the nucleus and to GDP in the cytoplasm, as a result of the assymetric distribution of factors that interact with Ran to promote guanine nucleotide exchange (in the nucleus) and GTP hydrolysis (in the cytoplasm). Guanosine Diphosphate 66-69 RAN, member RAS oncogene family Homo sapiens 0-3 9533885-2 1998 NTF2 binds GDP-Ran selectively and this interaction is important for efficient nuclear protein import in vivo. Guanosine Diphosphate 11-14 RAN, member RAS oncogene family Homo sapiens 15-18 9533885-3 1998 We have used X-ray crystallography to determine the structure of the macromolecular complex formed between GDP-Ran and nuclear transport factor 2 (NTF2) at 2.5 A resolution. Guanosine Diphosphate 107-110 RAN, member RAS oncogene family Homo sapiens 111-114 9398678-5 1997 T42A-Ran.GDP also retains the ability to bind p10/NTF2, a component of the nuclear import pathway. Guanosine Diphosphate 9-12 RAN, member RAS oncogene family Homo sapiens 5-8 9510255-4 1998 Biochemically, RCC1 is a guanine-nucleotide-exchange factor for the nuclear Ras homologue Ran; it increases the dissociation of Ran-bound GDP by 10(5)-fold. Guanosine Diphosphate 138-141 RAN, member RAS oncogene family Homo sapiens 90-93 9510255-4 1998 Biochemically, RCC1 is a guanine-nucleotide-exchange factor for the nuclear Ras homologue Ran; it increases the dissociation of Ran-bound GDP by 10(5)-fold. Guanosine Diphosphate 138-141 RAN, member RAS oncogene family Homo sapiens 128-131 9398678-4 1997 T42A-Ran binds guanine nucleotides as well as wild-type Ran and responds as well as wild-type Ran to GTP or GDP exchange stimulated by the Ran-specific guanine nucleotide exchange factor, RCC1. Guanosine Diphosphate 108-111 RAN, member RAS oncogene family Homo sapiens 5-8 9121474-3 1997 Using PRP20, encoding the Ran GTP/GDP exchange factor, we identified YRB1, previously identified as a protein able to interact with human Ran GTP/GDP exchange factor RCC1 in the two-hybrid system. Guanosine Diphosphate 34-37 RAN, member RAS oncogene family Homo sapiens 138-141 9261173-2 1997 Previous biochemical studies have shown that NTF2 binds directly to the GDP-bound form of Ran/TC4 and to proteins of the nuclear pore complex that contain phenylalanine-glycine repeats. Guanosine Diphosphate 72-75 RAN, member RAS oncogene family Homo sapiens 90-93 9261173-2 1997 Previous biochemical studies have shown that NTF2 binds directly to the GDP-bound form of Ran/TC4 and to proteins of the nuclear pore complex that contain phenylalanine-glycine repeats. Guanosine Diphosphate 72-75 RAN, member RAS oncogene family Homo sapiens 94-97 9201707-5 1997 The pore complex-binding domain overlaps the Ran-GTP- and Ran-GDP-binding domains on p97, but only Ran-GTP competes for docking in permeabilized cells. Guanosine Diphosphate 62-65 RAN, member RAS oncogene family Homo sapiens 58-61 9201707-5 1997 The pore complex-binding domain overlaps the Ran-GTP- and Ran-GDP-binding domains on p97, but only Ran-GTP competes for docking in permeabilized cells. Guanosine Diphosphate 62-65 RAN, member RAS oncogene family Homo sapiens 58-61 9315840-6 1997 Interestingly, the difference in affinity of RanBP1 for Ran.GDP was mostly due to a dramatic increase of the dissociation rate constant. Guanosine Diphosphate 60-63 RAN, member RAS oncogene family Homo sapiens 45-48 9315840-8 1997 Here, we show that RanBP1 binds RanDeltaC.mGppNHp with KD values around 10 microM, as is the case for its association with full-length Ran.GDP. Guanosine Diphosphate 139-142 RAN, member RAS oncogene family Homo sapiens 19-22 9121474-2 1997 We employed the two-hybrid method to identify proteins interacting with Ran and the Ran GTP/GDP exchange factor. Guanosine Diphosphate 92-95 RAN, member RAS oncogene family Homo sapiens 72-75 9121474-2 1997 We employed the two-hybrid method to identify proteins interacting with Ran and the Ran GTP/GDP exchange factor. Guanosine Diphosphate 92-95 RAN, member RAS oncogene family Homo sapiens 84-87 9121474-3 1997 Using PRP20, encoding the Ran GTP/GDP exchange factor, we identified YRB1, previously identified as a protein able to interact with human Ran GTP/GDP exchange factor RCC1 in the two-hybrid system. Guanosine Diphosphate 34-37 RAN, member RAS oncogene family Homo sapiens 26-29 9121474-3 1997 Using PRP20, encoding the Ran GTP/GDP exchange factor, we identified YRB1, previously identified as a protein able to interact with human Ran GTP/GDP exchange factor RCC1 in the two-hybrid system. Guanosine Diphosphate 146-149 RAN, member RAS oncogene family Homo sapiens 26-29 9121474-3 1997 Using PRP20, encoding the Ran GTP/GDP exchange factor, we identified YRB1, previously identified as a protein able to interact with human Ran GTP/GDP exchange factor RCC1 in the two-hybrid system. Guanosine Diphosphate 146-149 RAN, member RAS oncogene family Homo sapiens 138-141 8909533-7 1996 In solution binding assays, Ran-GTP bound p97 with high affinity, but the binding of Ran-GDP to p97 was undetectable. Guanosine Diphosphate 89-92 RAN, member RAS oncogene family Homo sapiens 85-88 9003787-6 1996 We further provide evidence that nuclear protein import requires Ran in the GDP form in the cytoplasm. Guanosine Diphosphate 76-79 RAN, member RAS oncogene family Homo sapiens 65-68 8978815-2 1996 A key regulator of the Ran GTP/GDP cycle is the 70-kD Ran-GTPase-activating protein RanGAP1. Guanosine Diphosphate 31-34 RAN, member RAS oncogene family Homo sapiens 23-26 8978815-2 1996 A key regulator of the Ran GTP/GDP cycle is the 70-kD Ran-GTPase-activating protein RanGAP1. Guanosine Diphosphate 31-34 RAN, member RAS oncogene family Homo sapiens 54-57 8909533-8 1996 The addition of RanBP1 with Ran-GDP or Ran-GTP increased the affinity of both forms of Ran for p97 to the same level. Guanosine Diphosphate 32-35 RAN, member RAS oncogene family Homo sapiens 16-19 8909533-8 1996 The addition of RanBP1 with Ran-GDP or Ran-GTP increased the affinity of both forms of Ran for p97 to the same level. Guanosine Diphosphate 32-35 RAN, member RAS oncogene family Homo sapiens 28-31 8909533-8 1996 The addition of RanBP1 with Ran-GDP or Ran-GTP increased the affinity of both forms of Ran for p97 to the same level. Guanosine Diphosphate 32-35 RAN, member RAS oncogene family Homo sapiens 28-31 8909533-12 1996 These results suggest that RanBP1 promotes both the docking and translocation steps in nuclear protein import by stabilizing the interaction of Ran-GDP with p97. Guanosine Diphosphate 148-151 RAN, member RAS oncogene family Homo sapiens 27-30 8923203-5 1996 Other experiments using dominant mutants of Ran that block its GTP/GDP cycle have suggested that Ran may have multiple roles. Guanosine Diphosphate 67-70 RAN, member RAS oncogene family Homo sapiens 44-47 8923203-5 1996 Other experiments using dominant mutants of Ran that block its GTP/GDP cycle have suggested that Ran may have multiple roles. Guanosine Diphosphate 67-70 RAN, member RAS oncogene family Homo sapiens 97-100 8889801-2 1996 RCC1 has no preference for GTP or GDP-bound Ran, so that GTP-Ran formation in vivo is regulated by relative concentrations of GTP/GDP and regulatory proteins interacting with RCC1, Ran, and RNA1. Guanosine Diphosphate 130-133 RAN, member RAS oncogene family Homo sapiens 61-64 8889801-2 1996 RCC1 has no preference for GTP or GDP-bound Ran, so that GTP-Ran formation in vivo is regulated by relative concentrations of GTP/GDP and regulatory proteins interacting with RCC1, Ran, and RNA1. Guanosine Diphosphate 130-133 RAN, member RAS oncogene family Homo sapiens 61-64 8755535-5 1996 By preloading recombinant Ran/TC4 with [gamma-32P]GTP or [3H]GDP, we show that the interactions with p97 and NTF2 are specific for the GTP- and GDP-bound forms, respectively. Guanosine Diphosphate 61-64 RAN, member RAS oncogene family Homo sapiens 26-29 8755535-5 1996 By preloading recombinant Ran/TC4 with [gamma-32P]GTP or [3H]GDP, we show that the interactions with p97 and NTF2 are specific for the GTP- and GDP-bound forms, respectively. Guanosine Diphosphate 61-64 RAN, member RAS oncogene family Homo sapiens 30-33 8755535-5 1996 By preloading recombinant Ran/TC4 with [gamma-32P]GTP or [3H]GDP, we show that the interactions with p97 and NTF2 are specific for the GTP- and GDP-bound forms, respectively. Guanosine Diphosphate 144-147 RAN, member RAS oncogene family Homo sapiens 26-29 8755535-5 1996 By preloading recombinant Ran/TC4 with [gamma-32P]GTP or [3H]GDP, we show that the interactions with p97 and NTF2 are specific for the GTP- and GDP-bound forms, respectively. Guanosine Diphosphate 144-147 RAN, member RAS oncogene family Homo sapiens 30-33 8755535-6 1996 These data together with previous studies lead us to suggest that the interaction of the GTP-bound form of Ran/TC4 with p97 is linked to an early step in the nuclear protein import pathway and that the association of the GDP-bound form of Ran/TC4 with NTF2 helps define vectorial transport. Guanosine Diphosphate 221-224 RAN, member RAS oncogene family Homo sapiens 107-110 8755535-6 1996 These data together with previous studies lead us to suggest that the interaction of the GTP-bound form of Ran/TC4 with p97 is linked to an early step in the nuclear protein import pathway and that the association of the GDP-bound form of Ran/TC4 with NTF2 helps define vectorial transport. Guanosine Diphosphate 221-224 RAN, member RAS oncogene family Homo sapiens 111-114 8755535-6 1996 These data together with previous studies lead us to suggest that the interaction of the GTP-bound form of Ran/TC4 with p97 is linked to an early step in the nuclear protein import pathway and that the association of the GDP-bound form of Ran/TC4 with NTF2 helps define vectorial transport. Guanosine Diphosphate 221-224 RAN, member RAS oncogene family Homo sapiens 239-242 7782302-0 1995 The C terminus of the nuclear RAN/TC4 GTPase stabilizes the GDP-bound state and mediates interactions with RCC1, RAN-GAP, and HTF9A/RANBP1. Guanosine Diphosphate 60-63 RAN, member RAS oncogene family Homo sapiens 30-33 8682210-4 1996 Proteins that interact with Ran in either the GDP-bound or the GTP-bound state coordinate transfer through the NPC. Guanosine Diphosphate 46-49 RAN, member RAS oncogene family Homo sapiens 28-31 8655589-12 1996 They also show that multiple types of Ran mutant exert dominant effects on this process, and that normal Ran function requires cycling between the GTP- and GDP-bound states of the protein. Guanosine Diphosphate 156-159 RAN, member RAS oncogene family Homo sapiens 105-108 7548002-5 1995 The affinities of RCC1 to Ran.GDP and Ran.GTP are similar (1.3 x 10(5) and 1.8 x 10(5) M-1, respectively) and are high enough to allow formation of the ternary complex under appropriate concentration conditions. Guanosine Diphosphate 30-33 RAN, member RAS oncogene family Homo sapiens 26-29 7548002-6 1995 In the absence of excess nucleotide and at low Ran concentrations, GDP (or GTP) can be efficiently displaced by excess RCC1 and the ternary complex can be produced. Guanosine Diphosphate 67-70 RAN, member RAS oncogene family Homo sapiens 47-50 7548002-7 1995 The affinities of both nucleotides (GDP or GTP) to Ran in the corresponding ternary complexes are reduced by orders of magnitude in comparison with the respective binary complexes. Guanosine Diphosphate 36-39 RAN, member RAS oncogene family Homo sapiens 51-54 7548002-9 1995 The quantitative results of the kinetic analysis suggest that the exchange reaction does not per se favor the formation of the Ran.GTP complex, but rather accelerates the formation of the equilibrium dictated by the relative affinities of Ran for GDP/GTP and the respective concentrations of the nucleotide in the cell. Guanosine Diphosphate 247-251 RAN, member RAS oncogene family Homo sapiens 239-242 7782302-0 1995 The C terminus of the nuclear RAN/TC4 GTPase stabilizes the GDP-bound state and mediates interactions with RCC1, RAN-GAP, and HTF9A/RANBP1. Guanosine Diphosphate 60-63 RAN, member RAS oncogene family Homo sapiens 34-37 7782302-0 1995 The C terminus of the nuclear RAN/TC4 GTPase stabilizes the GDP-bound state and mediates interactions with RCC1, RAN-GAP, and HTF9A/RANBP1. Guanosine Diphosphate 60-63 RAN, member RAS oncogene family Homo sapiens 113-116 7782302-5 1995 We demonstrate here that the -DEDDDL sequence stabilizes GDP binding to Ran, and that the domain is required for high affinity interaction with a Ran-binding protein, HTF9A/RanBP1. Guanosine Diphosphate 57-60 RAN, member RAS oncogene family Homo sapiens 72-75 7782302-5 1995 We demonstrate here that the -DEDDDL sequence stabilizes GDP binding to Ran, and that the domain is required for high affinity interaction with a Ran-binding protein, HTF9A/RanBP1. Guanosine Diphosphate 57-60 RAN, member RAS oncogene family Homo sapiens 146-149 7819259-6 1995 The Ran(T24N) mutant, which is analogous to the S17N mutant of p21ras, has decreased relative affinities for both GDP/GTP and favors GDP binding. Guanosine Diphosphate 114-117 RAN, member RAS oncogene family Homo sapiens 4-7 7885480-0 1995 Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form. Guanosine Diphosphate 64-67 RAN, member RAS oncogene family Homo sapiens 53-56 7885480-1 1995 The Ran proteins constitute a distinct branch of the superfamily of Ras-related GTP-binding proteins which function as molecular switches cycling between GTP-bound "on" and GDP-bound "off" states. Guanosine Diphosphate 173-176 RAN, member RAS oncogene family Homo sapiens 4-7 7885480-3 1995 We report here the crystal structure at 2.3 A resolution of human Ran (Mr 24K) complexed with GDP and Mg2+. Guanosine Diphosphate 94-97 RAN, member RAS oncogene family Homo sapiens 66-69 7891706-2 1995 Like other small GTPases, Ran appears to function as a switch: Ran-GTP and Ran-GDP levels are regulated both by guanine nucleotide exchange factors and GTPase activating proteins, and Ran-GTP and Ran-GDP interact differentially with one or more effectors. Guanosine Diphosphate 79-82 RAN, member RAS oncogene family Homo sapiens 26-29 7891706-2 1995 Like other small GTPases, Ran appears to function as a switch: Ran-GTP and Ran-GDP levels are regulated both by guanine nucleotide exchange factors and GTPase activating proteins, and Ran-GTP and Ran-GDP interact differentially with one or more effectors. Guanosine Diphosphate 200-203 RAN, member RAS oncogene family Homo sapiens 26-29 7891706-2 1995 Like other small GTPases, Ran appears to function as a switch: Ran-GTP and Ran-GDP levels are regulated both by guanine nucleotide exchange factors and GTPase activating proteins, and Ran-GTP and Ran-GDP interact differentially with one or more effectors. Guanosine Diphosphate 200-203 RAN, member RAS oncogene family Homo sapiens 63-66 7891706-2 1995 Like other small GTPases, Ran appears to function as a switch: Ran-GTP and Ran-GDP levels are regulated both by guanine nucleotide exchange factors and GTPase activating proteins, and Ran-GTP and Ran-GDP interact differentially with one or more effectors. Guanosine Diphosphate 200-203 RAN, member RAS oncogene family Homo sapiens 63-66 7891706-2 1995 Like other small GTPases, Ran appears to function as a switch: Ran-GTP and Ran-GDP levels are regulated both by guanine nucleotide exchange factors and GTPase activating proteins, and Ran-GTP and Ran-GDP interact differentially with one or more effectors. Guanosine Diphosphate 200-203 RAN, member RAS oncogene family Homo sapiens 63-66 7891706-2 1995 Like other small GTPases, Ran appears to function as a switch: Ran-GTP and Ran-GDP levels are regulated both by guanine nucleotide exchange factors and GTPase activating proteins, and Ran-GTP and Ran-GDP interact differentially with one or more effectors. Guanosine Diphosphate 200-203 RAN, member RAS oncogene family Homo sapiens 63-66 7819259-6 1995 The Ran(T24N) mutant, which is analogous to the S17N mutant of p21ras, has decreased relative affinities for both GDP/GTP and favors GDP binding. Guanosine Diphosphate 133-136 RAN, member RAS oncogene family Homo sapiens 4-7 8255297-2 1993 Ran has been proposed to undergo tightly controlled cycles of GTP binding and hydrolysis, to operate as a GTPase switch whose GTP- and GDP-bound forms interact differentially with regulators and effectors. Guanosine Diphosphate 135-138 RAN, member RAS oncogene family Homo sapiens 0-3 8026746-6 1994 Tt- and Tp-Ran, as well as other Ran/TC4, contain the four consensus regions involved in GTP/GDP-binding and GTPase activities. Guanosine Diphosphate 93-96 RAN, member RAS oncogene family Homo sapiens 11-14 8026746-6 1994 Tt- and Tp-Ran, as well as other Ran/TC4, contain the four consensus regions involved in GTP/GDP-binding and GTPase activities. Guanosine Diphosphate 93-96 RAN, member RAS oncogene family Homo sapiens 33-36 8026746-6 1994 Tt- and Tp-Ran, as well as other Ran/TC4, contain the four consensus regions involved in GTP/GDP-binding and GTPase activities. Guanosine Diphosphate 93-96 RAN, member RAS oncogene family Homo sapiens 37-40 1944575-6 1991 We have shown that this 25K protein has a sequence homologous to the translated reading frame of TC4, a cDNA found by screening a human teratocarcinoma cDNA library with oligonucleotides coding for a ras consensus sequence, and that the protein binds GDP and GTP. Guanosine Diphosphate 251-254 RAN, member RAS oncogene family Homo sapiens 97-100 32528950-2 2020 Like all the GTPases, Ran cycles between an active (GTP-bound) and inactive (GDP-bound) state. Guanosine Diphosphate 77-80 RAN, member RAS oncogene family Homo sapiens 22-25 33912945-3 2021 These include cargo-carrying importin and exportin receptors from the beta-karyopherin (Kapbeta) family and the small GTPase Ran, which switches between guanosine triphosphate (GTP)- and guanosine diphosphate (GDP)-bound forms to regulate cargo delivery and compartmentalization. Guanosine Diphosphate 187-208 RAN, member RAS oncogene family Homo sapiens 125-128 33912945-3 2021 These include cargo-carrying importin and exportin receptors from the beta-karyopherin (Kapbeta) family and the small GTPase Ran, which switches between guanosine triphosphate (GTP)- and guanosine diphosphate (GDP)-bound forms to regulate cargo delivery and compartmentalization. Guanosine Diphosphate 210-213 RAN, member RAS oncogene family Homo sapiens 125-128 25436539-1 2012 Abstract Like many other small GTPases, Ran functions in eukaryotic cells as a molecular switch that cycles between GTP- and GDP-bound forms. Guanosine Diphosphate 125-128 RAN, member RAS oncogene family Homo sapiens 40-43 31484720-0 2019 REV7 has a dynamic adaptor region to accommodate small GTPase RAN/Shigella IpaB ligands and its activity is regulated by RanGTP/GDP switch. Guanosine Diphosphate 128-131 RAN, member RAS oncogene family Homo sapiens 62-65 31484720-9 2019 Our structural and biochemical results further indicated that REV7 preferentially binds GTP-bound RAN, implying that a GTP/GDP-bound transition of RAN may serve as the molecular switch that controls REV7"s activity. Guanosine Diphosphate 123-126 RAN, member RAS oncogene family Homo sapiens 98-101 31484720-9 2019 Our structural and biochemical results further indicated that REV7 preferentially binds GTP-bound RAN, implying that a GTP/GDP-bound transition of RAN may serve as the molecular switch that controls REV7"s activity. Guanosine Diphosphate 123-126 RAN, member RAS oncogene family Homo sapiens 147-150 26304119-6 2015 In the nucleus of DRG neurons MYCBP2 co-localized with Ran and facilitated through its RCC1-like domain the GDP/GTP exchange of Ran. Guanosine Diphosphate 108-111 RAN, member RAS oncogene family Homo sapiens 128-131 24563355-3 2014 Like other GTPases, Ran relies on the cycling between GTP-bound and GDP-bound conformations to interact with effector proteins and regulate these processes. Guanosine Diphosphate 68-71 RAN, member RAS oncogene family Homo sapiens 20-23 23536659-3 2013 Exogenous GDP and GTP are inhibitory to L-Ran binding, but the guanine-nucleotide exchange factor RCC1 can relieve this inhibition. Guanosine Diphosphate 10-13 RAN, member RAS oncogene family Homo sapiens 42-45 29040603-5 2018 Our structure-guided functional analyses revealed that Mog1 competes with RCC1 for Ran binding in a GTP/GDP-dependent manner. Guanosine Diphosphate 104-107 RAN, member RAS oncogene family Homo sapiens 83-86 26124124-2 2015 An intracellular Ran GTP/Ran GDP gradient created by the distinct subcellular localization of its regulators RCC1 and RanGAP mediates many of its cellular effects. Guanosine Diphosphate 29-32 RAN, member RAS oncogene family Homo sapiens 17-20 26124124-2 2015 An intracellular Ran GTP/Ran GDP gradient created by the distinct subcellular localization of its regulators RCC1 and RanGAP mediates many of its cellular effects. Guanosine Diphosphate 29-32 RAN, member RAS oncogene family Homo sapiens 25-28 23878195-5 2013 As for most nuclear import cargoes, the driving force behind HIV-1 preintegration complex import is likely a gradient of the GDP- and GTP-bound forms of Ran, a small GTPase. Guanosine Diphosphate 125-128 RAN, member RAS oncogene family Homo sapiens 153-156 23160023-1 2013 BACKGROUND: The small GTPase Ran, Ras-related nuclear protein, plays important roles in multiple fundamental cellular functions such as nucleocytoplasmic transport, mitotic spindle assembly, and nuclear envelope formation, by binding to either GTP or GDP as a molecular switch. Guanosine Diphosphate 251-254 RAN, member RAS oncogene family Homo sapiens 29-32 25436539-2 2012 Through the proper modulation of the GTP/GDP cycle, Ran functions with a number of Ran-binding proteins to control a broad array of fundamental cellular functions, including nucleocytoplasmic transport, mitotic spindle assembly, and nuclear envelope and nuclear pore complex formation. Guanosine Diphosphate 41-44 RAN, member RAS oncogene family Homo sapiens 52-55 25436539-2 2012 Through the proper modulation of the GTP/GDP cycle, Ran functions with a number of Ran-binding proteins to control a broad array of fundamental cellular functions, including nucleocytoplasmic transport, mitotic spindle assembly, and nuclear envelope and nuclear pore complex formation. Guanosine Diphosphate 41-44 RAN, member RAS oncogene family Homo sapiens 83-86 20300488-6 2009 GTP-bound Ran is asymmetrically distributed in the nucleus, while GDP-bound Ran is predominantly cytoplasmic. Guanosine Diphosphate 66-69 RAN, member RAS oncogene family Homo sapiens 76-79 22880006-2 2012 Herein, we provide evidence for the first time that translocation of the mammalian NTF2 from the nucleus to the cytoplasm to collect Ran in the GDP form is subjected to regulation. Guanosine Diphosphate 144-147 RAN, member RAS oncogene family Homo sapiens 133-136 20609434-1 2010 Ran is a member of the superfamily of small GTPases, which cycle between a GTP-bound "on" and a GDP-bound "off" state. Guanosine Diphosphate 96-99 RAN, member RAS oncogene family Homo sapiens 0-3 20609434-3 2010 In order to maintain a gradient of excess Ran.GTP within the nucleoplasm and excess Ran.GDP within the cytoplasm, the hydrolysis of Ran.GTP in the nucleoplasm should be prevented, whereas in the cytoplasm, hydrolysis is catalyzed by Ran.GAP (GTPase-activating protein). Guanosine Diphosphate 88-91 RAN, member RAS oncogene family Homo sapiens 84-87 20609434-3 2010 In order to maintain a gradient of excess Ran.GTP within the nucleoplasm and excess Ran.GDP within the cytoplasm, the hydrolysis of Ran.GTP in the nucleoplasm should be prevented, whereas in the cytoplasm, hydrolysis is catalyzed by Ran.GAP (GTPase-activating protein). Guanosine Diphosphate 88-91 RAN, member RAS oncogene family Homo sapiens 84-87 20609434-3 2010 In order to maintain a gradient of excess Ran.GTP within the nucleoplasm and excess Ran.GDP within the cytoplasm, the hydrolysis of Ran.GTP in the nucleoplasm should be prevented, whereas in the cytoplasm, hydrolysis is catalyzed by Ran.GAP (GTPase-activating protein). Guanosine Diphosphate 88-91 RAN, member RAS oncogene family Homo sapiens 84-87 20300488-7 2009 Controlled by RanGEF and RanGAP, RanGTPase cycles between the GDP- and GTP-bound states enabling it to shuttle cargoes in an accurate spatial and temporal manner. Guanosine Diphosphate 62-65 RAN, member RAS oncogene family Homo sapiens 33-42 16248653-1 2005 A computational study was performed on the Mg(2+)-free conformations of the small guanine nucleotide-binding proteins (GNBPs): Ras, Rho, Rab, Arf, and Ran, which were complexed with GDP. Guanosine Diphosphate 182-185 RAN, member RAS oncogene family Homo sapiens 151-154 18708071-2 2008 In the nucleus, Ran is primarily in the guanosine 5"-triphosphate (GTP)-bound state, whereas in the cytoplasm, Ran is primarily guanosine 5"-diphosphate (GDP)-bound. Guanosine Diphosphate 128-152 RAN, member RAS oncogene family Homo sapiens 111-114 18708071-2 2008 In the nucleus, Ran is primarily in the guanosine 5"-triphosphate (GTP)-bound state, whereas in the cytoplasm, Ran is primarily guanosine 5"-diphosphate (GDP)-bound. Guanosine Diphosphate 154-157 RAN, member RAS oncogene family Homo sapiens 111-114 17433702-1 2007 Ran-binding proteins (RanBP) are a group of proteins that bind to Ran (Ras-related nuclear small G-protein) and thus control the GTP/GDP-bound states of the Ran and couple the Ran GTPase cycle to cellular processes. Guanosine Diphosphate 133-136 RAN, member RAS oncogene family Homo sapiens 0-3 17433702-1 2007 Ran-binding proteins (RanBP) are a group of proteins that bind to Ran (Ras-related nuclear small G-protein) and thus control the GTP/GDP-bound states of the Ran and couple the Ran GTPase cycle to cellular processes. Guanosine Diphosphate 133-136 RAN, member RAS oncogene family Homo sapiens 22-25 17433702-1 2007 Ran-binding proteins (RanBP) are a group of proteins that bind to Ran (Ras-related nuclear small G-protein) and thus control the GTP/GDP-bound states of the Ran and couple the Ran GTPase cycle to cellular processes. Guanosine Diphosphate 133-136 RAN, member RAS oncogene family Homo sapiens 71-106 17433702-1 2007 Ran-binding proteins (RanBP) are a group of proteins that bind to Ran (Ras-related nuclear small G-protein) and thus control the GTP/GDP-bound states of the Ran and couple the Ran GTPase cycle to cellular processes. Guanosine Diphosphate 133-136 RAN, member RAS oncogene family Homo sapiens 22-25 17433702-1 2007 Ran-binding proteins (RanBP) are a group of proteins that bind to Ran (Ras-related nuclear small G-protein) and thus control the GTP/GDP-bound states of the Ran and couple the Ran GTPase cycle to cellular processes. Guanosine Diphosphate 133-136 RAN, member RAS oncogene family Homo sapiens 22-25 17433702-4 2007 These proteins bound preferentially to the Ran-GTP over Ran-GDP conformation and subsequently stabilized its GTP-bound status. Guanosine Diphosphate 60-63 RAN, member RAS oncogene family Homo sapiens 43-46 17433702-4 2007 These proteins bound preferentially to the Ran-GTP over Ran-GDP conformation and subsequently stabilized its GTP-bound status. Guanosine Diphosphate 60-63 RAN, member RAS oncogene family Homo sapiens 56-59 18565325-5 2008 The constitutively GTP- or GDP-bound form of ARA24/Ran repressed the AR N-C interaction. Guanosine Diphosphate 27-30 RAN, member RAS oncogene family Homo sapiens 45-50 18565325-5 2008 The constitutively GTP- or GDP-bound form of ARA24/Ran repressed the AR N-C interaction. Guanosine Diphosphate 27-30 RAN, member RAS oncogene family Homo sapiens 51-54 18469014-2 2008 The cycling of Ran between its GTP- and GDP-bound forms is catalyzed by the chromatin-bound guanine nucleotide exchange factor RCC1 and the cytoplasmic Ran GTPase-activating protein RanGAP. Guanosine Diphosphate 40-43 RAN, member RAS oncogene family Homo sapiens 15-18 18469014-2 2008 The cycling of Ran between its GTP- and GDP-bound forms is catalyzed by the chromatin-bound guanine nucleotide exchange factor RCC1 and the cytoplasmic Ran GTPase-activating protein RanGAP. Guanosine Diphosphate 40-43 RAN, member RAS oncogene family Homo sapiens 152-155 15351280-1 2004 Ran is a small GTPase that cycles between a guanosine diphosphate (GDP)-bound form (RanGDP) and a guanosine triphosphate (GTP)-bound form (RanGTP) and plays important roles in nuclear transport and mitosis. Guanosine Diphosphate 44-65 RAN, member RAS oncogene family Homo sapiens 0-3 15807788-2 2005 In vertebrates, these functions are controlled by a three-dimensional gradient of Ran-GTP to Ran-GDP, established by the spatial separation of Ran GTPase-activating protein (RanGAP) and the Ran guanine nucleotide exchange factor RCC1. Guanosine Diphosphate 97-100 RAN, member RAS oncogene family Homo sapiens 82-85 15807788-2 2005 In vertebrates, these functions are controlled by a three-dimensional gradient of Ran-GTP to Ran-GDP, established by the spatial separation of Ran GTPase-activating protein (RanGAP) and the Ran guanine nucleotide exchange factor RCC1. Guanosine Diphosphate 97-100 RAN, member RAS oncogene family Homo sapiens 93-96 15807788-2 2005 In vertebrates, these functions are controlled by a three-dimensional gradient of Ran-GTP to Ran-GDP, established by the spatial separation of Ran GTPase-activating protein (RanGAP) and the Ran guanine nucleotide exchange factor RCC1. Guanosine Diphosphate 97-100 RAN, member RAS oncogene family Homo sapiens 93-96 15807788-2 2005 In vertebrates, these functions are controlled by a three-dimensional gradient of Ran-GTP to Ran-GDP, established by the spatial separation of Ran GTPase-activating protein (RanGAP) and the Ran guanine nucleotide exchange factor RCC1. Guanosine Diphosphate 97-100 RAN, member RAS oncogene family Homo sapiens 93-96 15454457-4 2004 As a model, we focused on the interaction between the nuclear transport effector, RanBP1, and two related complexes consisting of the nuclear import receptor, importin beta, and the GDP- or GppNHp-bound forms of the small GTPase, Ran. Guanosine Diphosphate 182-185 RAN, member RAS oncogene family Homo sapiens 82-85 15351280-1 2004 Ran is a small GTPase that cycles between a guanosine diphosphate (GDP)-bound form (RanGDP) and a guanosine triphosphate (GTP)-bound form (RanGTP) and plays important roles in nuclear transport and mitosis. Guanosine Diphosphate 67-70 RAN, member RAS oncogene family Homo sapiens 0-3 15155737-3 2004 Here, we identify a novel activity that stimulates release of GDP from Ran in the presence of NTF2. Guanosine Diphosphate 62-65 RAN, member RAS oncogene family Homo sapiens 71-74 11932251-5 2002 This interaction was stimulated by the addition of Ran; moreover, Ran.GDP, Ran.GTP, and Ran without nucleotide could all stimulate complex formation between RanBP3 and RCC1 even though binding of Ran.GDP to RanBP3 alone was undetectable. Guanosine Diphosphate 200-203 RAN, member RAS oncogene family Homo sapiens 66-69 12194828-6 2002 Either mislocalization of GFP-RCC1 by removal of the N-terminal region or the expression of dominant Ran mutants that perturb the GTP/GDP cycle causes defects in mitotic spindle morphology, including misalignment of chromosomes and abnormal numbers of spindle poles. Guanosine Diphosphate 134-137 RAN, member RAS oncogene family Homo sapiens 101-104 12034733-5 2002 Fluorescence resonance energy transfer (FRET) occurs efficiently between the green fluorescent protein (GFP) and Alexa546 for Ran x GDP and Ran x GTP, suggesting that the tail is tethered in both states. Guanosine Diphosphate 132-135 RAN, member RAS oncogene family Homo sapiens 126-129 12034733-11 2002 Nonetheless, a robust cytoplasmic FRET signal was detectable, which suggests that a significant fraction of cytoplasmic Ran.GDP may exist in a ternary complex with RanBP1 and importins. Guanosine Diphosphate 124-127 RAN, member RAS oncogene family Homo sapiens 120-123 11932251-5 2002 This interaction was stimulated by the addition of Ran; moreover, Ran.GDP, Ran.GTP, and Ran without nucleotide could all stimulate complex formation between RanBP3 and RCC1 even though binding of Ran.GDP to RanBP3 alone was undetectable. Guanosine Diphosphate 70-73 RAN, member RAS oncogene family Homo sapiens 51-54 11932251-5 2002 This interaction was stimulated by the addition of Ran; moreover, Ran.GDP, Ran.GTP, and Ran without nucleotide could all stimulate complex formation between RanBP3 and RCC1 even though binding of Ran.GDP to RanBP3 alone was undetectable. Guanosine Diphosphate 70-73 RAN, member RAS oncogene family Homo sapiens 66-69 11932251-5 2002 This interaction was stimulated by the addition of Ran; moreover, Ran.GDP, Ran.GTP, and Ran without nucleotide could all stimulate complex formation between RanBP3 and RCC1 even though binding of Ran.GDP to RanBP3 alone was undetectable. Guanosine Diphosphate 70-73 RAN, member RAS oncogene family Homo sapiens 66-69 11932251-5 2002 This interaction was stimulated by the addition of Ran; moreover, Ran.GDP, Ran.GTP, and Ran without nucleotide could all stimulate complex formation between RanBP3 and RCC1 even though binding of Ran.GDP to RanBP3 alone was undetectable. Guanosine Diphosphate 70-73 RAN, member RAS oncogene family Homo sapiens 66-69 11932251-5 2002 This interaction was stimulated by the addition of Ran; moreover, Ran.GDP, Ran.GTP, and Ran without nucleotide could all stimulate complex formation between RanBP3 and RCC1 even though binding of Ran.GDP to RanBP3 alone was undetectable. Guanosine Diphosphate 70-73 RAN, member RAS oncogene family Homo sapiens 66-69 11932251-5 2002 This interaction was stimulated by the addition of Ran; moreover, Ran.GDP, Ran.GTP, and Ran without nucleotide could all stimulate complex formation between RanBP3 and RCC1 even though binding of Ran.GDP to RanBP3 alone was undetectable. Guanosine Diphosphate 200-203 RAN, member RAS oncogene family Homo sapiens 51-54 11932251-5 2002 This interaction was stimulated by the addition of Ran; moreover, Ran.GDP, Ran.GTP, and Ran without nucleotide could all stimulate complex formation between RanBP3 and RCC1 even though binding of Ran.GDP to RanBP3 alone was undetectable. Guanosine Diphosphate 200-203 RAN, member RAS oncogene family Homo sapiens 66-69 11932251-5 2002 This interaction was stimulated by the addition of Ran; moreover, Ran.GDP, Ran.GTP, and Ran without nucleotide could all stimulate complex formation between RanBP3 and RCC1 even though binding of Ran.GDP to RanBP3 alone was undetectable. Guanosine Diphosphate 200-203 RAN, member RAS oncogene family Homo sapiens 66-69 11932251-5 2002 This interaction was stimulated by the addition of Ran; moreover, Ran.GDP, Ran.GTP, and Ran without nucleotide could all stimulate complex formation between RanBP3 and RCC1 even though binding of Ran.GDP to RanBP3 alone was undetectable. Guanosine Diphosphate 200-203 RAN, member RAS oncogene family Homo sapiens 66-69 11029654-5 2000 A small GTPase Ran ensures the directionality of nuclear transport by regulating the interaction between the receptors and their cargoes through its GTP/GDP cycle. Guanosine Diphosphate 153-156 RAN, member RAS oncogene family Homo sapiens 15-18 10995230-5 2000 We used biophysical assays based on fluorescence-labeled probes and on surface plasmon resonance to investigate the dynamic interplay of Ran in its GDP- and GTP-complexed states with RanBDis and with importin-beta. Guanosine Diphosphate 148-151 RAN, member RAS oncogene family Homo sapiens 137-140 11911364-4 2002 In either case, the Ran.GTP is then transported to the cytoplasm by the karyopherin, where it is hydrolyzed to Ran.GDP. Guanosine Diphosphate 115-118 RAN, member RAS oncogene family Homo sapiens 20-23 11911364-4 2002 In either case, the Ran.GTP is then transported to the cytoplasm by the karyopherin, where it is hydrolyzed to Ran.GDP. Guanosine Diphosphate 115-118 RAN, member RAS oncogene family Homo sapiens 111-114 11231159-6 2001 However, addition of antibodies to RCC1 and RanGAP1 shows that Ran-GDP must be converted to Ran-GTP by RCC1 before precursor vesicles are recruited, whereas GTP hydrolysis by Ran stimulated by RanGAP1 promotes vesicle recruitment and is necessary for vesicle fusion to form an intact envelope. Guanosine Diphosphate 67-70 RAN, member RAS oncogene family Homo sapiens 63-66 11231159-6 2001 However, addition of antibodies to RCC1 and RanGAP1 shows that Ran-GDP must be converted to Ran-GTP by RCC1 before precursor vesicles are recruited, whereas GTP hydrolysis by Ran stimulated by RanGAP1 promotes vesicle recruitment and is necessary for vesicle fusion to form an intact envelope. Guanosine Diphosphate 67-70 RAN, member RAS oncogene family Homo sapiens 63-66 11231159-7 2001 Thus, the GTP-GDP cycle of Ran controls both the recruitment of vesicles and their fusion to form NEs. Guanosine Diphosphate 14-17 RAN, member RAS oncogene family Homo sapiens 27-30 11099382-6 2000 In two of the four molecules of Sec4-GDP in the asymmetric unit of the Sec4-GDP crystals, the switch II region adopts a conformation similar to that seen in the structure of the small G protein Ran bound to GDP. Guanosine Diphosphate 37-40 RAN, member RAS oncogene family Homo sapiens 194-197