Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :1.1210637 |
The purified p40 . p37 . p36 complex , like the five subunit RFC , contained DNA dependent ATPase activity that was stimulated by PCNA , preferentially bound to primed DNA templates , interacted with PCNA , and was capable of unloading PCNA from singly nicked circular DNA . 1.1210637^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.70201808 |
Addition of p 21 did not inhibit RFC dependent PCNA loading ; rather , p 21 formed a stable complex with PCNA on the DNA . 0.70201808^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.505873 |
The p 21 binding sites of PCNA , mapped by affinity measurement of the mutant forms , found to be located within a distinct structure of the PCNA monomer , overlap with RFC and pol delta interaction sites . 0.505873^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.55754059 |
These results are in keeping with a model in which surface exposed regions of PCNA interact with RFC and the subsequent loading of PCNA onto DNA orients the elongation complex in a manner essential for processive DNA synthesis . . 0.55754059^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :1.1570397 |
Interactions of yeast RFC with PCNA and DNA were studied by surface plasmon resonance . 1.1570397^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.6703939 |
An ATP mediated complex between RFC and DNA was not competent for binding PCNA , and the RFC . 0.6703939^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :1.4086752 |
PCNA can directly interact with RFC , pol delta , FEN 1 and DNA ligase 1 . 1.4086752^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.58225385 |
Here , we provide evidence for the physical interaction of hPoliota with proliferating cell nuclear antigen ( PCNA ) , and show that PCNA , together with replication factor C ( RFC ) and replication protein A ( RPA ) , stimulates the DNA synthetic activity of hPoliota . 0.58225385^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.85066993 |
The checkpoint protein complexes , Rad 9 Hus1 Rad 1 ( Rad 9 1 1 ) and Rad 17 RFCs2 5 ( Rad 17 RFC ) , have been predicted to function as novel clamp and clamp loader proteins , respectively , due to their amino acid sequence similarities with PCNA and RFC . 0.85066993^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
One such protein , replication factor C ( RFC ) , functions with the proliferating cell nuclear antigen ( PCNA ) , replication protein A ( RPA ) , and DNA polymerase delta to synthesize the leading strand at a replication fork . ^^^ RFC from S . cerevisiae was purified by its ability to stimulate yeast DNA polymerase delta on a primed single stranded DNA template in the presence of yeast PCNA and RPA . ^^^ By analogy with the phage T 4 and SV 40 DNA replication in vitro systems , the yeast RFC , PCNA , RPA , and DNA polymerase delta activities function together as a leading strand DNA replication complex . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
The ATPase function of RFC is activated by proliferating cell nuclear antigen . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
The large subunit of RFC ( RFC p 140 ) has been suggested to be associated with the 3 ' end of elongating DNA primer and to recruit proliferating cell nuclear antigen ( PCNA ) onto DNA polymerase delta . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Complete repair synthesis was achieved by combining these factors with DNA polymerase epsilon , RFC , PCNA , and DNA ligase 1 . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Nucleotide excision repair DNA synthesis by DNA polymerase epsilon in the presence of PCNA , RFC , and RPA . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Using these proteins , complete SV 40 DNA replication was reconstituted with only purified DNA replication factors : SV 40 large tumor antigen ( TAg ) , replication protein A ( RPA ) , DNA topoisomerases 1 and 2 , DNA polymerase alpha primase , replication factor C ( RFC ) , the proliferating cell nuclear antigen ( PCNA ) , DNA polymerase delta , maturation factor 1 ( MF 1 ) , and DNA ligase 1 . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Proliferating cell nuclear antigen is loaded onto DNA through the action of RFC in an ATP dependent reaction . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
RFC is required , along with the proliferating cell nuclear antigen and DNA polymerase delta , for the synthesis of the leading strand during DNA replication . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Human replication factor C ( RFC , also called activator 1 ) is a five subunit protein complex ( p 140 , p 40 , p 38 , p 37 , and p 36 ) required for proliferating cell nuclear antigen ( PCNA ) dependent processive DNA synthesis catalyzed by DNA polymerase delta or epsilon . ^^^ The purified baculovirus produced RFC appears to contain equimolar levels of each subunit and was shown to be functionally identical to its native counterpart in ( 1 ) supporting DNA polymerase delta catalyzed PCNA dependent DNA chain elongation ; ( 2 ) catalyzing DNA dependent ATP hydrolysis that was stimulated by PCNA and human single stranded DNA binding protein ; ( 3 ) binding preferentially to DNA primer ends ; and ( 4 ) catalytically loading PCNA onto singly nicked circular DNA and catalytically removing PCNA from these DNA molecules . . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
As a consequence of this disruption , the distributions of PCNA and the large subunit of the RFC complex , proteins required for the elongation phase of DNA replication , are altered such that they are found within the intranucleoplasmic lamin aggregates . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Replication factor C ( RFC ) and proliferating cell nuclear antigen ( PCNA ) are processivity factors for eukaryotic DNA polymerases delta and epsilon . ^^^ RFC contains multiple activities , including its ability to recognize and bind to a DNA primer end and load the ring shaped PCNA onto DNA in an ATP dependent reaction . ^^^ Deletion of the p 140 N terminal half , including the DNA ligase homology domain , resulted in the formation of an RFC complex with enhanced activity in replication and PCNA loading . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Importantly , the Pol 2 holoenzyme complex does not contain some factors previously reported as stoichiometric components of the holoenzyme complex , most notably the proteins which function in repair of damaged DNA , such as PCNA , RFC and RPA . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
This process , which is ATP dependent , is carried out by 1 ) recognition of the primer terminus by RFC ( ) binding to and disruption of the PCNA trimer , and then 3 ) topologically linking the PCNA to the DNA . ^^^ Like native RFC derived from 293 cells , recombinant RFC was found to support SV 40 DNA synthesis and polymerase delta DNA synthesis in vitro and to possess an ATPase activity that was highly stimulated by DNA and further augmented by PCNA . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Destabilized PCNA trimers suppress defective Rfc 1 proteins in vivo and in vitro . ^^^ Replication factor C ( RFC ) and the proliferating cell nuclear antigen ( PCNA ) are two essential DNA polymerase accessory proteins that are required for numerous aspects of DNA metabolism including DNA replication , DNA repair , and telomere metabolism . ^^^ RFC is the 5 subunit multiprotein complex that loads PCNA onto DNA at primer template junctions in an ATP dependent reaction . ^^^ Mutant Rfc 1 1 complexes exhibit in vitro DNA replication defects that are sensitive to ATP concentrations , and these defects can be suppressed by mutant PCNA proteins which contain substitutions that destabilize the homotrimeric sliding DNA clamp . . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
They were the single stranded DNA binding protein , replication protein A ( RFA ) , the 3 ' primer binding complex , replication factor C ( RFC ) , and proliferating cell nuclear antigen ( PCNA ) . ^^^ AAV DNA replication could be reconstituted with purified Rep 78 , RPA , RFC , and PCNA and a phosphocellulose chromatography fraction ( IIA ) that contained DNA polymerase activity . ^^^ As both RFC and PCNA are known to be accessory proteins for polymerase delta and epsilon , we attempted to reconstitute AAV DNA replication by substituting either purified polymerase delta or polymerase epsilon for fraction IIA . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Replication factor C ( RFC ) and proliferating cell nuclear antigen ( PCNA ) are processivity factors for eukaryotic DNA polymerases delta and epsilon . ^^^ RFC binds to a DNA primer end and loads PCNA onto DNA in an ATP dependent reaction . ^^^ A N terminal region of the small subunits , containing the RFC homology box 2 , plays a critical role in the function of these subunits , deletion of which reduces but does not abolish RFC activity in loading PCNA onto DNA and in supporting an RFC dependent replication reaction . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
The salt eluates were examined for the presence of both DNA replication proteins ( Pol alpha , delta , straightepsilon , PCNA , RFC , RFA , DNA ligase 1 , NDH 2 , Topo 1 and Topo 2 ) and cell cycle proteins ( Cyclins A , B 1 , D 1 , D 2 , D 3 , E , CDK 2 , CDK 4 , CDK 5 and p 21 ) by western blotting with specific antibodies . ^^^ The DNA replication proteins which bound to PCNA Sepharose included DNA polymerase delta and straightepsilon , PCNA , the 37 and 40 kDa subunits of RFC , the 70 kDa subunit of RPA , NDH 2 and topoisomerase 1 . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Addition of the sliding DNA clamp PCNA , the clamp loader RFC , and ATP caused a drastic 30 fold increase in translesion replication . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Deletion of the rfc 2 + gene from the chromosome is lethal but does not result in the checkpoint dependent cell cycle arrest seen in cells deleted for the gene encoding PCNA or for those genes encoding subunits of either Pol delta or Pol straightepsilon . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
The temperature sensitive cdc 24 mutant is effectively rescued by pcn 1 ( + ) , rfc 1 ( + ) ( a fission yeast homologue of RFC 1 ) , and hhp 1 ( + ) , which encode the proliferating cell nuclear antigen ( PCNA ) , the large subunit of replication factor C ( RFC ) , and a casein kinase 1 involved in DNA damage repair , respectively . ^^^ The Cdc 24 protein binds PCNA and RFC 1 in vivo , and the domains essential for Cdc 24 function and for RFC 1 and PCNA binding colocalize in the N terminal two thirds of the molecule . ^^^ In addition , cdc 24 ( + ) genetically interacts with the gene encoding the catalytic subunit of DNA polymerase epsilon , which is stimulated by PCNA and RFC , and with those encoding the fission yeast counterparts of Mcm 2 , Mcm 4 , and Mcm 10 . ^^^ These results indicate that Cdc 24 is an RFC and PCNA interacting factor required for DNA replication and might serve as a target for regulation . . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
The processivity cofactors PCNA and RFC are essential even to synthesize as little as 30 nucleotides following strand invasion . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
The clamp loader , replication factor C ( RFC ) , can reverse this mark by unloading PCNA from the replicated DNA . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
A number of other proteins have been implicated in MMR , including DNA polymerase delta , RPA ( replication protein A ) , PCNA ( proliferating cell nuclear antigen ) , RFC ( replication factor C ) , Exonuclease 1 , FEN 1 ( RAD 27 ) and the DNA polymerase delta and epsilon associated exonucleases . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
The stimulatory effect of PfuPCNA on the DNA synthesis was observed by using a circular DNA template without the clamp loader ( replication factor C [ RFC ] ) in both Pol 1 and Pol 2 reactions in contrast to the case of eukaryotic organisms , which are known to require the RFC to open the ring structure of PCNA prior to loading onto a circular DNA . ^^^ Because RFC homologs have been found in the archaeal genomes , they may permit more efficient stimulation of DNA synthesis by archaeal DNA polymerases in the presence of PCNA . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
An intimate association between PCNA and RFC1p , RFC2p , and RFC3p is suggested by the allele restricted suppression of 10 different pol 30 alleles by the RFC suppressors . ^^^ RFC 1 , RFC 2 , and RFC 3 encode three of the five subunits of the replication factor C complex , which is required to load PCNA onto DNA in reconstituted DNA replication reactions . ^^^ Biochemical analysis of the wild type and mutant PCNA and RFC 3 proteins shows that mutant RFC3p enhances the production of long DNA products in pol delta dependent DNA synthesis , which is consistent with an increase in processivity . . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Complete repair was achieved by including highly purified human DNA polymerase delta or epsilon , PCNA , RFC , and DNA ligase 1 in reaction mixtures , reconstituting adduct repair for the first time with recombinant incision factors and human replication proteins . . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Replication factor C ( RFC , also called activator 1 ) , in conjunction with proliferating cell nuclear antigen ( PCNA ) , is responsible for processive DNA synthesis catalyzed by the eukaryotic replicative DNA polymerases delta and epsilon . ^^^ Here we report the isolation and characterization of homologues of RFC and PCNA from the archaeon , Methanobacterium thermoautotrophicum DeltaH . ^^^ Although mthRFC differs in organization from its eukaryotic counterpart , it was shown to be functionally similar to eukaryotic RFC in : ( 1 ) catalyzing DNA dependent ATP hydrolysis ; ( 2 ) binding preferentially to DNA primer ends ; ( 3 ) loading mthPCNA onto singly nicked circular DNA ; and ( 4 ) supporting mthPolB catalyzed PCNA dependent DNA chain elongation . ^^^ The importance and roles of RFC and PCNA in M . thermoautotrophicum DeltaH replication are discussed . . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
The fidelity of Schizosaccharomyces pombe DNA polymerase delta was measured in the presence or absence of its processivity subunits , proliferating cell nuclear antigen ( PCNA ) sliding clamp and replication factor C ( RFC ) clamp loading complex , using a synthetic 30 mer primer / 100 mer template . ^^^ Processive synthesis occurred in the presence of PCNA , RFC , and Escherichia coli single strand DNA binding protein ( SSB ) and required the presence of ATP . `` Passive ' ' self loading of PCNA onto DNA takes place in the absence of RFC , in an ATP independent reaction , which was strongly inhibited by SSB . ^^^ The nucleotide substitution error rate for pol delta holoenzyme ( HE ) ( pol delta + PCNA + RFC ) was 4 . 6 10 10 ( 4 ) for T . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
In addition , DNA replication factor C ( RFC ) , a protein complex that facilitates the loading of PCNA onto DNA , is also part of BASC . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Likewise , Rad 17 homologs have extensive homology with replication factor C ( RFC ) subunits ( p 36 , p 37 , p 38 , p 40 , and p 140 ) , which form a clamp loader for PCNA . ^^^ Mutational analysis of hRad 1 and hRad 17 demonstrates that this interaction has properties similar to the interaction between RFC and PCNA , a well characterized clamp clamp loader pair . ^^^ Collectively , these data provide the first experimental evidence that hRad 17 interacts with the PCNA like proteins hRad 1 , hHus 1 , and hRad 9 in manner similar to the interaction between RFC and PCNA . . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Although the RFC complex consists of RFCS and RFCL in vivo , RFCS alone , together with PCNA , substantially enhanced the DNA synthesizing activity of P . furiosus DNA polymerase 1 in vitro . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
The dimeric ring shaped sliding clamp of E . coli DNA polymerase 3 ( beta subunit , homolog of eukaryotic PCNA ) is loaded onto DNA by the clamp loader gamma complex ( homolog of eukaryotic Replication Factor C , RFC ) . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
The gamma complex , an AAA+ ATPase , is the bacterial homolog of eukaryotic replication factor C ( RFC ) that loads the sliding clamp ( beta , homologous to PCNA ) onto DNA . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
These results showed that the three dimensional structures of archaral PCNA and RFC are actually similar enough to their eukaryotic counterparts to allow a molecular substitution between the two biological domains , albeit at a lower efficiency . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
The eukaryotic equivalents are the replication factor C ( RFC ) clamp loader and the proliferating cell nuclear antigen ( PCNA ) clamp . ^^^ The implications of these actions for the workings of the E . coli clamp loading machinery and for eukaryotic RFC and PCNA are discussed . . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Here , we report the activity of Sso DNA pol Y 1 encoded by the dbh gene of the archaeon Sulfolobus solfataricus is greatly enhanced by the presence of PCNA and replication factor C ( RFC ) . ^^^ Sso pol Y 1 per se was a distributive enzyme but a substantial increase in the processivity was observed on poly ( dA ) oligo ( dT ) in the presence of PCNA ( 039p or 048p ) and RFC . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
The eukaryotic DNA sliding clamp that keeps DNA polymerase engaged at a replication fork , called proliferating cell nuclear antigen ( PCNA ) , is loaded onto the 3 ' ends of primer DNA through its interaction with a heteropentameric protein complex called replication factor C ( RFC ) . ^^^ The ATPase activity of RFC is necessary for formation of a functional PCNA clamp . ^^^ We further observe that PCNA is held between the two fingers of RFC and propose that the RFC structure change we observe during ATP hydrolysis causes the attached PCNA to form its active ring like clamp on DNA . . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
In deduced amino acid sequences of both PCNA homologues , the motif L / I A P K / R , implicated in binding of PCNA with replication factor C ( RFC ) , was identified . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Replication factor C ( RFC ) and proliferating cell nuclear antigen ( PCNA ) are accessory proteins essential for processive DNA synthesis in the domain Eucarya . ^^^ The function of RFC is to load PCNA , a processivity factor of eukaryotic DNA polymerases delta and epsilon , onto primed DNA templates . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
All of the mutant RFC complexes were capable of interacting with PCNA . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
RESULTS : The replication factor C ( RFC ) is known as the loading factor of PCNA on to the DNA strand . ^^^ P . furiosus RFC ( PfuRFC ) has a PCNA binding motif ( PIP box ) at the C terminus of the large subunit ( RFCL ) . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Here , we provide evidence for the physical interaction of human Polkappa ( hPolkappa ) with proliferating cell nuclear antigen ( PCNA ) and show that PCNA , replication factor C ( RFC ) , and replication protein A ( RPA ) act cooperatively to stimulate the DNA synthesis activity of hPolkappa . ^^^ The efficiency ( 5 ( max ) / K ( m ) ) of correct nucleotide incorporation by hPolkappa is enhanced approximately 50 to 200 fold in the presence of PCNA , RFC , and RPA , and this increase in efficiency is achieved by a reduction in the apparent K ( m ) for the nucleotide . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Replication factor C ( RFC ) is the accessory protein required to load the proliferating cell nuclear antigen ( PCNA ) onto DNA in replication process . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
The checkpoint proteins hRad 9 , hHus 1 , and hRad 1 have limited homology to the replication processivity factor proliferating cell nuclear antigen ( PCNA ) , and hRad 17 has homology to replication factor C ( RFC ) . ^^^ Therefore , our results demonstrate structural similarity between the checkpoint Rad complexes and the PCNA and RFC replication factors and thus provide further support for models proposing analogous functions for these complexes . . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Replication factor C ( RFC ) is a pentameric complex of five distinct subunits that functions as a clamp loader , facilitating the loading of proliferating cell nuclear antigen ( PCNA ) onto DNA during replication and repair . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Accordingly , the unwinding mediated by NS 1 and RPA promoted processive leading strand synthesis catalyzed by recombinant human DNA polymerase delta , PCNA , and RFC , using the minimal left end origin cloned in a plasmid as a template . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Combining the modeled structures for each RFC subunit with known structural , biochemical , and genetic data , we propose detailed models of how two of the RFC subunits , RFC 1 and RFC 3 , interact with the C terminal regions of PCNA . ^^^ RFC 1 is predicted to bind PCNA similarly to the p 21 PCNA interaction , while the RFC 3 PCNA binding is proposed to be similar to the E . coli delta beta interaction . ^^^ Additional sequence and structure analysis , supported by experimental data , suggests that RFC 5 might be the third clamp loader subunit to bind the equivalent PCNA region . ^^^ We discuss functional implications stemming from the proposed model of the RFC 1 PCNA interaction and compare putative clamp interacting regions in RFC 1 and its paralogs , Rad 17 and Ctf 18 . ^^^ Based on the individual intermolecular interactions , we propose RFC and PCNA arrangement that places three RFC subunits in association with each of the three C terminal regions in PCNA . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Replication factor C ( RFC ) catalyzes assembly of circular proliferating cell nuclear antigen clamps around primed DNA , enabling processive synthesis by DNA polymerase during DNA replication and repair . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Monomeric yeast PCNA mutants are defective in interacting with and stimulating the ATPase activity of RFC . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Replication factor C from the hyperthermophilic archaeon Pyrococcus abyssi does not need ATP hydrolysis for clamp loading and contains a functionally conserved RFC PCNA binding domain . ^^^ Finally , ( 1 ) the PabRFC large fraction cross reacted with anti human RFC PCNA binding domain antibody , corroborating the conservation of the protein sequence , ( 2 ) the human PCNA stimulated the PabRFC complex ATPase activity in a DNA dependent way and ( 3 ) the PabRFC complex could load human PCNA onto primed single stranded circular DNA , suggesting that the PCNA binding domain of RFC has been functionally conserved during evolution . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Furthermore , by screening for synthetic dosage lethality , we have shown that overexpression of MGS 1 causes lethality in combination with mutations in genes that encode replication proteins such as DNA polymerase delta , RFC , PCNA and RPA . ^^^ Moreover , loss of MGS 1 function interferes with the ability of multicopy PCNA to suppress the replication defect of the rfc 5 1 mutant . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
RFC is a clamp loader , facilitating the addition and removal of proliferating cell nuclear antigen from DNA during replication and repair but can also interact directly with the retinoblastoma tumor suppressor protein and the transcription factor C / EBPalpha . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Additionally , unique subunit specific interactions between components of the clamp loader , RFC , suggest a model for clamp loading of PCNA . . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Rad 17 RFC and the 9 1 1 complex have been shown to be structurally similar to the replication factors , RFC clamp loader and proliferating cell nuclear antigen polymerase clamp , respectively . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
The findings that CTF7 / ECO1 , POL 30 ( PCNA ) , and CHL12 / CTF18 ( a replication factor C [ RFC ] homolog ) genetically interact provided the first evidence that the processes of cohesion establishment and DNA replication are intimately coupled a link now confirmed by other studies . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
This alternative RFC containing complex interacts with proliferating cell nuclear antigen but not with the Rad9 / Rad1 / Hus1 complex , a proliferating cell nuclear antigen like clamp involved in the DNA damage response . hCTF 18 preferentially binds chromatin during S phase , suggesting a role during replication . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
In eukaryotic DNA replication , replication factor C ( RFC ) acts as a `` clamp loader ' ' that loads PCNA onto a primed DNA template in an ATP dependent manner . ^^^ The site directed reduction of the negative charges at the center part of the RFCS complex affected the stability of the RFC PCNA interaction and reduced the clamp loading activity . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Elg 1 forms an alternative PCNA interacting RFC complex required to maintain genome stability . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Replication factor C ( RFC ) is a heteropentameric AAA+ protein clamp loader of the proliferating cell nuclear antigen ( PCNA ) processivity factor . ^^^ In this report , Saccharomyces cerevisiae RFC protomers are examined for their interaction with each other and PCNA . ^^^ Furthermore , the RFC ( 2 / 3 ) and RFC ( 3 / 4 ) subassemblies bind stably to PCNA , yet neither RFC 2 nor RFC 4 bind tightly to PCNA , indicating that RFC 3 forms a strong contact point to PCNA . ^^^ The RFC 1 subunit also binds PCNA tightly , and we identify two hydrophobic residues in RFC 1 that are important for this interaction . ^^^ Therefore , at least two subunits in RFC make strong contacts with PCNA , unlike the Escherichia coli gamma complex in which only one subunit makes strong contact with the beta clamp . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Unlike replication factor C ( RFC ) , which uses the 3 ' primer / template junction to recruit proliferating cell nuclear antigen ( PCNA ) , the Rad 17 Rfc2 5 complex can use both the 5 ' and the 3 ' primer / template junctions to recruit the Rad 9 Rad1 Hus 1 complex , and it shows a preference for gapped DNA structures . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
The heteropentamer replication factor C ( RFC ) loads during DNA replication the homotrimer proliferating cell nuclear antigen ( PCNA ) polymerase clamp onto DNA . ^^^ Sequence similarities suggest the biochemical functions of an RSR ( Rad 17 Rfc2 Rfc 3 Rfc4 Rfc 5 ) complex and an RHR heterotrimer ( Rad 1 Hus1 Rad 9 ) may be similar to that of RFC and PCNA , respectively . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Replication factor C ( RFC ) catalyzes the assembly of circular proliferating cell nuclear antigen ( PCNA ) clamps around primed DNA , enabling processive synthesis by DNA polymerase . ^^^ The DNA elongation rate of the family B DNA polymerase from T . kodakaraensis KOD 1 ( KOD DNA polymerase ) , which has the highest elongation rate in all thermostable DNA polymerases , was increased about 1 . 7 times , when T . kodakaraensis KOD 1 PCNA ( Tk PCNA ) and the Tk RFC at the equal molar ratio of KOD DNA polymerase were reacted with primed DNA . . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Both the five and seven subunit Ctf 18 RFC complexes bind to single stranded and primed DNAs and possess weak ATPase activity that is stimulated by the addition of primed DNA and proliferating cell nuclear antigen ( PCNA ) . ^^^ Consistent with these observations , both Ctf 18 RFC complexes substituted for the replicative RFC in the PCNA dependent DNA polymerase delta catalyzed DNA replication reaction . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Proliferative cell nuclear antigen ( PCNA ) expression demonstrated a weak inverse relationship between sample PCNA and DHFR or RFC expression , suggesting that DHFR and RFC expression may be markers for factors other than drug resistance . ^^^ |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Expression of RFC 2 and PCNA in different gestational trophoblastic diseases ] . ^^^ The aim of current study was to investigate the expression levels of RFC 2 and proliferating cell nuclear antigen ( PCNA ) in gestational trophoblastic diseases ( GTD ) and to explore the relationship of expressions of two proteins with GTD . ^^^ METHODS : The expression of RFC 2 and PCNA were detected with immunohistochemical method in 15 cases of normal villi , 38 cases of hydatidiform moles ( HM ) , 42 cases of invasive moles ( IM ) , and 18 cases of choriocarcinomas ( CC ) . ^^^ RESULTS : The expression of RFC 2 and PCNA were significantly increased in HM , IM , and CC than in normal villi ( P=0 . 000 for RFC 2 , P=0 . 004 for PCNA ) . ^^^ The RFC 2 expression was positively correlated with the PCNA expression ( P=0 . 000 ) . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Interactions between the clamp loader and the clamp have been proposed to mirror those of the replication clamp loader RFC and the sliding clamp proliferating cell nuclear antigen ( PCNA ) . ^^^ In that system , three ATP molecules bound to the Rfc 2 , Rfc 3 , and Rfc 4 subunits are necessary and sufficient for efficient loading of PCNA , whereas ATP binding to Rfc 1 is not required . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
The reconstituted human Chl 12 RFC complex functions as a second PCNA loader . ^^^ It has been shown that the human Chl 12 RFC complex , reconstituted with a baculovirus expression system , specifically interacts with human proliferating cell nuclear antigen ( PCNA ) . ^^^ The purified Chl 12 RFC complex is structurally indistinguishable from RFC , as shown by electron microscopy , and it exhibits DNA stimulated ATPase activity that is further enhanced by PCNA , and by DNA binding activity on specific primer / template DNA structures . ^^^ These results demonstrate that the human Chl 12 RFC complex is a second PCNA loader and that its roles in replication are clearly distinguishable from those of RFC . . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Here we report the crystal structure of the five protein clamp loader complex ( replication factor C , RFC ) of the yeast Saccharomyces cerevisiae , bound to the sliding clamp ( proliferating cell nuclear antigen , PCNA ) . ^^^ Tight interfacial coordination of the ATP analogue ATP gammaS by RFC results in a spiral arrangement of the ATPase domains of the clamp loader above the PCNA ring . ^^^ Placement of a model for primed DNA within the central hole of PCNA reveals a striking correspondence between the RFC spiral and the grooves of the DNA double helix . ^^^ This model , in which the clamp loader complex locks onto primed DNA in a screw cap like arrangement , provides a simple explanation for the process by which the engagement of primer template junctions by the RFC : PCNA complex results in ATP hydrolysis and release of the sliding clamp on DNA . . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Although RFC inhibited DNA joining by DNA ligase 1 , the addition of PCNA alleviated inhibition by RFC . ^^^ Together , these results provide a molecular explanation for the key in vivo role of the DNA ligase I / PCNA interaction and suggest that the joining of Okazaki fragments is coordinated by pairwise interactions among RFC , PCNA , and DNA ligase I . . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
DNA polymerase delta , RFC and PCNA are required for repair synthesis of large looped heteroduplexes in Saccharomyces cerevisiae . ^^^ Similar results were obtained with antisera to the clamp loader proteins Rfc 3 and Rfc 4 , and to PCNA , i . e . ^^^ Thus PCNA and RFC seem to act in LLR only during repair synthesis , in contrast to their roles at both pre and post excision steps of MMR . ^^^ These biochemical experiments support the idea that yeast polymerase delta , RFC and PCNA are required for large loop DNA repair synthesis . . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Replication Factor C ( RFC ) is required for the loading of Proliferating Cell Nuclear Antigen ( PCNA ) onto DNA during DNA replication , repair and recombination . ^^^ RFC 40 , the second subunit of the RFC complex , and PCNA have been shown to be overexpressed in gestational trophoblastic diseases . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
The PCNA RFC families of DNA clamps and clamp loaders . ^^^ Loading of PCNA onto DNA at template primer junctions is performed in an ATP dependent process by replication factor C ( RFC ) , a heteropentameric AAA+ protein complex consisting of the Rfc 1 , Rfc 2 , Rfc 3 , Rfc 4 , and Rfc 5 subunits . ^^^ Multiple stepwise ATP binding events to RFC are required to load PCNA onto primed DNA . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Here we report the three dimensional structure of an archaeal clamp loading complex ( RFC PCNA DNA ) determined by single particle EM . ^^^ The three dimensional structure of the complex , reconstituted in vitro using a nonhydrolyzable ATP analog , reveals two components , a closed ring and a horseshoe shaped element , which correspond to PCNA and RFC , respectively . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
While MutSalpha , EXOI , and RPA are sufficient to support hydrolysis directed by a 5 ' strand break , 3 ' directed excision also requires MutLalpha , PCNA , and RFC . ^^^ RFC and PCNA suppress EXOI mediated 5 ' to 3 ' hydrolysis when the nick that directs excision is located 3 ' to the mispair and activate 3 ' to 5 ' excision , which is dependent on loaded PCNA and apparently mediated by a cryptic EXOI 3 ' to 5 ' hydrolytic function . ^^^ By contrast , RFC and PCNA have only a limited effect on 5 ' to 3 ' excision directed by a 5 ' strand break . . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Three of these proteins Rad 9 , Hus 1 , and Rad 1 interact in a heterotrimeric complex ( dubbed the 9 1 1 complex ) , which resembles a PCNA like sliding clamp , whereas Rad 17 is part of a clamp loading complex that is related to the PCNA clamp loader , replication factor C ( RFC ) . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
In budding yeast cells lacking Asf 1 , the amounts of several DNA replication proteins , including replication factor C ( RFC ) , proliferating cell nuclear antigen ( PCNA ) , and DNA polymerase epsilon ( Pol epsilon ) , are reduced at stalled replication forks . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
The replication clamp PCNA is loaded around DNA by replication factor C ( RFC ) and functions in DNA replication and repair . ^^^ Ctf 18 RFC was also a weak loader of PCNA onto naked template primer DNA . ^^^ However , when the single stranded DNA template was coated by the yeast single stranded DNA binding protein replication protein A ( RPA ) but not by a mutant form of RPA or a heterologous single stranded DNA binding protein , both binding of Ctf 18 RFC to substrate DNA and loading of PCNA were strongly inhibited , and unloading predominated . ^^^ Neither yeast RFC itself nor two other related clamp loaders , containing either Rad 24 or Elg 1 , catalyzed significant unloading of PCNA . ^^^ The Dcc 1 and Ctf 8 subunits of Ctf 18 RFC , while required for establishing sister chromatid cohesion in vivo , did not function specifically in PCNA unloading in vitro , thereby separating the functionality of the Ctf 18 RFC complex into two distinct paths . . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Proliferating cell nuclear antigen loading onto DNA by replication factor C ( RFC ) is a key step in eukaryotic DNA replication and repair processes . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
The reconstituted system includes MutSalpha or MutSbeta , MutLalpha , RPA , EXO 1 , HMGB 1 , PCNA , RFC , polymerase delta , and ligase 1 . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Replication factor C ( RFC ) and proliferating cell nuclear antigen ( PCNA ) are accessory proteins essential for processive DNA synthesis . ^^^ The function of RFC is to load PCNA , a processivity factor of replicative DNA polymerases , onto primed DNA templates . ^^^ However , the region containing the basic cluster is important for the stable ternary ( RFC PCNA DNA ) complex formation . . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Bidirectional mismatch repair directed by a strand break located 3 ' or 5 ' to the mispair has been reconstituted using seven purified human activities : MutSalpha , MutLalpha , EXOI , replication protein A ( RPA ) , proliferating cell nuclear antigen ( PCNA ) , replication factor C ( RFC ) and DNA polymerase delta . ^^^ In addition to DNA polymerase delta , PCNA , RFC , and RPA , 5 ' directed repair depends on MutSalpha and EXOI , whereas 3 ' directed mismatch correction also requires MutLalpha . ^^^ RFC and PCNA dramatically activate polymerase delta mediated hydrolysis of a primer template . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
We show that human MutLalpha is a latent endonuclease that is activated in a mismatch , MutSalpha , RFC , PCNA , and ATP dependent manner . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
To better understand this central role in mutagenesis in vivo , here we report the fidelity of DNA synthesis in vitro by yeast pol zeta alone and with RFC , PCNA and RPA . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
In eukarya and archaea , the replication factor C ( RFC ) and the proliferating cell nuclear antigen ( PCNA ) play crucial roles as the clamp loader and the clamp , respectively . ^^^ Here , we report the electron microscopic structure of an archaeal RFC PCNA DNA complex at 12 A resolution . ^^^ This complex exhibits excellent fitting of each atomic structure of RFC , PCNA , and the primed DNA . ^^^ The PCNA ring retains an open conformation by extensive interactions with RFC , with a distorted spring washer like conformation . ^^^ The complex appears to represent the intermediate , where the PCNA ring is kept open before ATP hydrolysis by RFC . . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Loading of the circular PCNA onto duplex DNA requires the activity of a clamp loader [ replication factor C ( RFC ) ] complex and the energy derived from ATP hydrolysis . ^^^ The mechanistic and structural details regarding PCNA loading by the RFC complex are still developing . ^^^ In this study , we capture an open yeast PCNA clamp in a complex with RFC through fluorescence energy transfer experiments . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
The eukaryotic replication factor C ( RFC ) clamp loader is an AAA+ spiral shaped heteropentamer that opens and closes the circular proliferating cell nuclear antigen ( PCNA ) clamp processivity factor on DNA . ^^^ In this study , we examined the roles of individual RFC subunits in opening the PCNA clamp . ^^^ Interestingly , Rfc 1 , which occupies the position analogous to the delta clamp opening subunit in the Escherichia coli clamp loader , is not required to open PCNA . ^^^ The Rfc 5 subunit is required to open PCNA . ^^^ Rfc 5 is positioned opposite the PCNA interface from Rfc 1 , and therefore , its action with Rfc 2 in opening PCNA indicates that PCNA is opened from the opposite side of the interface that the E . coli delta wrench acts upon . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
A conformational change associated with nucleotide binding may relate to the opening of PCNA rings by RFC during the loading reaction . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
Overproduction and purification of RFC related clamp loaders and PCNA related clamps from Saccharomyces cerevisiae . ^^^ The replication clamp PCNA and its loader RFC ( Replication Factor C ) are central factors required for processive replication and coordinated DNA repair . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
We identified nine mutations that display synthetic lethality with pol 30 104 ; three mutations affected the structural gene for the large subunit of replication factor C ( rfc 1 ) , which loads PCNA onto DNA , and six mutations affected three members of the RAD 52 epistasis group for DNA recombinational repair ( rad 50 , rad 52 and rad 57 ) . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
These include genes encoding the anti apoptosis factor SURVIVIN , positive cell cycle regulators ( CDC 2 , CYCLIN B 1 , CYCLIN B 2 , CYCLIN G 1 , CHK 1 , BUB 3 , STK 6 , SKB 1 , CSE 1 L ) and chromosome replication proteins ( MCM 2 , MCM 3 , FEN 1 , RRM 2 , TOP2A , RFC 1 ) . ^^^ |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: P35251 and P12004 |
Pubmed |
SVM Score :0.0 |
NA |
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