PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
12522103-4	2003	KIF1A colocalizes with liprin-alpha in various subcellular regions of neurons.	Clofibrate	23-29	kinesin family member 1A	Homo sapiens	0-5
25126531-2	2014	The developed method was validated and extended for application on human subjects to study drug interaction of atorvastatin (ATSV) and olmesartan (OLM) on levels of ALD.	Atorvastatin	111-123	kinesin family member 1A	Homo sapiens	125-129
23500491-4	2013	By combining our structure with previously solved KIF1A structures complexed with two ATP analogs, molecular snapshots during ATP binding reveal that the closure of the nucleotide-binding pocket during ATP binding is achieved by closure of the backdoor.	Adenosine Triphosphate	86-89	kinesin family member 1A	Homo sapiens	50-55
23500491-4	2013	By combining our structure with previously solved KIF1A structures complexed with two ATP analogs, molecular snapshots during ATP binding reveal that the closure of the nucleotide-binding pocket during ATP binding is achieved by closure of the backdoor.	Adenosine Triphosphate	126-129	kinesin family member 1A	Homo sapiens	50-55
23500491-4	2013	By combining our structure with previously solved KIF1A structures complexed with two ATP analogs, molecular snapshots during ATP binding reveal that the closure of the nucleotide-binding pocket during ATP binding is achieved by closure of the backdoor.	Adenosine Triphosphate	126-129	kinesin family member 1A	Homo sapiens	50-55
23776493-10	2013	Nevertheless, high glucose increased the number of fluorescent accumulations of KIF1A and synaptotagmin-1 and decreased KIF5B, SNAP-25 and synaptophysin immunoreactivity specifically in axons of hippocampal neurons.	Glucose	19-26	kinesin family member 1A	Homo sapiens	80-85
22857951-5	2012	Dcx specifically enhances binding of the ADP-bound Kif1a motor domain to MTs.	Adenosine Diphosphate	41-44	kinesin family member 1A	Homo sapiens	51-56
15286375-3	2004	We report crystal structures of monomeric kinesin KIF1A with three transition-state analogs: adenylyl imidodiphosphate (AMP-PNP), adenosine diphosphate (ADP)-vanadate, and ADP-AlFx (aluminofluoride complexes).	Adenylyl Imidodiphosphate	93-118	kinesin family member 1A	Homo sapiens	50-55
15286375-3	2004	We report crystal structures of monomeric kinesin KIF1A with three transition-state analogs: adenylyl imidodiphosphate (AMP-PNP), adenosine diphosphate (ADP)-vanadate, and ADP-AlFx (aluminofluoride complexes).	Adenylyl Imidodiphosphate	120-127	kinesin family member 1A	Homo sapiens	50-55
15286375-3	2004	We report crystal structures of monomeric kinesin KIF1A with three transition-state analogs: adenylyl imidodiphosphate (AMP-PNP), adenosine diphosphate (ADP)-vanadate, and ADP-AlFx (aluminofluoride complexes).	Adenosine Diphosphate	130-151	kinesin family member 1A	Homo sapiens	50-55
15286375-3	2004	We report crystal structures of monomeric kinesin KIF1A with three transition-state analogs: adenylyl imidodiphosphate (AMP-PNP), adenosine diphosphate (ADP)-vanadate, and ADP-AlFx (aluminofluoride complexes).	Adenosine Diphosphate	153-156	kinesin family member 1A	Homo sapiens	50-55
15286375-3	2004	We report crystal structures of monomeric kinesin KIF1A with three transition-state analogs: adenylyl imidodiphosphate (AMP-PNP), adenosine diphosphate (ADP)-vanadate, and ADP-AlFx (aluminofluoride complexes).	Vanadates	158-166	kinesin family member 1A	Homo sapiens	50-55
15286375-3	2004	We report crystal structures of monomeric kinesin KIF1A with three transition-state analogs: adenylyl imidodiphosphate (AMP-PNP), adenosine diphosphate (ADP)-vanadate, and ADP-AlFx (aluminofluoride complexes).	adp-alfx	172-180	kinesin family member 1A	Homo sapiens	50-55
15286375-3	2004	We report crystal structures of monomeric kinesin KIF1A with three transition-state analogs: adenylyl imidodiphosphate (AMP-PNP), adenosine diphosphate (ADP)-vanadate, and ADP-AlFx (aluminofluoride complexes).	aluminofluoride	182-197	kinesin family member 1A	Homo sapiens	50-55
12891363-5	2003	Here we show, by measuring its movement with an optical trapping system, that a single ATP hydrolysis triggers a single stepping movement of a single KIF1A monomer.	Adenosine Triphosphate	87-90	kinesin family member 1A	Homo sapiens	150-155
24032868-1	2013	KIF1A is a single-headed molecular motor that moves processively and unidirectionally along a microtubule by using the chemical energy released by hydrolyzing adenosine triphosphate (ATP) into adenosine diphosphate (ADP) and inorganic phosphate (P(i)).	Adenosine Triphosphate	159-181	kinesin family member 1A	Homo sapiens	0-5
24032868-1	2013	KIF1A is a single-headed molecular motor that moves processively and unidirectionally along a microtubule by using the chemical energy released by hydrolyzing adenosine triphosphate (ATP) into adenosine diphosphate (ADP) and inorganic phosphate (P(i)).	Adenosine Triphosphate	183-186	kinesin family member 1A	Homo sapiens	0-5
24032868-1	2013	KIF1A is a single-headed molecular motor that moves processively and unidirectionally along a microtubule by using the chemical energy released by hydrolyzing adenosine triphosphate (ATP) into adenosine diphosphate (ADP) and inorganic phosphate (P(i)).	Adenosine Diphosphate	193-214	kinesin family member 1A	Homo sapiens	0-5
24032868-1	2013	KIF1A is a single-headed molecular motor that moves processively and unidirectionally along a microtubule by using the chemical energy released by hydrolyzing adenosine triphosphate (ATP) into adenosine diphosphate (ADP) and inorganic phosphate (P(i)).	Adenosine Diphosphate	216-219	kinesin family member 1A	Homo sapiens	0-5
24032868-1	2013	KIF1A is a single-headed molecular motor that moves processively and unidirectionally along a microtubule by using the chemical energy released by hydrolyzing adenosine triphosphate (ATP) into adenosine diphosphate (ADP) and inorganic phosphate (P(i)).	Phosphates	225-244	kinesin family member 1A	Homo sapiens	0-5
23459019-5	2013	Based on the energy landscape view of proteins, for the first time, we conducted a set of molecular simulations of the truncated KIF1A movements over an ATP hydrolysis cycle and found a mechanism exhibiting and enhancing stochastic forward-biased movements in a similar way to those in experiments.	Adenosine Triphosphate	153-156	kinesin family member 1A	Homo sapiens	129-134
23459019-6	2013	First, simulating stand-alone KIF1A, we did not find any biased movements, while we found that KIF1A with a large friction cargo-analog attached to the C-terminus can generate clearly biased Brownian movements upon an ATP hydrolysis cycle.	Adenosine Triphosphate	218-221	kinesin family member 1A	Homo sapiens	95-100
21844601-7	2011	Furthermore, by combining single-molecule biophysics with structural biology such as cryo-electrom microscopy and X-ray crystallography, atomic structures of KIF1A motor protein of almost all states during ATP hydrolysis have been determined and a common mechanism of motility has been proposed.	Adenosine Triphosphate	206-209	kinesin family member 1A	Homo sapiens	158-163
18849981-0	2008	KIF1Bbeta- and KIF1A-mediated axonal transport of presynaptic regulator Rab3 occurs in a GTP-dependent manner through DENN/MADD.	Guanosine Triphosphate	89-92	kinesin family member 1A	Homo sapiens	15-20
18806800-2	2008	To gain insight into the structural basis of this process, we solved the atomic structures of kinesin superfamily protein-1A (KIF1A) during and after Mg(2+) release.	magnesium ion	150-156	kinesin family member 1A	Homo sapiens	94-124
18806800-2	2008	To gain insight into the structural basis of this process, we solved the atomic structures of kinesin superfamily protein-1A (KIF1A) during and after Mg(2+) release.	magnesium ion	150-156	kinesin family member 1A	Homo sapiens	126-131
18806800-3	2008	On the basis of new structural and mutagenesis data, we propose a model mechanism for microtubule activation of Mg-ADP release from KIF1A.	Adenosine Diphosphate	112-118	kinesin family member 1A	Homo sapiens	132-137
12522103-5	2003	KIF1A coaccumulates with liprin-alpha in ligated sciatic nerves.	Clofibrate	25-31	kinesin family member 1A	Homo sapiens	0-5
12015984-0	2002	Role of phosphatidylinositol(4,5)bisphosphate organization in membrane transport by the Unc104 kinesin motor.	Phosphatidylinositol 4,5-Diphosphate	8-45	kinesin family member 1A	Homo sapiens	88-94
12015984-3	2002	Through its PH domain, Unc104 can transport phosphatidylinositol(4,5)bisphosphate (PtdIns(4,5)P2)-containing liposomes with similar properties to native vesicles.	Phosphatidylinositol 4,5-Diphosphate	44-81	kinesin family member 1A	Homo sapiens	23-29
12015984-3	2002	Through its PH domain, Unc104 can transport phosphatidylinositol(4,5)bisphosphate (PtdIns(4,5)P2)-containing liposomes with similar properties to native vesicles.	Phosphatidylinositol 4,5-Diphosphate	83-96	kinesin family member 1A	Homo sapiens	23-29
12015984-4	2002	Interestingly, liposome movement by monomeric Unc104 motors shows a very steep dependence on PtdIns(4,5)P2 concentration (Hill coefficient of approximately 20), even though liposome binding is noncooperative.	Phosphatidylinositol 4,5-Diphosphate	93-106	kinesin family member 1A	Homo sapiens	46-52
12015984-5	2002	This switch-like transition for movement can be shifted to lower PtdIns(4,5)P2 concentrations by the addition of cholesterol/sphingomyelin or GM1 ganglioside/cholera toxin, conditions that produce raft-like behavior of Unc104 bound to lipid bilayers.	Phosphatidylinositol 4,5-Diphosphate	65-78	kinesin family member 1A	Homo sapiens	219-225
12015984-5	2002	This switch-like transition for movement can be shifted to lower PtdIns(4,5)P2 concentrations by the addition of cholesterol/sphingomyelin or GM1 ganglioside/cholera toxin, conditions that produce raft-like behavior of Unc104 bound to lipid bilayers.	Cholesterol	113-124	kinesin family member 1A	Homo sapiens	219-225
12015984-5	2002	This switch-like transition for movement can be shifted to lower PtdIns(4,5)P2 concentrations by the addition of cholesterol/sphingomyelin or GM1 ganglioside/cholera toxin, conditions that produce raft-like behavior of Unc104 bound to lipid bilayers.	Sphingomyelins	125-138	kinesin family member 1A	Homo sapiens	219-225
12015984-5	2002	This switch-like transition for movement can be shifted to lower PtdIns(4,5)P2 concentrations by the addition of cholesterol/sphingomyelin or GM1 ganglioside/cholera toxin, conditions that produce raft-like behavior of Unc104 bound to lipid bilayers.	G(M1) Ganglioside	142-145	kinesin family member 1A	Homo sapiens	219-225
12015984-6	2002	These studies suggest that clustering of Unc104 in PtdIns(4,5)P2-containing rafts provides a trigger for membrane transport.	Phosphatidylinositol 4,5-Diphosphate	51-64	kinesin family member 1A	Homo sapiens	41-47
33683823-6	2021	We found that lower oxygen and glucose concentrations enhance the expression of mesodermal (Brachyury, KIF1A) and ectodermal (Nestin, beta-Tubulin) markers.	Oxygen	20-26	kinesin family member 1A	Homo sapiens	103-108
11373668-5	2001	The conformational change observed between the ADP-bound and the ATP-like structures of the KIF1A catalytic core is modular, extends to all kinesins and is similar to the conformational change used by myosin motors and G proteins.	Adenosine Diphosphate	47-50	kinesin family member 1A	Homo sapiens	92-97
11373668-5	2001	The conformational change observed between the ADP-bound and the ATP-like structures of the KIF1A catalytic core is modular, extends to all kinesins and is similar to the conformational change used by myosin motors and G proteins.	Adenosine Triphosphate	65-68	kinesin family member 1A	Homo sapiens	92-97
11373668-6	2001	Docking of the ADP-bound and ATP-like crystallographic models of KIF1A into the corresponding cryo-electron microscopy maps suggests a rationale for the plus-end directional bias associated with the kinesin catalytic core.	Adenosine Diphosphate	15-18	kinesin family member 1A	Homo sapiens	65-70
11373668-6	2001	Docking of the ADP-bound and ATP-like crystallographic models of KIF1A into the corresponding cryo-electron microscopy maps suggests a rationale for the plus-end directional bias associated with the kinesin catalytic core.	Adenosine Triphosphate	29-32	kinesin family member 1A	Homo sapiens	65-70
10639132-3	2000	Here we demonstrate the nucleotide-dependent binding between the lysine-rich, highly positively charged loop 12 of the KIF1A motor domain (K-loop) and the glutamate-rich, highly negatively charged C-terminal region of tubulin (E-hook).	Lysine	65-71	kinesin family member 1A	Homo sapiens	119-124
10639132-3	2000	Here we demonstrate the nucleotide-dependent binding between the lysine-rich, highly positively charged loop 12 of the KIF1A motor domain (K-loop) and the glutamate-rich, highly negatively charged C-terminal region of tubulin (E-hook).	Glutamic Acid	155-164	kinesin family member 1A	Homo sapiens	119-124
34321916-3	2021	The relationship between KIF1A expression and prognosis was analyzed using Oncomine and Kaplan-Meier plotter tools.	oncomine	75-83	kinesin family member 1A	Homo sapiens	25-30
34321916-8	2021	GO and KEGG analysis showed KIF1A had a potential role in the biological process of ATP-dependent chromatin remodeling, transcription, DNA-templated cytolysis, positive regulation of T cell proliferation, positive regulation of transcription, DNA-templated via cell adhesion molecules (CAMs), primary immunodeficiency, oxidative phosphorylation, NF-kappa B signaling pathway, pathways in cancer and Wnt signaling pathway, and immune infiltrating cells.	Adenosine Triphosphate	84-87	kinesin family member 1A	Homo sapiens	28-33
11163131-3	2001	This surprising behavior for a monomeric motor depends upon a lysine-rich loop in KIF1A that binds to the negatively charged carboxyl terminus of tubulin and, in the context of motor processivity, compensates for the lack of a second motor domain on the KIF1A holoenzyme.	Lysine	62-68	kinesin family member 1A	Homo sapiens	82-87
11163131-3	2001	This surprising behavior for a monomeric motor depends upon a lysine-rich loop in KIF1A that binds to the negatively charged carboxyl terminus of tubulin and, in the context of motor processivity, compensates for the lack of a second motor domain on the KIF1A holoenzyme.	Lysine	62-68	kinesin family member 1A	Homo sapiens	254-259
33683823-6	2021	We found that lower oxygen and glucose concentrations enhance the expression of mesodermal (Brachyury, KIF1A) and ectodermal (Nestin, beta-Tubulin) markers.	Glucose	31-38	kinesin family member 1A	Homo sapiens	103-108
32652677-2	2020	Here we report one mutation-negative female with classic Rett syndrome (RTT) harboring a de novo heterozygous novel variant [NP_001230937.1:p.(Asp248Glu)] in the highly-conserved motor domain of KIF1A.	asp248glu	143-152	kinesin family member 1A	Homo sapiens	195-200
33082143-4	2020	We established that the KIF1A forward step is triggered by hydrolysis of ATP and not by ATP binding, meaning that KIF1A follows the same chemomechanical cycle as established for kinesin-1 and-2.	Adenosine Triphosphate	73-76	kinesin family member 1A	Homo sapiens	24-29
33082143-4	2020	We established that the KIF1A forward step is triggered by hydrolysis of ATP and not by ATP binding, meaning that KIF1A follows the same chemomechanical cycle as established for kinesin-1 and-2.	Adenosine Triphosphate	73-76	kinesin family member 1A	Homo sapiens	114-119
33082143-5	2020	The ATP-triggered half-site release rate of KIF1A was similar to the stepping rate, indicating that during stepping, rear-head detachment is an order of magnitude faster than in kinesin-1 and kinesin-2.	Adenosine Triphosphate	4-7	kinesin family member 1A	Homo sapiens	44-49
33082143-8	2020	Based on the measured run length and the relatively slow off-rate in ADP, we conclude that attachment of the tethered head is the rate limiting transition in the KIF1A stepping cycle.	Adenosine Diphosphate	69-72	kinesin family member 1A	Homo sapiens	162-167
33082143-9	2020	Thus, KIF1A"s activity can be explained by a fast rear head detachment rate, a rate-limiting step of tethered head attachment that follows ATP hydrolysis, and a relatively strong electrostatic interaction with the microtubule in the weakly-bound post-hydrolysis state.	Adenosine Triphosphate	139-142	kinesin family member 1A	Homo sapiens	6-11
32652677-3	2020	In addition, three individuals with severe neurodevelopmental disorder along with clinical features overlapping with KAND are also reported carrying de novo heterozygous novel [NP_001230937.1:p.(Cys92Arg) & p.(Pro305Leu)] or previously reported [NP_001230937.1:p.(Thr99Met)] variants in KIF1A.	cys92arg	195-203	kinesin family member 1A	Homo sapiens	287-292
32652677-3	2020	In addition, three individuals with severe neurodevelopmental disorder along with clinical features overlapping with KAND are also reported carrying de novo heterozygous novel [NP_001230937.1:p.(Cys92Arg) & p.(Pro305Leu)] or previously reported [NP_001230937.1:p.(Thr99Met)] variants in KIF1A.	thr99met	264-272	kinesin family member 1A	Homo sapiens	287-292
31813911-5	2020	This case suggests that alterations in this arginine at codon 13 might lead to a common clinical spectrum and further expand the genetic and clinical spectra associated with KIF1A mutations.	Arginine	44-52	kinesin family member 1A	Homo sapiens	174-179
29166604-5	2017	Phosphorylation of serine 135 of Syt4 by JNK steers DCV trafficking by destabilizing Syt4-Kif1A interaction, leading to a transition from microtubule-dependent DCV trafficking to capture at en passant presynaptic boutons by actin.	Serine	19-25	kinesin family member 1A	Homo sapiens	90-95
30612907-6	2019	A disease-causing mutation within KIF1A that reduces preferential binding to GDP- versus GTP-rich microtubules disrupts SVP delivery and reduces presynaptic release upon neuronal stimulation.	Guanosine Diphosphate	77-80	kinesin family member 1A	Homo sapiens	34-39
30612907-6	2019	A disease-causing mutation within KIF1A that reduces preferential binding to GDP- versus GTP-rich microtubules disrupts SVP delivery and reduces presynaptic release upon neuronal stimulation.	Guanosine Triphosphate	89-92	kinesin family member 1A	Homo sapiens	34-39
30612907-6	2019	A disease-causing mutation within KIF1A that reduces preferential binding to GDP- versus GTP-rich microtubules disrupts SVP delivery and reduces presynaptic release upon neuronal stimulation.	svp	120-123	kinesin family member 1A	Homo sapiens	34-39
30021165-4	2018	We showed that calcium, acting via CaM, enhances KIF1A binding to DCVs and increases vesicle motility.	Calcium	15-22	kinesin family member 1A	Homo sapiens	49-54
25585697-5	2015	Structural modeling of the predicted p.(Ser69Leu) amino acid change suggested that it impairs the stable binding of ATP to the KIF1A protein.	Adenosine Triphosphate	116-119	kinesin family member 1A	Homo sapiens	127-132
25773145-5	2015	METHODS: Bisulfite-treated DNA samples from 73 eligible patients were amplified by quantitative methylation-specific polymerase chain reaction (QMSP) targeting 6 genes (deleted in colorectal cancer [DCC], endothelin receptor type B [EDNRB], homeobox protein A9 [HOXA9], kinesin family member 1A [KIF1A], nidogen-2 [NID2], and N-methyl D-aspartate receptor subtype 2B [NR2B]).	hydrogen sulfite	9-18	kinesin family member 1A	Homo sapiens	270-294
25773145-5	2015	METHODS: Bisulfite-treated DNA samples from 73 eligible patients were amplified by quantitative methylation-specific polymerase chain reaction (QMSP) targeting 6 genes (deleted in colorectal cancer [DCC], endothelin receptor type B [EDNRB], homeobox protein A9 [HOXA9], kinesin family member 1A [KIF1A], nidogen-2 [NID2], and N-methyl D-aspartate receptor subtype 2B [NR2B]).	hydrogen sulfite	9-18	kinesin family member 1A	Homo sapiens	296-301
25684691-7	2015	These results suggest that KIF1A regulates affinity to MT by changing the flexibility of the helix alpha4 during the ATP hydrolysis process: the binding site becomes more flexible in the strong binding state than in the weak binding state.	Adenosine Triphosphate	117-120	kinesin family member 1A	Homo sapiens	27-32